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S-adenosyl-L-methionine + 4-demethylwyosine
S-adenosyl-L-homocysteine + isowyosine
S-adenosyl-L-methionine + 7-aminocarboxypropyl-demethylwyosine
S-adenosyl-L-homocysteine + wyosine
S-adenosyl-L-methionine + 7-[(3S)-(3-amino-3-carboxypropyl)]-4-demethylwyosine37 in tRNAPhe
S-adenosyl-L-homocysteine + 7-[(3S)-(3-amino-3-carboxypropyl)]wyosine37 in tRNAPhe
S-adenosyl-L-methionine + guanine36 in tRNALeu
S-adenosyl-L-homocysteine + N1-methylguanine36 in tRNALeu
S-adenosyl-L-methionine + guanine37 in Aquifex aeolicus tRNAArg(ACG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in Aquifex aeolicus tRNAArg(ACG)
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in Aquifex aeolicus tRNAArg(CCG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in Aquifex aeolicus tRNAArg(CCG)
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in Aquifex aeolicus tRNAGln(UUG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in Aquifex aeolicus tRNAGln(UUG)
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in Aquifex aeolicus tRNAHis(GUG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in Aquifex aeolicus tRNAHis(GUG)
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in Aquifex aeolicus tRNALeu(CAG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in Aquifex aeolicus tRNALeu(CAG)
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in Aquifex aeolicus tRNAPro(GGG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in Aquifex aeolicus tRNAPro(GGG)
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in elongator tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in elongator tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in Escherichia coli tRNA1Leu
S-adenosyl-L-homocysteine + N1-methylguanine37 in Escherichia coli tRNA1Leu
S-adenosyl-L-methionine + guanine37 in Escherichia coli tRNAPro
S-adenosyl-L-homocysteine + N1-methylguanine37 in Escherichia coli tRNAPro
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in Haloferax volcanii tRNACys(GCA)
S-adenosyl-L-homocysteine + N1-methylguanine37 in Haloferax volcanii tRNACys(GCA)
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in Haloferax volcanii tRNALeu(CAA)
S-adenosyl-L-homocysteine + N1-methylguanine37 in Haloferax volcanii tRNALeu(CAA)
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in Haloferax volcanii tRNATrp(CCA)
S-adenosyl-L-homocysteine + N1-methylguanine37 in Haloferax volcanii tRNATrp(CCA)
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in Haloferax volcanii tRNATyr(GUA)
S-adenosyl-L-homocysteine + N1-methylguanine37 in Haloferax volcanii tRNATyr(GUA)
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in human mitochondrial tRNAPro
S-adenosyl-L-homocysteine + N1-methylguanine37 in human mitochondrial tRNAPro
S-adenosyl-L-methionine + guanine37 in human mitochondrial tRNAPro possessing an A36G37 sequence
S-adenosyl-L-homocysteine + N1-methylguanine37 in human mitochondrial tRNAPro possessing an A36G37 sequence
-
-
-
?
S-adenosyl-L-methionine + guanine37 in in Escherichia coli tRNALeu(CAG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in in Escherichia coli tRNALeu(CAG)
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in Methanocaldococcus jannaschii tRNA(Cys)
S-adenosyl-L-homocysteine + N1-methylguanine37 in Methanocaldococcus jannaschii tRNA(Cys)
-
-
-
?
S-adenosyl-L-methionine + guanine37 in Methanocaldococcus jannaschii tRNAArg(UCG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in Methanocaldococcus jannaschii tRNAArg(UCG)
possessing the sequence G36G37
-
-
?
S-adenosyl-L-methionine + guanine37 in Methanocaldococcus jannaschii tRNACys
S-adenosyl-L-homocysteine + N1-methylguanine37 in Methanocaldococcus jannaschii tRNACys
-
-
-
?
S-adenosyl-L-methionine + guanine37 in Methanocaldococcus jannaschii tRNACys(GCA)
S-adenosyl-L-homocysteine + N1-methylguanine37 in Methanocaldococcus jannaschii tRNACys(GCA)
possessing the sequence A36G37. The enzyme is inactive with mutant forms of Methanocaldococcus jannaschii tRNACys(GCA) containing A37, C37, or U37
-
-
?
S-adenosyl-L-methionine + guanine37 in Methanocaldococcus jannaschii tRNAGlu(UUC)
S-adenosyl-L-homocysteine + N1-methylguanine37 in Methanocaldococcus jannaschii tRNAGlu(UUC)
possessing the sequence C36G37
-
-
?
S-adenosyl-L-methionine + guanine37 in Methanocaldococcus jannaschii tRNALeu(UCG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in Methanocaldococcus jannaschii tRNALeu(UCG)
possessing the sequence G36G37
-
-
?
S-adenosyl-L-methionine + guanine37 in Methanocaldococcus jannaschii tRNAPro
S-adenosyl-L-homocysteine + N1-methylguanine37 in Methanocaldococcus jannaschii tRNAPro
S-adenosyl-L-methionine + guanine37 in Methanocaldococcus jannaschii tRNAPro(GGG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in Methanocaldococcus jannaschii tRNAPro(GGG)
possessing the sequence G36G37
-
-
?
S-adenosyl-L-methionine + guanine37 in Methanocaldococcus jannaschii tRNAPro(UGG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in Methanocaldococcus jannaschii tRNAPro(UGG)
possessing the sequence G36G37
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
S-adenosyl-L-methionine + guanine37 in tRNAArg
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAArg
S-adenosyl-L-methionine + guanine37 in tRNAArgCCG
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAArgCCG
S-adenosyl-L-methionine + guanine37 in tRNAAsp(GUC)
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAAsp(GUC)
enzyme AtTrm5a can methylate Saccharomyces cerevisiae tRNAAsp(GUC) in vivo and in vitro
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNACys
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNACys
S-adenosyl-L-methionine + guanine37 in tRNACysGCA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNACysGCA
S-adenosyl-L-methionine + guanine37 in tRNAGlnCUG
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAGlnCUG
S-adenosyl-L-methionine + guanine37 in tRNAGlnG36A
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAGlnG36A
-
tRNA substrate from Thermotoga maritima
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAGlnG36C
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAGlnG36C
-
tRNA substrate from Thermotoga maritima
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAGlnG36U
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAGlnG36U
-
tRNA substrate from Thermotoga maritima
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAHis(GUG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAHis(GUG)
S-adenosyl-L-methionine + guanine37 in tRNAHisGUG
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAHisGUG
S-adenosyl-L-methionine + guanine37 in tRNAIleUaU
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAIleUaU
S-adenosyl-L-methionine + guanine37 in tRNALeu
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNALeu
S-adenosyl-L-methionine + guanine37 in tRNALeu(CAG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNALeu(CAG)
S-adenosyl-L-methionine + guanine37 in tRNALeu(GAC)
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNALeu(GAC)
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNALeu(GAG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNALeu(GAG)
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNALeu(UAG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNALeu(UAG)
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNALeuCAG
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNALeuCAG
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAPhe
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPhe
S-adenosyl-L-methionine + guanine37 in tRNAPro
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPro
S-adenosyl-L-methionine + guanine37 in tRNAPro(CGG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPro(CGG)
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAPro(GGG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPro(GGG)
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAPro(UGG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPro(UGG)
S-adenosyl-L-methionine + guanine37 in tRNAProAGG
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAProAGG
-
-
-
?
S-adenosyl-L-methionine + guanine37 in yeast tRNA(Asp) possessing a G36G37 sequence
S-adenosyl-L-homocysteine + N1-methylguanine37 in yeast tRNA(Asp) possessing a G36G37 sequence
-
-
-
?
S-adenosyl-L-methionine + guanine37 in yeast tRNAAsp possessing a C36G37 sequence
S-adenosyl-L-homocysteine + N1-methylguanine37 in yeast tRNAAsp possessing a C36G37 sequence
-
-
-
?
S-adenosyl-L-methionine + guanine37 in yeast tRNAAsp possessing a G36G37 sequence
S-adenosyl-L-homocysteine + N1-methylguanine37 in yeast tRNAAsp possessing a G36G37 sequence
S-adenosyl-L-methionine + guanine37 in yeast tRNAAsp possessing an A36G37 sequence
S-adenosyl-L-homocysteine + N1-methylguanine37 in yeast tRNA(Asp) possessing an A36G37 sequence
-
-
-
?
S-adenosyl-L-methionine + guanine37 in yeast tRNAAsp possessing an A36G37 sequence
S-adenosyl-L-homocysteine + N1-methylguanine37 in yeast tRNAAsp possessing an A36G37 sequence
-
-
-
?
S-adenosyl-L-methionine + guanine37 in yeast tRNAAsp possessing an U36G37 sequence
S-adenosyl-L-homocysteine + N1-methylguanine37 in yeast tRNAAsp possessing an U36G37 sequence
-
-
-
?
S-adenosyl-L-methionine + guanine37 in yeast tRNAPhe possessing an A36G37 sequence
S-adenosyl-L-homocysteine + N1-methylguanine37 in yeast tRNAPhe possessing an A36G37 sequence
-
-
-
?
S-adenosyl-L-methionine + guanine37 in yeast tRNAPhe(GAA)
S-adenosyl-L-homocysteine + N1-methylguanine37 in yeast tRNAPhe(GAA)
-
-
-
-
?
S-adenosyl-L-methionine + inosine37 in yeast tRNAAsp possessing a G36I37 sequence
S-adenosyl-L-homocysteine + N1-methylinosine37 in yeast tRNAAsp possessing a G36I37 sequence
-
-
-
?
S-adenosyl-L-methionine + wyosine37 in tRNAPhe
S-adenosyl-L-homocysteine + N1-methylwyosine37 in tRNAPhe
additional information
?
-
S-adenosyl-L-methionine + 4-demethylwyosine
S-adenosyl-L-homocysteine + isowyosine
-
-
-
?
S-adenosyl-L-methionine + 4-demethylwyosine
S-adenosyl-L-homocysteine + isowyosine
i.e. im-G14, activity of EC 2.1.1.282
-
-
?
S-adenosyl-L-methionine + 4-demethylwyosine
S-adenosyl-L-homocysteine + isowyosine
-
-
-
?
S-adenosyl-L-methionine + 4-demethylwyosine
S-adenosyl-L-homocysteine + isowyosine
i.e. im-G14, activity of EC 2.1.1.282
-
-
?
S-adenosyl-L-methionine + 4-demethylwyosine
S-adenosyl-L-homocysteine + isowyosine
-
-
-
?
S-adenosyl-L-methionine + 4-demethylwyosine
S-adenosyl-L-homocysteine + isowyosine
i.e. im-G14, activity of EC 2.1.1.282
-
-
?
S-adenosyl-L-methionine + 7-aminocarboxypropyl-demethylwyosine
S-adenosyl-L-homocysteine + wyosine
-
-
-
?
S-adenosyl-L-methionine + 7-aminocarboxypropyl-demethylwyosine
S-adenosyl-L-homocysteine + wyosine
i.e. yW-86, activity of EC 2.1.1.228
-
-
?
S-adenosyl-L-methionine + 7-aminocarboxypropyl-demethylwyosine
S-adenosyl-L-homocysteine + wyosine
-
-
-
?
S-adenosyl-L-methionine + 7-aminocarboxypropyl-demethylwyosine
S-adenosyl-L-homocysteine + wyosine
i.e. yW-86, activity of EC 2.1.1.228
-
-
?
S-adenosyl-L-methionine + 7-aminocarboxypropyl-demethylwyosine
S-adenosyl-L-homocysteine + wyosine
-
-
-
?
S-adenosyl-L-methionine + 7-[(3S)-(3-amino-3-carboxypropyl)]-4-demethylwyosine37 in tRNAPhe
S-adenosyl-L-homocysteine + 7-[(3S)-(3-amino-3-carboxypropyl)]wyosine37 in tRNAPhe
-
-
-
?
S-adenosyl-L-methionine + 7-[(3S)-(3-amino-3-carboxypropyl)]-4-demethylwyosine37 in tRNAPhe
S-adenosyl-L-homocysteine + 7-[(3S)-(3-amino-3-carboxypropyl)]wyosine37 in tRNAPhe
-
-
-
?
S-adenosyl-L-methionine + guanine36 in tRNALeu
S-adenosyl-L-homocysteine + N1-methylguanine36 in tRNALeu
-
G36-substituted tRNA substrate Escherichia coli tRNALeu, TrmD shows a 90fold reduced catalytic efficiency, discrimination between the two sequences of G36 and G37
-
-
?
S-adenosyl-L-methionine + guanine36 in tRNALeu
S-adenosyl-L-homocysteine + N1-methylguanine36 in tRNALeu
-
G36-substituted tRNA substrate Escherichia coli tRNALeu, Trm5 shows a lack of discrimination between the two sequences of G36 and G37
-
-
?
S-adenosyl-L-methionine + guanine37 in Escherichia coli tRNA1Leu
S-adenosyl-L-homocysteine + N1-methylguanine37 in Escherichia coli tRNA1Leu
-
-
-
?
S-adenosyl-L-methionine + guanine37 in Escherichia coli tRNA1Leu
S-adenosyl-L-homocysteine + N1-methylguanine37 in Escherichia coli tRNA1Leu
-
-
-
?
S-adenosyl-L-methionine + guanine37 in human mitochondrial tRNAPro
S-adenosyl-L-homocysteine + N1-methylguanine37 in human mitochondrial tRNAPro
-
-
-
?
S-adenosyl-L-methionine + guanine37 in human mitochondrial tRNAPro
S-adenosyl-L-homocysteine + N1-methylguanine37 in human mitochondrial tRNAPro
-
-
-
?
S-adenosyl-L-methionine + guanine37 in Methanocaldococcus jannaschii tRNAPro
S-adenosyl-L-homocysteine + N1-methylguanine37 in Methanocaldococcus jannaschii tRNAPro
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in Methanocaldococcus jannaschii tRNAPro
S-adenosyl-L-homocysteine + N1-methylguanine37 in Methanocaldococcus jannaschii tRNAPro
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
the enzyme methylates tRNA transcripts possessing an A36G37 sequence as well as tRNA transcripts possessing a G36G37 sequence. tRNA transcripts possessing pyrimidine36G37 are not methylated at all. The modified nucleoside and the position in yeast tRNA(Phe) transcript are confirmed by LC/MS. Nine truncated tRNA molecules are tested to clarify the additional recognition site. The TrmD protein efficiently methylates the micro helix corresponding to the anti-codon arm. Because the disruption of the anti-codon stem causes the complete loss of the methyl group acceptance activity, the anti-codon stem is essential for the recognition. The existence of the D-arm structure inhibits the activity
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
methylates the N1 position of guanosine 37 (G37) in selected tRNA transcripts
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
substrate binding stoichiometry to TrmD, dissociation constants, overview
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
TrmD recognizes N1 and O6 of G37 and the exocyclic 2-amino group of G37 is important for TrmD, also TrmD requires G36 for synthesis of m1G37
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
the pH-activity profile indicates one proton transfer during the TrmD reaction
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
TrmD catalyzes the N1-methylguanosine (m1G) modification at position 37 in tRNAs with the 36GG37 sequence, using S-adenosyl-L-methionine as the methyl donor
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
TrmD catalyzes the N1-methylguanosine (m1G) modification at position 37 in tRNAs with the 36GG37 sequence, using S-adenosyl-L-methionine as the methyl donor
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
methylates the N1 position of guanosine 37 (G37) in selected tRNA transcripts
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
tight binding of Trm5 to products
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
Trm5 recognizes N1 and O6 of G37, but the exocyclic 2-amino group of G37 is dispensable for Trm5. Trm5 does not require G36
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
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?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
Trm5p is responsible for m1G37 methylation of mitochondrial and cytoplasmic tRNAs
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
methyltransferase activity with tRNA isolated from a DELTAtrm5 mutant strain, as well as with a synthetic mitochondrial initiator tRNA (tRNAMetf). N1-Methylguanine is determined by high pressure liquid chromatography analysis
the site of methylation is guanosine 37 in both mitochondrial tRNAMetf and tRNAPhe, determined by primer extension
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
the streptococcal enzyme utilizes a sequential mechanism. Nonsubstrate tRNA species, like tRNAThr(GGT), tRNAPhe, and tRNAAla(TGC), bind the enzyme with similar affinities, suggesting that tRNA specificity is achieved via a postbinding events. The streptococcal TrmD requires the complete tRNA structure since it cannot modify the tRNALeu(CAG) minihelix lacking the D, T, and extra loops of complete tRNA. In addition, and consistent with a requirement for G at positions 36 and 37 in the tRNA, the enzyme methylates yeast tRNAAsp possessing a G36G37 sequence with kinetic values that are indistinguishable from those obtained with substrate tRNALeu(CAG) but does not methylate either tRNAAsp possessing a C36G37 sequence or tRNA(Asp) possessing a C36A37 sequence
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-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
TrmD catalyzes the N1-methylguanosine (m1G) modification at position 37 in tRNAs with the 36GG37 sequence, using S-adenosyl-L-methionine as the methyl donor
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAArg
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAArg
-
tRNA substrate from Haemophilus influenzae
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAArg
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAArg
-
tRNA substrate from Haemophilus influenzae
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAArgCCG
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAArgCCG
Trametes pubescens 927 / 4 GUTat10.1 / TREU927
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAArgCCG
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAArgCCG
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNACys
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNACys
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNACys
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNACys
-
Methanococcus jannaschii tRNACys
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNACys
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNACys
Methanococcus jannaschii tRNACys
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNACysGCA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNACysGCA
Trametes pubescens 927 / 4 GUTat10.1 / TREU927
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNACysGCA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNACysGCA
-
-
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?
S-adenosyl-L-methionine + guanine37 in tRNAGlnCUG
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAGlnCUG
-
the wild-type Thermotoga maritima tRNAGlnCUG transcript is methylated by Haemophilus influenzae TrmD 2.2 to 99fold more efficiently than the Haemophilus influenzae tRNA transcripts
-
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?
S-adenosyl-L-methionine + guanine37 in tRNAGlnCUG
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAGlnCUG
-
the wild-type Thermotoga maritima tRNAGlnCUG transcript is methylated by Haemophilus influenzae TrmD 2.2 to 99fold more efficiently than the Haemophilus influenzae tRNA transcripts
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAGlnCUG
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAGlnCUG
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-
-
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?
S-adenosyl-L-methionine + guanine37 in tRNAHis(GUG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAHis(GUG)
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAHis(GUG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAHis(GUG)
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAHisGUG
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAHisGUG
Trametes pubescens 927 / 4 GUTat10.1 / TREU927
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-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAHisGUG
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAHisGUG
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAIleUaU
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAIleUaU
Trametes pubescens 927 / 4 GUTat10.1 / TREU927
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-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAIleUaU
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAIleUaU
Trametes pubescens 927 / 4 GUTat10.1 / TREU927
TbTRM5 is responsible for m1G37 formation in several tRNAs, cytosolic tRNAIle UAU is essentially fully modified at G37
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-
?
S-adenosyl-L-methionine + guanine37 in tRNAIleUaU
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAIleUaU
-
-
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?
S-adenosyl-L-methionine + guanine37 in tRNAIleUaU
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAIleUaU
TbTRM5 is responsible for m1G37 formation in several tRNAs, cytosolic tRNAIle UAU is essentially fully modified at G37
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNALeu
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNALeu
-
-
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?
S-adenosyl-L-methionine + guanine37 in tRNALeu
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNALeu
-
Escherichia coli tRNALeu
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-
?
S-adenosyl-L-methionine + guanine37 in tRNALeu
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNALeu
-
tRNA substrate from Haemophilus influenzae
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-
?
S-adenosyl-L-methionine + guanine37 in tRNALeu
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNALeu
-
tRNA substrate from Haemophilus influenzae
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-
?
S-adenosyl-L-methionine + guanine37 in tRNALeu(CAG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNALeu(CAG)
-
-
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?
S-adenosyl-L-methionine + guanine37 in tRNALeu(CAG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNALeu(CAG)
-
-
-
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?
S-adenosyl-L-methionine + guanine37 in tRNALeu(CAG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNALeu(CAG)
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAPhe
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPhe
-
-
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?
S-adenosyl-L-methionine + guanine37 in tRNAPhe
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPhe
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAPhe
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPhe
-
-
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?
S-adenosyl-L-methionine + guanine37 in tRNAPhe
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPhe
-
-
-
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?
S-adenosyl-L-methionine + guanine37 in tRNAPhe
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPhe
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAPro
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPro
the A37 mutant of EctRNAPro is no substrate for the enzyme
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAPro
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPro
-
tRNA substrate from Haemophilus influenzae
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-
?
S-adenosyl-L-methionine + guanine37 in tRNAPro(UGG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPro(UGG)
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-
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?
S-adenosyl-L-methionine + guanine37 in tRNAPro(UGG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPro(UGG)
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-
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?
S-adenosyl-L-methionine + guanine37 in tRNAPro(UGG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPro(UGG)
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-
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?
S-adenosyl-L-methionine + guanine37 in yeast tRNAAsp possessing a G36G37 sequence
S-adenosyl-L-homocysteine + N1-methylguanine37 in yeast tRNAAsp possessing a G36G37 sequence
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-
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?
S-adenosyl-L-methionine + guanine37 in yeast tRNAAsp possessing a G36G37 sequence
S-adenosyl-L-homocysteine + N1-methylguanine37 in yeast tRNAAsp possessing a G36G37 sequence
-
-
-
?
S-adenosyl-L-methionine + wyosine37 in tRNAPhe
S-adenosyl-L-homocysteine + N1-methylwyosine37 in tRNAPhe
-
-
-
?
S-adenosyl-L-methionine + wyosine37 in tRNAPhe
S-adenosyl-L-homocysteine + N1-methylwyosine37 in tRNAPhe
-
-
-
?
additional information
?
-
-
no activity with guanine37 in yeast tRNAAsp(GUC) possessing a C36G37 sequence, guanine37 in Haloferax volcanii tRNAGlu(UUC) possessing a C36G37 sequence, guanine37 in yeast tRNAPhe A36U mutant(GAU) possessing a U36G37 sequence, guanine37 in Escherichia coli tRNASer(UGA) possessing a A36G37 sequence
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-
?
additional information
?
-
TrmD synthesizes the methylated m1G37 on bacterial tRNAs that contain both G37 and a preceding G36, the 3'-nucleotide of the anticodon
-
-
-
additional information
?
-
TrmD can methylate a truncated tRNA, in which T- and D-arms have been deleted, the anticodon-arm region is mainly protected. The tRNA recognition mechanism of Aquifex aeolicus TrmD shows that a micro-helix RNA corresponding to the anticodon-arm is the minimal substrate for this enzyme
-
-
-
additional information
?
-
TrmD recognizes the G36pG37 motif preferentially and does not methylate inosine. The TrmD enzyme is tolerant of alterations in tRNA-protein tertiary interactions as long as the core tRNA structure and the G36pG37 are present
-
-
?
additional information
?
-
-
TrmD recognizes the G36pG37 motif preferentially and does not methylate inosine. The TrmD enzyme is tolerant of alterations in tRNA-protein tertiary interactions as long as the core tRNA structure and the G36pG37 are present
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-
?
additional information
?
-
-
TrmD catalyzes methyl transfer to synthesize the m1G37 base at the 3' position adjacent to the tRNA anticodon
-
-
?
additional information
?
-
-
recognition of N1 of G37 in tRNA is essential for translational fidelity in all biological domains, TrmD shows a more rigid requirement of guanosine functional groups. Replacment of functional groups of G37 by guanosine analogues, i.e. deoxyG, 6-thioG, inosine, and 2-aminopurine, in EctRNALeu, to design the optimal substrate for TrmD. All but deoxyG of these analogs probed the Watson-Crick basepairing interface of G37
-
-
?
additional information
?
-
TrmD synthesizes the methylated m1G37 on bacterial tRNAs that contain both G37 and a preceding G36, the 3'-nucleotide of the anticodon
-
-
-
additional information
?
-
proposed model for the TrmD enzymatic cycle which consists of the AdoMet-binding, tRNA-binding, and methyl transfer stages, overview. Anticodon-branch recognition and detection of position 37, interaction analysis of TrmD with G36 and G37
-
-
-
additional information
?
-
radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the TrmD reaction is the chemistry of methyl transfer
-
-
-
additional information
?
-
TrmD can methylate a truncated tRNA, in which T- and D-arms have been deleted, the anticodon-arm region is mainly protected
-
-
-
additional information
?
-
TrmD is a bacterial enzyme with a trefoil-knot in the active site, involving three crossings of the protein backbone through a loop. TrmD catalyzes methyl transfer from AdoMet to the N1 of G37 on the 3' side of the tRNA anticodon
-
-
-
additional information
?
-
TrmD synthesizes the methylated m1G37 on bacterial tRNAs that contain both G37 and a preceding G36, the 3'-nucleotide of the anticodon
-
-
-
additional information
?
-
proposed model for the TrmD enzymatic cycle which consists of the AdoMet-binding, tRNA-binding, and methyl transfer stages, overview. Anticodon-branch recognition and detection of position 37, interaction analysis of TrmD with G36 and G37
-
-
-
additional information
?
-
radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the TrmD reaction is the chemistry of methyl transfer
-
-
-
additional information
?
-
TrmD can methylate a truncated tRNA, in which T- and D-arms have been deleted, the anticodon-arm region is mainly protected
-
-
-
additional information
?
-
proposed model for the TrmD enzymatic cycle which consists of the AdoMet-binding, tRNA-binding, and methyl transfer stages, overview. Anticodon-branch recognition and detection of position 37, interaction analysis of TrmD with G36 and G37
-
-
-
additional information
?
-
radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the TrmD reaction is the chemistry of methyl transfer
-
-
-
additional information
?
-
proposed model for the TrmD enzymatic cycle which consists of the AdoMet-binding, tRNA-binding, and methyl transfer stages, overview. Anticodon-branch recognition and detection of position 37, interaction analysis of TrmD with G36 and G37
-
-
-
additional information
?
-
radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the TrmD reaction is the chemistry of methyl transfer
-
-
-
additional information
?
-
proposed model for the TrmD enzymatic cycle which consists of the AdoMet-binding, tRNA-binding, and methyl transfer stages, overview. Anticodon-branch recognition and detection of position 37, interaction analysis of TrmD with G36 and G37
-
-
-
additional information
?
-
radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the TrmD reaction is the chemistry of methyl transfer
-
-
-
additional information
?
-
proposed model for the TrmD enzymatic cycle which consists of the AdoMet-binding, tRNA-binding, and methyl transfer stages, overview. Anticodon-branch recognition and detection of position 37, interaction analysis of TrmD with G36 and G37
-
-
-
additional information
?
-
radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the TrmD reaction is the chemistry of methyl transfer
-
-
-
additional information
?
-
guanosine37-methylation by TRM5 occurs regardless of the nature of the nucleotide at position 36. TRM5 also methylates inosine at position 37. The TRM5 enzyme is sensitive to subtle changes in the tRNA-protein tertiary interaction leading to loss of activity. The enzyme does not methylate adenosine37, cytosine37 or uridine37 in tRNA. The TRM5 enzyme is sensitive to subtle changes in the tRNA-protein tertiary interaction leading to loss of activity
-
-
?
additional information
?
-
-
guanosine37-methylation by TRM5 occurs regardless of the nature of the nucleotide at position 36. TRM5 also methylates inosine at position 37. The TRM5 enzyme is sensitive to subtle changes in the tRNA-protein tertiary interaction leading to loss of activity. The enzyme does not methylate adenosine37, cytosine37 or uridine37 in tRNA. The TRM5 enzyme is sensitive to subtle changes in the tRNA-protein tertiary interaction leading to loss of activity
-
-
?
additional information
?
-
radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the Trm5 reaction is after methyl transfer and is associated with release of the m1G37-tRNA product
-
-
-
additional information
?
-
the enzyme is specific for methylation of guanine37 in tRNA. No methylation of tRNAArg(UCU) possessing the sequence U36G37
-
-
?
additional information
?
-
-
the enzyme is specific for methylation of guanine37 in tRNA. No methylation of tRNAArg(UCU) possessing the sequence U36G37
-
-
?
additional information
?
-
-
Trm5 catalyzes methyl transfer to synthesize the m1G37 base at the 3' position adjacent to the tRNA anticodon
-
-
?
additional information
?
-
-
recognition of N1 of G37 in tRNA is essential for translational fidelity in all biological domains, Trm5 shows a less rigid requirement of guanosine functional groups. Replacment of functional groups of G37 by guanosine analogues, i.e. deoxyG, 6-thioG, inosine, and 2-aminopurine, in MjtRNACys, to design the optimal substrate for Trm5
-
-
?
additional information
?
-
structure of Trm5 active site bound to tRNA and S-adenosyl-L-methionine, induced fit for active-site assembly, detailed overview. E185 is crucial both for general base catalysis and for the conformational change that precedes catalysis
-
-
?
additional information
?
-
radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the Trm5 reaction is after methyl transfer and is associated with release of the m1G37-tRNA product
-
-
-
additional information
?
-
structural basis for substrate recognition, the D1 domain of the enzyme undergoes large conformational changes upon the binding of tRNA, the enzyme recognizes the overall shape of tRNA, overview. Enzyme-substrate interactions in the catalytic domain, D1 domain ofMjTrm5b transitions, overview
-
-
-
additional information
?
-
the mutant tRNAMet transcripts (G37) are modified with m1G37 modification by the Mj-Trm5 but as less efficiently as cytoplasmic tRNALeu(CAG) transcripts. In contrast, the modification is not detected in the human wild-type tRNAMet transcripts (A37) in the presence of Mj-Trm5. The human cytoplasmic tRNALeu(CAG) transcripts (G37) are modified by the Mj-Trm5, whereas human cytoplasmic tRNAThr transcripts (A37) are not modified in the presence of Mj-Trm5. Marked decrease in the steady-state levels of mutated tRNAMet
-
-
-
additional information
?
-
tRNA recognition by Trm5, detailed overview. The structure of positions 33-37 in the anticodon loop is largely altered from the canonical tRNA structure, and the target G37 is flipped out into the catalytic pocket formed by the D2 and D3 domains. The flipped G37 is recognized in a guanosine-specific manner by the side chains of Arg145 and Asn265, and the N1-atom (the methylation atom) of G37 is located next to the methyl moiety of AdoMet. The adequate interaction between D1 and tRNA enables the catalytic D2-D3 to perform the m1G37 methylation. The m1G37 methylation is achieved by a sensor-effector mechanism in which the affinity of Trm5 for tRNA increases only when the sensor (D1) confirms the completion of the L-shape formation and the catalytically competent effector (D2-D3) is recruited to the tRNA
-
-
-
additional information
?
-
tRNA recognition by Trm5, detailed overview. The structure of positions 33-37 in the anticodon loop is largely altered from the canonical tRNA structure, and the target G37 is flipped out into the catalytic pocket formed by the D2 and D3 domains. The flipped G37 is recognized in a guanosine-specific manner by the side chains of Arg145 and Asn265, and the N1-atom (the methylation atom) of G37 is located next to the methyl moiety of AdoMet. The adequate interaction between D1 and tRNA enables the catalytic D2-D3 to perform the m1G37 methylation. The m1G37 methylation is achieved by a sensor-effector mechanism in which the affinity of Trm5 for tRNA increases only when the sensor (D1) confirms the completion of the L-shape formation and the catalytically competent effector (D2-D3) is recruited to the tRNA
-
-
-
additional information
?
-
the mutant tRNAMet transcripts (G37) are modified with m1G37 modification by the Mj-Trm5 but as less efficiently as cytoplasmic tRNALeu(CAG) transcripts. In contrast, the modification is not detected in the human wild-type tRNAMet transcripts (A37) in the presence of Mj-Trm5. The human cytoplasmic tRNALeu(CAG) transcripts (G37) are modified by the Mj-Trm5, whereas human cytoplasmic tRNAThr transcripts (A37) are not modified in the presence of Mj-Trm5. Marked decrease in the steady-state levels of mutated tRNAMet
-
-
-
additional information
?
-
radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the Trm5 reaction is after methyl transfer and is associated with release of the m1G37-tRNA product
-
-
-
additional information
?
-
structural basis for substrate recognition, the D1 domain of the enzyme undergoes large conformational changes upon the binding of tRNA, the enzyme recognizes the overall shape of tRNA, overview. Enzyme-substrate interactions in the catalytic domain, D1 domain ofMjTrm5b transitions, overview
-
-
-
additional information
?
-
tRNA recognition by Trm5, detailed overview. The structure of positions 33-37 in the anticodon loop is largely altered from the canonical tRNA structure, and the target G37 is flipped out into the catalytic pocket formed by the D2 and D3 domains. The flipped G37 is recognized in a guanosine-specific manner by the side chains of Arg145 and Asn265, and the N1-atom (the methylation atom) of G37 is located next to the methyl moiety of AdoMet. The adequate interaction between D1 and tRNA enables the catalytic D2-D3 to perform the m1G37 methylation. The m1G37 methylation is achieved by a sensor-effector mechanism in which the affinity of Trm5 for tRNA increases only when the sensor (D1) confirms the completion of the L-shape formation and the catalytically competent effector (D2-D3) is recruited to the tRNA
-
-
-
additional information
?
-
the mutant tRNAMet transcripts (G37) are modified with m1G37 modification by the Mj-Trm5 but as less efficiently as cytoplasmic tRNALeu(CAG) transcripts. In contrast, the modification is not detected in the human wild-type tRNAMet transcripts (A37) in the presence of Mj-Trm5. The human cytoplasmic tRNALeu(CAG) transcripts (G37) are modified by the Mj-Trm5, whereas human cytoplasmic tRNAThr transcripts (A37) are not modified in the presence of Mj-Trm5. Marked decrease in the steady-state levels of mutated tRNAMet
-
-
-
additional information
?
-
radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the Trm5 reaction is after methyl transfer and is associated with release of the m1G37-tRNA product
-
-
-
additional information
?
-
tRNA recognition by Trm5, detailed overview. The structure of positions 33-37 in the anticodon loop is largely altered from the canonical tRNA structure, and the target G37 is flipped out into the catalytic pocket formed by the D2 and D3 domains. The flipped G37 is recognized in a guanosine-specific manner by the side chains of Arg145 and Asn265, and the N1-atom (the methylation atom) of G37 is located next to the methyl moiety of AdoMet. The adequate interaction between D1 and tRNA enables the catalytic D2-D3 to perform the m1G37 methylation. The m1G37 methylation is achieved by a sensor-effector mechanism in which the affinity of Trm5 for tRNA increases only when the sensor (D1) confirms the completion of the L-shape formation and the catalytically competent effector (D2-D3) is recruited to the tRNA
-
-
-
additional information
?
-
the mutant tRNAMet transcripts (G37) are modified with m1G37 modification by the Mj-Trm5 but as less efficiently as cytoplasmic tRNALeu(CAG) transcripts. In contrast, the modification is not detected in the human wild-type tRNAMet transcripts (A37) in the presence of Mj-Trm5. The human cytoplasmic tRNALeu(CAG) transcripts (G37) are modified by the Mj-Trm5, whereas human cytoplasmic tRNAThr transcripts (A37) are not modified in the presence of Mj-Trm5. Marked decrease in the steady-state levels of mutated tRNAMet
-
-
-
additional information
?
-
radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the Trm5 reaction is after methyl transfer and is associated with release of the m1G37-tRNA product
-
-
-
additional information
?
-
tRNA recognition by Trm5, detailed overview. The structure of positions 33-37 in the anticodon loop is largely altered from the canonical tRNA structure, and the target G37 is flipped out into the catalytic pocket formed by the D2 and D3 domains. The flipped G37 is recognized in a guanosine-specific manner by the side chains of Arg145 and Asn265, and the N1-atom (the methylation atom) of G37 is located next to the methyl moiety of AdoMet. The adequate interaction between D1 and tRNA enables the catalytic D2-D3 to perform the m1G37 methylation. The m1G37 methylation is achieved by a sensor-effector mechanism in which the affinity of Trm5 for tRNA increases only when the sensor (D1) confirms the completion of the L-shape formation and the catalytically competent effector (D2-D3) is recruited to the tRNA
-
-
-
additional information
?
-
the mutant tRNAMet transcripts (G37) are modified with m1G37 modification by the Mj-Trm5 but as less efficiently as cytoplasmic tRNALeu(CAG) transcripts. In contrast, the modification is not detected in the human wild-type tRNAMet transcripts (A37) in the presence of Mj-Trm5. The human cytoplasmic tRNALeu(CAG) transcripts (G37) are modified by the Mj-Trm5, whereas human cytoplasmic tRNAThr transcripts (A37) are not modified in the presence of Mj-Trm5. Marked decrease in the steady-state levels of mutated tRNAMet
-
-
-
additional information
?
-
radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the Trm5 reaction is after methyl transfer and is associated with release of the m1G37-tRNA product
-
-
-
additional information
?
-
tRNA recognition by Trm5, detailed overview. The structure of positions 33-37 in the anticodon loop is largely altered from the canonical tRNA structure, and the target G37 is flipped out into the catalytic pocket formed by the D2 and D3 domains. The flipped G37 is recognized in a guanosine-specific manner by the side chains of Arg145 and Asn265, and the N1-atom (the methylation atom) of G37 is located next to the methyl moiety of AdoMet. The adequate interaction between D1 and tRNA enables the catalytic D2-D3 to perform the m1G37 methylation. The m1G37 methylation is achieved by a sensor-effector mechanism in which the affinity of Trm5 for tRNA increases only when the sensor (D1) confirms the completion of the L-shape formation and the catalytically competent effector (D2-D3) is recruited to the tRNA
-
-
-
additional information
?
-
the mutant tRNAMet transcripts (G37) are modified with m1G37 modification by the Mj-Trm5 but as less efficiently as cytoplasmic tRNALeu(CAG) transcripts. In contrast, the modification is not detected in the human wild-type tRNAMet transcripts (A37) in the presence of Mj-Trm5. The human cytoplasmic tRNALeu(CAG) transcripts (G37) are modified by the Mj-Trm5, whereas human cytoplasmic tRNAThr transcripts (A37) are not modified in the presence of Mj-Trm5. Marked decrease in the steady-state levels of mutated tRNAMet
-
-
-
additional information
?
-
radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the Trm5 reaction is after methyl transfer and is associated with release of the m1G37-tRNA product
-
-
-
additional information
?
-
Nanoarchaeum equitans NEQ228 protein displays a dual tRNAPhe:m1G/imG2 methyltransferase activity. Two different types of substrates are used: (1) bulk tRNA, isolated from Salmonella enterica trmDELTA27 mutant containing the unmodified G37 nucleotide leading tothe formation of pm1G, and (2) tRNA, which is isolated from the Saccharomes cerevisiae DELTAtyw2 mutant that contains the imG-14 wyosine derivative leading to formation of pimG2pA dinucleotide and to a lesser extent to pm1G, likely resulting from the small amounts of G37-containing tRNAPhe present in the bulk tRNA isolates from the Scetyw2 mutant
-
-
-
additional information
?
-
substrate specificity, mass spectrometric analysis confirms the G36G37-containing tRNAs Leu(GAG), Leu(CAG), Leu(UAG), Pro(GGG), Pro(UGG), Pro(CGG), and His(GUG) as PaTrmD substrates, overview. PaTrmD catalyzes m1G formation in synthetic tRNA substrates. PaTrmD catalyzes m1G at position 37 in the tRNA anticodon loop. Preparation of tRNA substrates by in vitro transcription, product determination by mass spectrometry
-
-
-
additional information
?
-
-
substrate specificity, mass spectrometric analysis confirms the G36G37-containing tRNAs Leu(GAG), Leu(CAG), Leu(UAG), Pro(GGG), Pro(UGG), Pro(CGG), and His(GUG) as PaTrmD substrates, overview. PaTrmD catalyzes m1G formation in synthetic tRNA substrates. PaTrmD catalyzes m1G at position 37 in the tRNA anticodon loop. Preparation of tRNA substrates by in vitro transcription, product determination by mass spectrometry
-
-
-
additional information
?
-
TrmD luminescence assay development
-
-
-
additional information
?
-
-
TrmD luminescence assay development
-
-
-
additional information
?
-
TrmD luminescence assay development
-
-
-
additional information
?
-
substrate specificity, mass spectrometric analysis confirms the G36G37-containing tRNAs Leu(GAG), Leu(CAG), Leu(UAG), Pro(GGG), Pro(UGG), Pro(CGG), and His(GUG) as PaTrmD substrates, overview. PaTrmD catalyzes m1G formation in synthetic tRNA substrates. PaTrmD catalyzes m1G at position 37 in the tRNA anticodon loop. Preparation of tRNA substrates by in vitro transcription, product determination by mass spectrometry
-
-
-
additional information
?
-
bifunctional Trm5a from Pyrococcus abyssi (PaTrm5a) catalyses not only the methylation of N1, but also the further methylation of C7 on 4 demethylwyosine at position 37 to produce isowyosine (EC 2.1.1.228 and EC 2.1.1.282, respectively)
-
-
-
additional information
?
-
bifunctional Trm5a from Pyrococcus abyssi (PaTrm5a) catalyses not only the methylation of N1, but also the further methylation of C7 on 4 demethylwyosine at position 37 to produce isowyosine (EC 2.1.1.228 and EC 2.1.1.282, respectively)
-
-
-
additional information
?
-
-
bifunctional Trm5a from Pyrococcus abyssi (PaTrm5a) catalyses not only the methylation of N1, but also the further methylation of C7 on 4 demethylwyosine at position 37 to produce isowyosine (EC 2.1.1.228 and EC 2.1.1.282, respectively)
-
-
-
additional information
?
-
no activity of Trm5b with 7-[(3S)-(3-amino-3-carboxypropyl)]-4-demethylwyosine37 in tRNAPhe (cf. EC 2.1.1.282)
-
-
-
additional information
?
-
-
no activity of Trm5b with 7-[(3S)-(3-amino-3-carboxypropyl)]-4-demethylwyosine37 in tRNAPhe (cf. EC 2.1.1.282)
-
-
-
additional information
?
-
Pyrococcus abyssi PAB2272 protein displays a dual tRNAPhe:m1G/imG2 methyltransferase activity. Two different types of substrates are used: (1) bulk tRNA, isolated from Salmonella enterica trmDELTA27 mutant containing the unmodified G37 nucleotide leading to the formation of pm1G, and (2) tRNA, which is isolated from the Saccharomes cerevisiae DELTAtyw2 mutant that contains the imG-14 wyosine derivative leading to formation of pimG2pA dinucleotide and to a lesser extent to pm1G, likely resulting from the small amounts of G37-containing tRNAPhe present in the bulk tRNA isolates from the Scetyw2 mutant
-
-
-
additional information
?
-
structural basis for substrate recognition, the D1 domain of the enzyme undergoes large conformational changes upon the binding of tRNA. The enzyme recognizes the overall shape of tRNA. PaTrm5a adopts distinct open conformations before and after the binding of tRNA. Enzyme-substrate interactions in the catalytic domain. The anticodon interactions mostly concentrate on the A36-G37-A38 triplet. Proposed reaction mechanism of Trm5a with modified yeast tRNAPhe, overview
-
-
-
additional information
?
-
substrate-binding modes of PaTrm5a, and recognition of substrate analogues, overview
-
-
-
additional information
?
-
-
substrate-binding modes of PaTrm5a, and recognition of substrate analogues, overview
-
-
-
additional information
?
-
tRNA recognition by Trm5, detailed overview. The structure of positions 33-37 in the anticodon loop is largely altered from the canonical tRNA structure, and the target G37 is flipped out into the catalytic pocket formed by the D2 and D3 domains. The flipped G37 is recognized in a guanosine-specific manner by the side chains of Arg145 and Asn265, and the N1-atom (the methylation atom) of G37 is located next to the methyl moiety of AdoMet. The adequate interaction between D1 and tRNA enables the catalytic D2-D3 to perform the m1G37 methylation. The m1G37 methylation is achieved by a sensor-effector mechanism in which the affinity of Trm5 for tRNA increases only when the sensor (D1) confirms the completion of the L-shape formation and the catalytically competent effector (D2-D3) is recruited to the tRNA
-
-
-
additional information
?
-
tRNA recognition by Trm5, detailed overview. The structure of positions 33-37 in the anticodon loop is largely altered from the canonical tRNA structure, and the target G37 is flipped out into the catalytic pocket formed by the D2 and D3 domains. The flipped G37 is recognized in a guanosine-specific manner by the side chains of Arg145 and Asn265, and the N1-atom (the methylation atom) of G37 is located next to the methyl moiety of AdoMet. The adequate interaction between D1 and tRNA enables the catalytic D2-D3 to perform the m1G37 methylation. The m1G37 methylation is achieved by a sensor-effector mechanism in which the affinity of Trm5 for tRNA increases only when the sensor (D1) confirms the completion of the L-shape formation and the catalytically competent effector (D2-D3) is recruited to the tRNA
-
-
-
additional information
?
-
Pyrococcus abyssi PAB2272 protein displays a dual tRNAPhe:m1G/imG2 methyltransferase activity. Two different types of substrates are used: (1) bulk tRNA, isolated from Salmonella enterica trmDELTA27 mutant containing the unmodified G37 nucleotide leading to the formation of pm1G, and (2) tRNA, which is isolated from the Saccharomes cerevisiae DELTAtyw2 mutant that contains the imG-14 wyosine derivative leading to formation of pimG2pA dinucleotide and to a lesser extent to pm1G, likely resulting from the small amounts of G37-containing tRNAPhe present in the bulk tRNA isolates from the Scetyw2 mutant
-
-
-
additional information
?
-
TrmD synthesizes the methylated m1G37 on bacterial tRNAs that contain both G37 and a preceding G36, the 3'-nucleotide of the anticodon
-
-
-
additional information
?
-
TrmD synthesizes the methylated m1G37 on bacterial tRNAs that contain both G37 and a preceding G36, the 3'-nucleotide of the anticodon
-
-
-
additional information
?
-
TrmD synthesizes the methylated m1G37 on bacterial tRNAs that contain both G37 and a preceding G36, the 3'-nucleotide of the anticodon
-
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-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
S-adenosyl-L-methionine + 4-demethylwyosine
S-adenosyl-L-homocysteine + isowyosine
S-adenosyl-L-methionine + 7-aminocarboxypropyl-demethylwyosine
S-adenosyl-L-homocysteine + wyosine
S-adenosyl-L-methionine + 7-[(3S)-(3-amino-3-carboxypropyl)]-4-demethylwyosine37 in tRNAPhe
S-adenosyl-L-homocysteine + 7-[(3S)-(3-amino-3-carboxypropyl)]wyosine37 in tRNAPhe
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
S-adenosyl-L-methionine + guanine37 in tRNAAsp(GUC)
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAAsp(GUC)
enzyme AtTrm5a can methylate Saccharomyces cerevisiae tRNAAsp(GUC) in vivo and in vitro
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAIleUaU
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAIleUaU
S-adenosyl-L-methionine + guanine37 in tRNAPhe
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPhe
S-adenosyl-L-methionine + guanine37 in tRNAPro(UGG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPro(UGG)
-
-
-
?
S-adenosyl-L-methionine + wyosine37 in tRNAPhe
S-adenosyl-L-homocysteine + N1-methylwyosine37 in tRNAPhe
additional information
?
-
S-adenosyl-L-methionine + 4-demethylwyosine
S-adenosyl-L-homocysteine + isowyosine
-
-
-
?
S-adenosyl-L-methionine + 4-demethylwyosine
S-adenosyl-L-homocysteine + isowyosine
-
-
-
?
S-adenosyl-L-methionine + 4-demethylwyosine
S-adenosyl-L-homocysteine + isowyosine
-
-
-
?
S-adenosyl-L-methionine + 7-aminocarboxypropyl-demethylwyosine
S-adenosyl-L-homocysteine + wyosine
-
-
-
?
S-adenosyl-L-methionine + 7-aminocarboxypropyl-demethylwyosine
S-adenosyl-L-homocysteine + wyosine
-
-
-
?
S-adenosyl-L-methionine + 7-aminocarboxypropyl-demethylwyosine
S-adenosyl-L-homocysteine + wyosine
-
-
-
?
S-adenosyl-L-methionine + 7-[(3S)-(3-amino-3-carboxypropyl)]-4-demethylwyosine37 in tRNAPhe
S-adenosyl-L-homocysteine + 7-[(3S)-(3-amino-3-carboxypropyl)]wyosine37 in tRNAPhe
-
-
-
?
S-adenosyl-L-methionine + 7-[(3S)-(3-amino-3-carboxypropyl)]-4-demethylwyosine37 in tRNAPhe
S-adenosyl-L-homocysteine + 7-[(3S)-(3-amino-3-carboxypropyl)]wyosine37 in tRNAPhe
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
TrmD catalyzes the N1-methylguanosine (m1G) modification at position 37 in tRNAs with the 36GG37 sequence, using S-adenosyl-L-methionine as the methyl donor
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
TrmD catalyzes the N1-methylguanosine (m1G) modification at position 37 in tRNAs with the 36GG37 sequence, using S-adenosyl-L-methionine as the methyl donor
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
Trm5p is responsible for m1G37 methylation of mitochondrial and cytoplasmic tRNAs
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
TrmD catalyzes the N1-methylguanosine (m1G) modification at position 37 in tRNAs with the 36GG37 sequence, using S-adenosyl-L-methionine as the methyl donor
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAIleUaU
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAIleUaU
Trametes pubescens 927 / 4 GUTat10.1 / TREU927
TbTRM5 is responsible for m1G37 formation in several tRNAs, cytosolic tRNAIle UAU is essentially fully modified at G37
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAIleUaU
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAIleUaU
TbTRM5 is responsible for m1G37 formation in several tRNAs, cytosolic tRNAIle UAU is essentially fully modified at G37
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAPhe
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPhe
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAPhe
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPhe
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAPhe
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPhe
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAPhe
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPhe
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAPhe
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPhe
-
-
-
?
S-adenosyl-L-methionine + wyosine37 in tRNAPhe
S-adenosyl-L-homocysteine + N1-methylwyosine37 in tRNAPhe
-
-
-
?
S-adenosyl-L-methionine + wyosine37 in tRNAPhe
S-adenosyl-L-homocysteine + N1-methylwyosine37 in tRNAPhe
-
-
-
?
additional information
?
-
TrmD synthesizes the methylated m1G37 on bacterial tRNAs that contain both G37 and a preceding G36, the 3'-nucleotide of the anticodon
-
-
-
additional information
?
-
-
TrmD catalyzes methyl transfer to synthesize the m1G37 base at the 3' position adjacent to the tRNA anticodon
-
-
?
additional information
?
-
TrmD synthesizes the methylated m1G37 on bacterial tRNAs that contain both G37 and a preceding G36, the 3'-nucleotide of the anticodon
-
-
-
additional information
?
-
TrmD is a bacterial enzyme with a trefoil-knot in the active site, involving three crossings of the protein backbone through a loop. TrmD catalyzes methyl transfer from AdoMet to the N1 of G37 on the 3' side of the tRNA anticodon
-
-
-
additional information
?
-
TrmD synthesizes the methylated m1G37 on bacterial tRNAs that contain both G37 and a preceding G36, the 3'-nucleotide of the anticodon
-
-
-
additional information
?
-
-
Trm5 catalyzes methyl transfer to synthesize the m1G37 base at the 3' position adjacent to the tRNA anticodon
-
-
?
additional information
?
-
bifunctional Trm5a from Pyrococcus abyssi (PaTrm5a) catalyses not only the methylation of N1, but also the further methylation of C7 on 4 demethylwyosine at position 37 to produce isowyosine (EC 2.1.1.228 and EC 2.1.1.282, respectively)
-
-
-
additional information
?
-
bifunctional Trm5a from Pyrococcus abyssi (PaTrm5a) catalyses not only the methylation of N1, but also the further methylation of C7 on 4 demethylwyosine at position 37 to produce isowyosine (EC 2.1.1.228 and EC 2.1.1.282, respectively)
-
-
-
additional information
?
-
-
bifunctional Trm5a from Pyrococcus abyssi (PaTrm5a) catalyses not only the methylation of N1, but also the further methylation of C7 on 4 demethylwyosine at position 37 to produce isowyosine (EC 2.1.1.228 and EC 2.1.1.282, respectively)
-
-
-
additional information
?
-
TrmD synthesizes the methylated m1G37 on bacterial tRNAs that contain both G37 and a preceding G36, the 3'-nucleotide of the anticodon
-
-
-
additional information
?
-
TrmD synthesizes the methylated m1G37 on bacterial tRNAs that contain both G37 and a preceding G36, the 3'-nucleotide of the anticodon
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additional information
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TrmD synthesizes the methylated m1G37 on bacterial tRNAs that contain both G37 and a preceding G36, the 3'-nucleotide of the anticodon
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(4-aminoquinazolin-2-yl)methyl 3-aminopyrazine-2-carboxylate
-
(4-oxo-3,4-dihydrothieno[3,2-d]pyrimidin-2-yl)methyl 2-(furan-2-yl)quinoline-4-carboxylate
-
1-(1H-pyrrol-2-yl)-2-[(thieno[2,3-d]pyrimidin-4-yl)oxy]ethan-1-one
-
1-(2-phenylpyrimidin-4-yl)-N-[(4-propoxyphenyl)methyl]piperidine-4-carboxamide
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1-(3-chlorophenyl)-5-ethyl-N-(4H-1,2,4-triazol-3-yl)-1H-pyrazole-4-carboxamide
-
1-[(2-chlorophenyl)methyl]-N-(4H-1,2,4-triazol-3-yl)-1H-pyrazole-4-carboxamide
-
1-[7-(3,4-dimethylbenzoyl)-2H-[1,3]dioxolo[4,5-g]quinolin-8-yl]piperidine-4-carboxamide
-
1H-indol-4-ylboronic acid
-
-
1H-indol-5-ylboronic acid
-
-
1H-indole-4-carboxylic acid
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2-((6-(3-amino-1H-pyrazol-5-yl)-1H-indol-1-yl)methyl)-benzamide
-
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2-((6-(3-amino-1H-pyrazol-5-yl)-1H-indol-1-yl)methyl)-benzonitrile
-
-
2-(1H-inden-2-yl)-5-[2-(1H-indol-3-yl)ethyl]-4-methyl-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
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2-(5-chlorothiophen-2-yl)-2-oxoethyl (3,4-dimethoxyphenyl)acetate
-
2-(8-fluoro-3,4-dihydroquinolin-1(2H)-yl)-N-(quinolin-5-yl)acetamide
-
2-oxo-2-(2-oxo-2,3-dihydro-1H-benzimidazol-5-yl)ethyl 2-methylquinoline-4-carboxylate
-
2-oxo-2-(2-oxo-2,3-dihydro-1H-benzimidazol-5-yl)ethyl 3-(cyclopropylsulfamoyl)thiophene-2-carboxylate
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2-oxo-2-(3-sulfamoylanilino)ethyl 2-(furan-2-yl)quinoline-4-carboxylate
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2-oxo-2-[(quinolin-5-yl)amino]ethyl 1-(5-carbamoylpyridin-2-yl)piperidine-4-carboxylate
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2-phenyl-7-(quinoline-6-carbonyl)-5,6,7,8-tetrahydropyrazolo[1,5-a]pyrido[4,3-d]pyrimidin-9(1H)-one
-
2-[(3,5-dichloropyridin-2-yl)amino]-2-oxoethyl 5,6-dihydro-4H-cyclopenta[b]thiophene-2-carboxylate
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2-[(4-acetylbenzene-1-sulfonyl)amino]thiophene-3-carboxamide
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2-[(5-chloropyridin-2-yl)amino]-2-oxoethyl 2-(furan-2-yl)quinoline-4-carboxylate
-
2-[2-(1-methyl-2-phenyl-2,3-dihydro-1H-indol-3-yl)-2-oxoethyl]-1,3-dioxo-1,2,3,5,6,7-hexahydropyrrolo[1,2-c]pyrimidine-4-carbonitrile
-
2-[2-(3-chlorophenoxy)acetamido]thiophene-3-carboxamide
-
2-[2-(4-oxocinnolin-1(4H)-yl)acetamido]-5,6-dihydro-4H-cyclopenta[b]thiophene-3-carboxamide
-
2-[3-(benzenesulfonyl)-7-methyl-4-oxo-1,8-naphthyridin-1(4H)-yl]-N-methyl-N-phenylacetamide
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2-[5-[2-(methylamino)-1,3-thiazol-4-yl]thiophen-2-yl]acetamide
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3-(1H-pyrrol-1-yl)-N-[4-[(1,3-thiazol-2-yl)sulfamoyl]phenyl]benzamide
-
3-(2-methoxy-2-oxoethoxy)benzyl 1H-pyrazole-4-carboxylate
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3-(4-methoxyphenyl)-7-[(1H-pyrrol-2-yl)methyl]-5,6,7,8-tetrahydro[1,2,4]triazolo[4,3-a]pyrazine
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3-(pyridin-2-ylmethoxy)benzyl 1H-pyrazole-4-carboxylate
-
-
3-amino-5-(1-((1-methylpiperidin-2-yl)methyl)-1H-indol-6-yl)-1H-pyrazole-4-carbonitrile
-
-
3-amino-5-(1-((1-methylpiperidin-3-yl)methyl)-1H-indol-6-yl)-1H-pyrazole-4-carbonitrile
-
-
3-amino-5-(1-((2-hydroxypyridin-3-yl)methyl)-1H-indol-6-yl)-1H-pyrazole-4-carbonitrile
-
-
3-amino-5-(1-((6-hydroxypyridin-3-yl)methyl)-1H-indol-6-yl)-1H-pyrazole-4-carbonitrile
-
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3-amino-5-(1-(4-((4-isopropylpiperazin-1-yl)methyl)-benzyl)-1H-indol-6-yl)-1H-pyrazole-4-carbonitrile
-
-
3-amino-5-(1-(4-(morpholinomethyl)benzyl)-1H-indol-6-yl)-1H-pyrazole-4-carbonitrile
-
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3-amino-5-(1-(4-(piperidin-1-ylmethyl)benzyl)-1H-indol-6-yl)-1H-pyrazole-4-carbonitrile
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3-amino-5-(1-(pyridin-3-ylmethyl)-1H-indol-6-yl)-1H-pyrazole-4-carbonitrile
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3-amino-5-(1-(pyridin-4-ylmethyl)-1H-indol-6-yl)-1H-pyrazole-4-carbonitrile
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3-amino-5-(1-(quinolin-4-ylmethyl)-1H-indol-6-yl)-1H-pyrazole-4-carbonitrile
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3-amino-5-(1-benzyl-1H-indol-6-yl)-1H-pyrazole-4-carbonitrile
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3-amino-5-(1H-indol-6-yl)-1H-pyrazole-4-carbonitrile
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3-amino-5-(3-chloro-1-(pyridin-3-ylmethyl)-1H-indol-6-yl)-1H-pyrazole-4-carbonitrile
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3-amino-5-[1-([4-[(4-methylpiperazin-1-yl)methyl]phenyl]methyl)-1H-indol-6-yl]-1H-pyrazole-4-carbonitrile
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3-amino-5-[1-([4-[(pyrrolidin-1-yl)methyl]phenyl]methyl)-1H-indol-6-yl]-1H-pyrazole-4-carbonitrile
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3-amino-5-[1-([5-[(pyrrolidin-1-yl)methyl]pyridin-2-yl]methyl)-1H-indol-6-yl]-1H-pyrazole-4-carbonitrile
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3-amino-5-[1-[(pyridin-2-yl)methyl]-1H-indol-6-yl]-1H-pyrazole-4-carbonitrile
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3-cyanobenzyl 1H-pyrazole-4-carboxylate
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3-ethoxybenzyl 1H-pyrazole-4-carboxylate
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3-methoxy-5-(pyridin-3-yl)benzyl 1H-pyrazole-4-carboxylate
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3-methoxy-5-(pyridin-3-ylmethyl)benzyl-1H-pyrazole-4-carboxylate
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3-methoxy-5-(pyrrolidin-1-yl)benzyl 1H-pyrazole-4-carboxylate
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3-methoxybenzyl 1H-pyrazole-4-carboxylate
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3-oxo-N-(5,6,7,8-tetrahydronaphthalen-1-yl)-3,4-dihydro-2H-1,4-benzoxazine-6-carboxamide
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3-oxo-N-[1-[4-(1H-1,2,4-triazol-1-yl)phenyl]ethyl]-3,4-dihydro-2H-1,4-benzoxazine-6-carboxamide
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3-oxo-N-[[2-(thiophen-2-yl)-1,3-oxazol-4-yl]methyl]-3,4-dihydro-2H-1,4-benzoxazine-6-carboxamide
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3-phenethoxybenzyl 1H-pyrazole-4-carboxylate
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4-((4-azidobenzyl)oxy)-N-(4-((octylamino)methyl)benzyl)thieno-[2,3-d]pyrimidine-5-carboxamide
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4-(hexyloxy)-N-(4-((octylamino)methyl)benzyl)thieno[2,3-d]-pyrimidine-5-carboxamide
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4-(methoxycarbonyl)benzyl 1H-pyrazole-4-carboxylate
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4-methoxy-N-(4-(morpholinomethyl)benzyl)thieno[2,3-d]-pyrimidine-5-carboxamide
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4-methyl-5-(1-(4-(pyrrolidin-1-ylmethyl)benzyl)-1H-indol-6-yl)-1H-pyrazol-3-amine
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4-nitrobenzyl 1H-pyrazole-4-carboxylate
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4-oxo-N-(4-((pentylamino)methyl)benzyl)-3,4-dihydrothieno-[2,3-d]pyrimidine-5-carboxamide
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4-oxo-N-(4-(piperidin-1-ylmethyl)benzyl)-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
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4-[(tetrazolo[1,5-b]pyridazin-6-yl)amino]benzamide
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4-[3-(8-hydroxyimidazo[1,2-a]pyridin-2-yl)-2,5-dimethyl-1H-pyrrol-1-yl]benzene-1-sulfonamide
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4-[3-(pyridin-4-yl)-1H-pyrazol-5-yl]thiomorpholine
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5'-[(2-aminoethyl)thio]-5'-deoxy-adenosine
5,7-dimethyl-N-(4H-1,2,4-triazol-3-yl)pyrazolo[1,5-a]pyrimidine-3-carboxamide
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5-(1-(3-methoxybenzyl)-1H-indol-6-yl)-1H-pyrazol-3-amine
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5-(1-(4-(piperidin-1-ylmethyl)benzyl)-1H-indol-6-yl)-1H-pyrazol-3-amine
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5-(1-(4-methoxybenzyl)-1H-indol-6-yl)-1H-pyrazol-3-amine
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5-(1-benzyl-1H-indol-6-yl)-1H-pyrazol-3-amine
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5-(1H-indol-6-yl)-1H-pyrazol-3-amine
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5-(3-methoxyphenyl)-1H-pyrazol-3-amine
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5-(4-methoxyphenyl)-1H-pyrazol-3-amine
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5-(4-methylphenyl)-1H-pyrazol-3-amine
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5-(5-methylthiophen-2-yl)thieno[2,3-d]pyrimidin-4(3H)-one
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5-phenyl-1H-pyrazol-3-amine
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5-[1-([4-[(pyrrolidin-1-yl)methyl]phenyl]methyl)-1H-indol-6-yl]-1H-pyrazol-3-amine
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5-[1-[(pyridin-2-yl)methyl]-1H-indol-6-yl]-1H-pyrazol-3-amine
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5-[2-(1,4-dioxa-8-azaspiro[4.5]decan-8-yl)-2-oxoethyl]-2-(3-fluorophenyl)-7-methyl-3-(1H-pyrrol-1-yl)-2,3,3a,5-tetrahydro-4H-pyrazolo[3,4-d]pyridazin-4-one
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6-(2-[[(furan-2-yl)methyl]amino]-1,3-thiazol-4-yl)-3,4-dihydroquinolin-2(1H)-one
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6-[5-(thiophen-2-yl)-1,2,4-oxadiazol-3-yl][1,2,4]triazolo[4,3-a]pyridine
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benzyl 1H-pyrazole-4-carboxylate
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ethyl 1-(3-(3-(((1H-pyrazole-4-carbonyl)oxy)methyl)-5-methoxyphenyl)prop-2-yn-1-yl)-1H-pyrazole-4-carboxylate
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ethyl 1H-pyrazole-4-carboxylate
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ethyl 4-[(3-cyano-6,7-dimethoxyquinolin-4-yl)amino]benzoate
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glycerol
the Escherichia coli TRmD performs best in the absence of glycerol, its activity decresaing linearly with increasing glycerol concentrations. No activity at 50% glycerol
N-(2-methoxy-5-methylphenyl)-N'-[1,2,4]triazolo[4,3-a]pyridin-3-ylurea
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N-(3,4-dimethylphenyl)-5,6-dihydro-4H-cyclopenta[d][1,2]oxazole-3-carboxamide
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N-(3-acetylphenyl)-N2-[5-chloro-2-(pyrrolidin-1-yl)phenyl]glycinamide
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N-(3-carbamoyl-5,6-dihydro-4H-cyclopenta[b]thiophen-2-yl)-4-chloropyridine-2-carboxamide
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N-(3-carbamoylthiophen-2-yl)-2-(pyridin-4-yl)quinoline-4-carboxamide
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N-(3-cyanothiophen-2-yl)-2-(furan-2-yl)quinoline-4-carboxamide
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N-(4-((((3s,5s,7s)-adamantan-1-yl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
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N-(4-(((2-(2-(2-aminoethoxy)ethoxy)ethyl)amino)methyl)-benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
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N-(4-(((2-(2-ethoxyethoxy)ethyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
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N-(4-(((2-(2-hydroxyethoxy)ethyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
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N-(4-(((4-aminobutyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide dihydrochloride
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N-(4-(((5-(1,5-dihydroxy-4-oxo-1,4-dihydropyridine-2-carboxamido)pentyl)amino) methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
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N-(4-(((5-aminopentyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
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N-(4-(((7-aminohexyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
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N-(4-((1,5-dihydroxy-4-oxo-1,4-dihydropyridine-2-carboxamido)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]-pyrimidine-5-carboxamide
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N-(4-((benzyl(ethyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
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N-(4-((benzyl(hexyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
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N-(4-((benzyl(octyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
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N-(4-((benzylamino)methyl)benzyl)-4-(hexyloxy)thieno[2,3-d]-pyrimidine-5-carboxamide
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N-(4-((benzylamino)methyl)benzyl)-4-methoxythieno[2,3-d]-pyrimidine-5-carboxamide
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N-(4-((benzylamino)methyl)benzyl)-4-oxo-3,4-dihydrothieno-[2,3-d]pyrimidine-5-carboxamide
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N-(4-((benzylamino)methyl)benzyl)-4-propoxythieno[2,3-d]-pyrimidine-5-carboxamide
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N-(4-((butylamino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
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N-(4-((cyclohexyl(ethyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
N-(4-((cyclohexylamino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
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N-(4-((decylamino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
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N-(4-((diethylamino)methyl)benzyl)-4-oxo-3,4-dihydrothieno-[2,3-d]pyrimidine-5-carboxamide
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enzyme-bound crystal structure, overview
N-(4-((dodecylamino)methyl)benzyl)-4-oxo-3,4-dihydrothieno-[2,3-d]pyrimidine-5-carboxamide
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N-(4-((ethyl(octyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
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N-(4-((octylamino)methyl)benzyl)-4-moxythieno[2,3-d]-pyrimidine-5-carboxamide
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N-(4-((octylamino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
N-(4-((octylamino)methyl)benzyl)-4-propoxythieno[2,3-d]-pyrimidine-5-carboxamide
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N-(4-(morpholinomethyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
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N-(4-(morpholinomethyl)benzyl)-4-propoxythieno[2,3-d]-pyrimidine-5-carboxamide
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N-([1-[3-(pyridin-4-yl)-1H-pyrazol-5-yl]piperidin-4-yl]methyl)-1H-indole-2-carboxamide
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N-([2-[(morpholin-4-yl)methyl]phenyl]methyl)-2-(thiophene-2-carbonyl)benzamide
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N-([4-[(4-aminopiperidin-1-yl)methyl]phenyl]methyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
-
N-ethyl-1H-pyrazole-4-carboxamide
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N-methyl-1-[2-([[2-(pyridin-3-yl)quinazolin-4-yl]amino]methyl)phenyl]methanesulfonamide
-
N-methyl-N-[(oxan-4-yl)methyl]-2-(thiophen-3-yl)acetamide
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N-methyl-N-[[2-(pyrrolidin-1-yl)phenyl]methyl]-3-(1H-pyrrol-1-yl)benzamide
-
N-[(3,5-dimethyl-1,2-oxazol-4-yl)methyl]quinoline-6-carboxamide
-
N-[1-[3-(pyridin-4-yl)-1H-pyrazol-5-yl]piperidin-3-yl]-1H-indole-2-carboxamide
-
N-[1-[3-(pyridin-4-yl)-1H-pyrazol-5-yl]piperidin-3-yl]-2-(thiophen-2-yl)acetamide
-
N-[2-oxo-2-[(1,3,5-trimethyl-4,5-dihydro-1H-pyrazol-4-yl)amino]ethyl]-5,6-dihydro-4H-cyclopenta[b]thiophene-2-carboxamide
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N-[3-(pyridin-4-yl)-1,2-oxazol-5-yl]-5,6,7,8-tetrahydronaphthalene-2-sulfonamide
-
N-[3-([1,3]thiazolo[5,4-b]pyridin-2-yl)phenyl]quinoline-2-carboxamide
-
N-[3-[(3-fluoro-4-methylphenyl)carbamoyl]phenyl]-1-([1,3]thiazolo[5,4-b]pyridin-2-yl)piperidine-3-carboxamide
-
N-[4-(2-amino-2-oxoethyl)-1,3-thiazol-2-yl]-3-(3,5-dimethyl-1-phenyl-1H-pyrazol-4-yl)propanamide
-
N-[4-chloro-3-(pyrrolidine-1-sulfonyl)phenyl]-3-oxo-3,4-dihydro-2H-1,4-benzoxazine-6-carboxamide
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N-[[4-(piperidine-1-carbonyl)phenyl]methyl]-2-(thiophene-2-carbonyl)benzamide
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S-adenosyl-L-homocysteine
[4-(hydroxymethyl)-2,8-diazaspiro[4.5]decan-2-yl][1-(4-methoxyphenyl)cyclohexyl]methanone
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[5-(furan-2-yl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]methyl pyrazine-2-carboxylate
-
5'-[(2-aminoethyl)thio]-5'-deoxy-adenosine
-
-
5'-[(2-aminoethyl)thio]-5'-deoxy-adenosine
-
-
6-Chloropurine
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-
adenosine
-
-
AdoButyn
-
an S-adenosyl-L-methionine analogue
AdoButyn
-
an S-adenosyl-L-methionine analogue
AdoPropen
-
an S-adenosyl-L-methionine analogue
AdoPropen
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an S-adenosyl-L-methionine analogue
DTT
TrmD has maximal activity below 1 mM DTT and loses 20% of its activity above that value
DTT
TRM5 displays maximal activity above 1 mM DTT and loses 20% of its activity below that value
Inosine
-
-
KCl
the enzyme is most active in absence of KCl
KCl
TRM5 enzyme is stimulated 4fold by 100 mM KCl. TRM5 tends to lose all activity in 600 mM KCl
methionine
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-
methylthioadenosine
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N-(4-((cyclohexyl(ethyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
-
enzyme-bound crystal structure, overview
N-(4-((cyclohexyl(ethyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
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-
N-(4-((octylamino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
-
enzyme-bound crystal structure, overview
N-(4-((octylamino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
-
enzyme-bound crystal structure, overview
N-(4-((octylamino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
-
-
N-([4-[(4-aminopiperidin-1-yl)methyl]phenyl]methyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
-
the binding of AZ51 does not induce the side chain flip of Tyr111 in MtbTrmD, while the corresponding residue Tyr120 in PaTrmD turned 180° to form stacking interactions with the phenyl ring of the inhibitor, enzyme-bound crystal structure, overview
-
N-([4-[(4-aminopiperidin-1-yl)methyl]phenyl]methyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
-
i.e. AZ51, inhibitor binding induces conformational changes of the wall loop, whereupon the side chain of aromatic ring of Tyr120 flips about 180° and forms stacking interactions with both the phenyl and piperidine rings of AZ51. This feature appears unique to AZ51 and P
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N-([4-[(4-aminopiperidin-1-yl)methyl]phenyl]methyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
-
-
-
S-adenosyl-L-homocysteine
-
an S-adenosyl-L-methionine analogue
S-adenosyl-L-homocysteine
-
an S-adenosyl-L-methionine analogue
S-methyl-L-cysteine
-
-
sinefungin
-
an S-adenosyl-L-methionine analogue
sinefungin
-
an S-adenosyl-L-methionine analogue
sinefungin
competitive inhibitor
sinefungin
an active-site inhibitor and S-adenosyl-L-methionine (SAM) analogue, that binds at the N-terminal dommain in the SAM binding site. Structure analysis of crystallized isolated dimeric NTD, overview
sinefungin
and isosteric SAM analogue in which the methyl group of SAM is replaced by an amino group and the sulfur by a carbon atom, competitive inhibition with respect to SAM and uncompetitive for tRNA. A set of crystal structures of the homodimeric PaTrmD protein bound to SAM and sinefungin provide the molecular basis for enzyme competitive inhibition and identify the location of the bound divalent ion. Crystal structure of PaTrmD bound to the SAM-competitive inhibitor sinefungin (SFG) is refined at a resolution of 2.45 A. In order to unambiguously locate the divalent ion, a third structure where crystals of PaTrmD are soaked with Mn2+ and SFG is determined. One Mn2+ near each of the bound sinefungin can be built. Mn2+ is coordinated by side-chain carbonyl group of E173', carboxylic groups of E121, D174' and D182' and the nitrogen atom of the sinefungin tail
additional information
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fragments of S-adenosyl-L-methionine, adenosine and methionine, are selectively inhibitory of TrmD, while they are poor inhibitors for Trm5 from Methanocaldococcus jannaschii
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additional information
-
fragments of S-adenosyl-L-methionine, adenosine and methionine, are poor inhibitors of Trm5, while they are selectve inhibitors for TrmD from Escherichia coli
-
additional information
-
synthesis of thienopyrimidinone derivatives that inhibit bacterial tRNA (guanine37-N1)-methyltransferase (TrmD) by restructuring the active site with a tyrosine-flipping mechanism, overview. The tyrosine-flipping mechanism is uniquely found in Pseudomonas aeruginosa TrmD and renders the enzyme inaccessible to the cofactor S-adenosyl-L-methionine (SAM) and probably to the substrate tRNA
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additional information
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development of inhibitors against Mycobacterium abscessus tRNA (m1G37) methyltransferase (TrmD) using fragment-based approaches, inhibitor screening, overview. Determination of inhibitor thermodynamics and binding kinetics
-
additional information
high-throughput small-molecule library inhibitor screening, antibacterial growth inhibitory activities and haemolytic activity of selected TrmD inhibitors, binding affinity confirmed by thermal stability and surface plasmon resonance, overview
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additional information
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high-throughput small-molecule library inhibitor screening, antibacterial growth inhibitory activities and haemolytic activity of selected TrmD inhibitors, binding affinity confirmed by thermal stability and surface plasmon resonance, overview
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additional information
the N-terminal domain is a useful construct to probe the molecular interactions with SAM competitive inhibitors, in the search for molecules with antibiotic activity
-
additional information
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the N-terminal domain is a useful construct to probe the molecular interactions with SAM competitive inhibitors, in the search for molecules with antibiotic activity
-
additional information
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synthesis of thienopyrimidinone derivatives that inhibit bacterial tRNA (guanine37-N1)-methyltransferase (TrmD) by restructuring the active site with a tyrosine-flipping mechanism, nanomolar potency against TrmD in vitro, overview. This tyrosine-flipping mechanism is uniquely found in Pseudomonas aeruginosa TrmD and renders the enzyme inaccessible to the cofactor S-adenosyl-L-methionine (SAM) and probably to the substrate tRNA. Biochemical structure-activity relationships (SAR) for TrmD inhibitors, the thienopyrimidinone substituent flexibility is critical for potent TrmD inhibition. Analysis of hemolytic activity of the compounds. Effect of side chain length of 15 analogues
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additional information
-
synthesis of thienopyrimidinone derivatives that inhibit bacterial tRNA (guanine37-N1)-methyltransferase (TrmD) by restructuring the active site with a tyrosine-flipping mechanism, overview. The tyrosine-flipping mechanism is uniquely found in Pseudomonas aeruginosa TrmD and renders the enzyme inaccessible to the cofactor S-adenosyl-L-methionine (SAM) and probably to the substrate tRNA
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0.0092
(4-aminoquinazolin-2-yl)methyl 3-aminopyrazine-2-carboxylate
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0017
(4-oxo-3,4-dihydrothieno[3,2-d]pyrimidin-2-yl)methyl 2-(furan-2-yl)quinoline-4-carboxylate
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0049
1-(1H-pyrrol-2-yl)-2-[(thieno[2,3-d]pyrimidin-4-yl)oxy]ethan-1-one
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.013
1-(2-phenylpyrimidin-4-yl)-N-[(4-propoxyphenyl)methyl]piperidine-4-carboxamide
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0017
1-(3-chlorophenyl)-5-ethyl-N-(4H-1,2,4-triazol-3-yl)-1H-pyrazole-4-carboxamide
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.00011
1-[(2-chlorophenyl)methyl]-N-(4H-1,2,4-triazol-3-yl)-1H-pyrazole-4-carboxamide
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0058
1-[7-(3,4-dimethylbenzoyl)-2H-[1,3]dioxolo[4,5-g]quinolin-8-yl]piperidine-4-carboxamide
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0038
2-(1H-inden-2-yl)-5-[2-(1H-indol-3-yl)ethyl]-4-methyl-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0011
2-(5-chlorothiophen-2-yl)-2-oxoethyl (3,4-dimethoxyphenyl)acetate
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0066
2-(8-fluoro-3,4-dihydroquinolin-1(2H)-yl)-N-(quinolin-5-yl)acetamide
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0045
2-oxo-2-(2-oxo-2,3-dihydro-1H-benzimidazol-5-yl)ethyl 2-methylquinoline-4-carboxylate
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0053
2-oxo-2-(2-oxo-2,3-dihydro-1H-benzimidazol-5-yl)ethyl 3-(cyclopropylsulfamoyl)thiophene-2-carboxylate
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0015 - 0.0034
2-oxo-2-(3-sulfamoylanilino)ethyl 2-(furan-2-yl)quinoline-4-carboxylate
0.0034
2-oxo-2-[(quinolin-5-yl)amino]ethyl 1-(5-carbamoylpyridin-2-yl)piperidine-4-carboxylate
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.00093
2-phenyl-7-(quinoline-6-carbonyl)-5,6,7,8-tetrahydropyrazolo[1,5-a]pyrido[4,3-d]pyrimidin-9(1H)-one
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0007
2-[(3,5-dichloropyridin-2-yl)amino]-2-oxoethyl 5,6-dihydro-4H-cyclopenta[b]thiophene-2-carboxylate
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0029
2-[(4-acetylbenzene-1-sulfonyl)amino]thiophene-3-carboxamide
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.00053
2-[(5-chloropyridin-2-yl)amino]-2-oxoethyl 2-(furan-2-yl)quinoline-4-carboxylate
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0014
2-[2-(1-methyl-2-phenyl-2,3-dihydro-1H-indol-3-yl)-2-oxoethyl]-1,3-dioxo-1,2,3,5,6,7-hexahydropyrrolo[1,2-c]pyrimidine-4-carbonitrile
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0019
2-[2-(3-chlorophenoxy)acetamido]thiophene-3-carboxamide
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0025
2-[2-(4-oxocinnolin-1(4H)-yl)acetamido]-5,6-dihydro-4H-cyclopenta[b]thiophene-3-carboxamide
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0027
2-[3-(benzenesulfonyl)-7-methyl-4-oxo-1,8-naphthyridin-1(4H)-yl]-N-methyl-N-phenylacetamide
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.002
2-[5-[2-(methylamino)-1,3-thiazol-4-yl]thiophen-2-yl]acetamide
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.00031
3-(1H-pyrrol-1-yl)-N-[4-[(1,3-thiazol-2-yl)sulfamoyl]phenyl]benzamide
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0017
3-(4-methoxyphenyl)-7-[(1H-pyrrol-2-yl)methyl]-5,6,7,8-tetrahydro[1,2,4]triazolo[4,3-a]pyrazine
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0087
3-oxo-N-(5,6,7,8-tetrahydronaphthalen-1-yl)-3,4-dihydro-2H-1,4-benzoxazine-6-carboxamide
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0091
3-oxo-N-[1-[4-(1H-1,2,4-triazol-1-yl)phenyl]ethyl]-3,4-dihydro-2H-1,4-benzoxazine-6-carboxamide
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0097
3-oxo-N-[[2-(thiophen-2-yl)-1,3-oxazol-4-yl]methyl]-3,4-dihydro-2H-1,4-benzoxazine-6-carboxamide
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0018
4-((4-azidobenzyl)oxy)-N-(4-((octylamino)methyl)benzyl)thieno-[2,3-d]pyrimidine-5-carboxamide
Pseudomonas aeruginosa
-
pH 8.0, 37°C
0.000085
4-oxo-N-(4-((pentylamino)methyl)benzyl)-3,4-dihydrothieno-[2,3-d]pyrimidine-5-carboxamide
Pseudomonas aeruginosa
-
pH 8.0, 37°C
0.0011
4-oxo-N-(4-(piperidin-1-ylmethyl)benzyl)-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
Pseudomonas aeruginosa
-
pH 8.0, 37°C
0.0019
4-[(tetrazolo[1,5-b]pyridazin-6-yl)amino]benzamide
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0056
4-[3-(8-hydroxyimidazo[1,2-a]pyridin-2-yl)-2,5-dimethyl-1H-pyrrol-1-yl]benzene-1-sulfonamide
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0029
4-[3-(pyridin-4-yl)-1H-pyrazol-5-yl]thiomorpholine
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0025
5,7-dimethyl-N-(4H-1,2,4-triazol-3-yl)pyrazolo[1,5-a]pyrimidine-3-carboxamide
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.00049
5-(5-methylthiophen-2-yl)thieno[2,3-d]pyrimidin-4(3H)-one
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0036
5-[2-(1,4-dioxa-8-azaspiro[4.5]decan-8-yl)-2-oxoethyl]-2-(3-fluorophenyl)-7-methyl-3-(1H-pyrrol-1-yl)-2,3,3a,5-tetrahydro-4H-pyrazolo[3,4-d]pyridazin-4-one
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.011
6-(2-[[(furan-2-yl)methyl]amino]-1,3-thiazol-4-yl)-3,4-dihydroquinolin-2(1H)-one
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0054
6-[5-(thiophen-2-yl)-1,2,4-oxadiazol-3-yl][1,2,4]triazolo[4,3-a]pyridine
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.006
ethyl 4-[(3-cyano-6,7-dimethoxyquinolin-4-yl)amino]benzoate
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0028
N-(2-methoxy-5-methylphenyl)-N'-[1,2,4]triazolo[4,3-a]pyridin-3-ylurea
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.005
N-(3,4-dimethylphenyl)-5,6-dihydro-4H-cyclopenta[d][1,2]oxazole-3-carboxamide
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0047
N-(3-acetylphenyl)-N2-[5-chloro-2-(pyrrolidin-1-yl)phenyl]glycinamide
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0016
N-(3-carbamoyl-5,6-dihydro-4H-cyclopenta[b]thiophen-2-yl)-4-chloropyridine-2-carboxamide
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.006
N-(3-carbamoylthiophen-2-yl)-2-(pyridin-4-yl)quinoline-4-carboxamide
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0021
N-(3-cyanothiophen-2-yl)-2-(furan-2-yl)quinoline-4-carboxamide
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.00072
N-(4-((((3s,5s,7s)-adamantan-1-yl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
Pseudomonas aeruginosa
-
pH 8.0, 37°C
0.00045
N-(4-(((2-(2-(2-aminoethoxy)ethoxy)ethyl)amino)methyl)-benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
Pseudomonas aeruginosa
-
pH 8.0, 37°C
0.00021
N-(4-(((2-(2-ethoxyethoxy)ethyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
Pseudomonas aeruginosa
-
pH 8.0, 37°C
0.00011
N-(4-(((2-(2-hydroxyethoxy)ethyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
Pseudomonas aeruginosa
-
pH 8.0, 37°C
0.00008
N-(4-(((4-aminobutyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide dihydrochloride
Pseudomonas aeruginosa
-
pH 8.0, 37°C
0.0013
N-(4-(((5-(1,5-dihydroxy-4-oxo-1,4-dihydropyridine-2-carboxamido)pentyl)amino) methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
Pseudomonas aeruginosa
-
pH 8.0, 37°C
0.00011
N-(4-(((5-aminopentyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
Pseudomonas aeruginosa
-
pH 8.0, 37°C
0.00014
N-(4-(((7-aminohexyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
Pseudomonas aeruginosa
-
pH 8.0, 37°C
0.0007
N-(4-((1,5-dihydroxy-4-oxo-1,4-dihydropyridine-2-carboxamido)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]-pyrimidine-5-carboxamide
Pseudomonas aeruginosa
-
pH 8.0, 37°C
0.0022
N-(4-((benzyl(ethyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
Pseudomonas aeruginosa
-
pH 8.0, 37°C
0.0022
N-(4-((benzyl(hexyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
Pseudomonas aeruginosa
-
pH 8.0, 37°C
0.012
N-(4-((benzyl(octyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
Pseudomonas aeruginosa
-
pH 8.0, 37°C
0.00013
N-(4-((benzylamino)methyl)benzyl)-4-oxo-3,4-dihydrothieno-[2,3-d]pyrimidine-5-carboxamide
Pseudomonas aeruginosa
-
pH 8.0, 37°C
0.00015
N-(4-((butylamino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
Pseudomonas aeruginosa
-
pH 8.0, 37°C
0.00049
N-(4-((cyclohexyl(ethyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
Pseudomonas aeruginosa
-
pH 8.0, 37°C
0.00079
N-(4-((cyclohexylamino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
Pseudomonas aeruginosa
-
pH 8.0, 37°C
0.000025
N-(4-((decylamino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
Pseudomonas aeruginosa
-
pH 8.0, 37°C
0.00073
N-(4-((diethylamino)methyl)benzyl)-4-oxo-3,4-dihydrothieno-[2,3-d]pyrimidine-5-carboxamide
Pseudomonas aeruginosa
-
pH 8.0, 37°C
0.00038
N-(4-((dodecylamino)methyl)benzyl)-4-oxo-3,4-dihydrothieno-[2,3-d]pyrimidine-5-carboxamide
Pseudomonas aeruginosa
-
pH 8.0, 37°C
0.00037
N-(4-((ethyl(octyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
Pseudomonas aeruginosa
-
pH 8.0, 37°C
0.000024
N-(4-((octylamino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
Pseudomonas aeruginosa
-
pH 8.0, 37°C
0.003
N-(4-(morpholinomethyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
Pseudomonas aeruginosa
-
pH 8.0, 37°C
0.0013
N-([1-[3-(pyridin-4-yl)-1H-pyrazol-5-yl]piperidin-4-yl]methyl)-1H-indole-2-carboxamide
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.01
N-([2-[(morpholin-4-yl)methyl]phenyl]methyl)-2-(thiophene-2-carbonyl)benzamide
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.00018
N-([4-[(4-aminopiperidin-1-yl)methyl]phenyl]methyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
Pseudomonas aeruginosa
-
pH 8.0, 37°C
-
0.0043
N-methyl-1-[2-([[2-(pyridin-3-yl)quinazolin-4-yl]amino]methyl)phenyl]methanesulfonamide
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0062
N-methyl-N-[(oxan-4-yl)methyl]-2-(thiophen-3-yl)acetamide
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0013
N-methyl-N-[[2-(pyrrolidin-1-yl)phenyl]methyl]-3-(1H-pyrrol-1-yl)benzamide
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0039
N-[(3,5-dimethyl-1,2-oxazol-4-yl)methyl]quinoline-6-carboxamide
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0029
N-[1-[3-(pyridin-4-yl)-1H-pyrazol-5-yl]piperidin-3-yl]-1H-indole-2-carboxamide
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.012
N-[1-[3-(pyridin-4-yl)-1H-pyrazol-5-yl]piperidin-3-yl]-2-(thiophen-2-yl)acetamide
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0068
N-[2-oxo-2-[(1,3,5-trimethyl-4,5-dihydro-1H-pyrazol-4-yl)amino]ethyl]-5,6-dihydro-4H-cyclopenta[b]thiophene-2-carboxamide
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0087
N-[3-(pyridin-4-yl)-1,2-oxazol-5-yl]-5,6,7,8-tetrahydronaphthalene-2-sulfonamide
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0021
N-[3-([1,3]thiazolo[5,4-b]pyridin-2-yl)phenyl]quinoline-2-carboxamide
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.014
N-[3-[(3-fluoro-4-methylphenyl)carbamoyl]phenyl]-1-([1,3]thiazolo[5,4-b]pyridin-2-yl)piperidine-3-carboxamide
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0019
N-[4-(2-amino-2-oxoethyl)-1,3-thiazol-2-yl]-3-(3,5-dimethyl-1-phenyl-1H-pyrazol-4-yl)propanamide
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0031
N-[4-chloro-3-(pyrrolidine-1-sulfonyl)phenyl]-3-oxo-3,4-dihydro-2H-1,4-benzoxazine-6-carboxamide
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.001
N-[[4-(piperidine-1-carbonyl)phenyl]methyl]-2-(thiophene-2-carbonyl)benzamide
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0083
sinefungin
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0091
suramin
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0059
[4-(hydroxymethyl)-2,8-diazaspiro[4.5]decan-2-yl][1-(4-methoxyphenyl)cyclohexyl]methanone
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0053
[5-(furan-2-yl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]methyl pyrazine-2-carboxylate
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0015
2-oxo-2-(3-sulfamoylanilino)ethyl 2-(furan-2-yl)quinoline-4-carboxylate
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.0034
2-oxo-2-(3-sulfamoylanilino)ethyl 2-(furan-2-yl)quinoline-4-carboxylate
Pseudomonas aeruginosa
pH and temperature not specified in the publication
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evolution
-
the dedication of Mg2+ to rate enhancement separates TrmD from O- and N6-methyl transferases. TrmD shows the topologically knotted protein fold
evolution
-
the deep trefoil knot architecture is unique to the SpoU and tRNA methyltransferase D (TrmD) (SPOUT) family of methyltransferases (MTases) in all three domains of life
evolution
-
the deep trefoil knot architecture is unique to the SpoU and tRNA methyltransferase D (TrmD) (SPOUT) family of methyltransferases (MTases) in all three domains of life
evolution
-
the enzyme shows strong homology to members of the class I-like methyltransferase superfamily
evolution
archaeal Trm5a, a member of the archaeal Trm5a/b/c family of enzymes involved in the biosynthesis of the wyosine derivatives, division of the family aTrm5 into three subfamilies aTrm5a (further divided into Taw21 and Taw22 which are monofunctional and bifunctional aTrm5a), aTrm5b, and aTrm5c. While the enzymes belonging to these subfamilies do not significantly differ in their AdoMet-binding site, small differences have been observed within the NPPY motif, which, in certain amino-methyltransferases, is involved in the positioning of the target nitrogen atom. In contrast, the N-terminal sequences of the aforementioned enzymes differ substantially, e.g. a small conservative domain called D1 is present in aTrm5b and aTrm5c but absent in most of the aTrm5a proteins. Evolution of tRNAPhe:imG2 methyltransferases involved in the biosynthesis of wyosine derivatives in Archaea. Amino acid sequence alignment of Trm5a/b/c family of proteins. Monofunctional and bifunctional aTrm5a enzymes, overview
evolution
archaeal Trm5a, a member of the archaeal Trm5a/b/c family of enzymes involved in the biosynthesis of the wyosine derivatives, division of the family aTrm5 into three subfamilies aTrm5a (further divided into Taw21 and Taw22 which are monofunctional and bifunctional aTrm5a), aTrm5b, and aTrm5c. While the enzymes belonging to these subfamilies do not significantly differ in their AdoMet-binding site, small differences have been observed within the NPPY motif, which, in certain amino-methyltransferases, is involved in the positioning of the target nitrogen atom. In contrast, the N-terminal sequences of the aforementioned enzymes differ substantially, e.g. a small conservative domain called D1 is present in aTrm5b and aTrm5c but absent in most of the aTrm5a proteins. Evolution of tRNAPhe:imG2 methyltransferases involved in the biosynthesis of wyosine derivatives in Archaea. Amino acid sequence alignment of Trm5a/b/c/ family of proteins. Monofunctional and bifunctional aTrm5a enzymes, overview
evolution
at least 5 classes (class I-V) of structurally distinct AdoMet-dependent methyltransferases have been identified. Trm5 belongs to the class I tRNA methyl transferases. Trm5 is an active monomer that uses the class I-fold. Methanococcus jannaschii MjTrm5 is homologous to human Trm5
evolution
at least 5 classes (class I-V) of structurally distinct AdoMet-dependent methyltransferases have been identified. Trm5 belongs to the class I tRNA methyl transferases. Trm5 is an active monomer that uses the class I-fold. MjTrm5 is homologous to human Trm5
evolution
at least 5 classes (class I-V) of structurally distinct AdoMet-dependent methyltransferases have been identified. TrmD belongs to the class IV tRNA methyl transferases. TrmD is an obligated dimer that uses the class IV-fold for AdoMet binding. EcTrmD is homologous to Haemophilus influenza TrmD
evolution
at least 5 classes (class I-V) of structurally distinct AdoMet-dependent methyltransferases have been identified. TrmD belongs to the class IV tRNA methyl transferases. TrmD is an obligated dimer that uses the class IV-fold for AdoMet binding. Escherichia coli EcTrmD is homologous to Haemophilus influenza TrmD
evolution
during the evolutionary process, some euryarchaeota like Thermococcus and Pyrococcus preserved both the trm5 genes from the crenarchaeal origin as well as the native copy, but others apparently lost the latter. Phylogenetic distribution analyses of trm5 homologues in archaeal genomes allow the identification of three archaeal Trm5 (aTrm5) subfamilies: Trm5a, Trm5b, and Trm5c. Trm5b refers to the native form, while Trm5a refers to the crenarchaeal origin, and Trm5c to other members with divergent Trm5 sequences11. The three Trm5s differ substantially in primary sequences
evolution
in the bacterial domain, the biosynthesis of m1G37 is catalyzed by the tRNA methyltransferase TrmD, whereas in the eukaryotic and archaeal domains, it is catalyzed by Trm5. While both TrmD and Trm5 perform the same methyl transfer reaction, using S-adenosyl methionine (AdoMet) as the methyl donor, they are fundamentally different in structure, where TrmD is a member of the SpoU-TrmD family and Trm5 is a member of the Rossmann-fold family. TrmD and Trm5 also differ in virtually all aspects of the reaction mechanism
evolution
in the bacterial domain, the biosynthesis of m1G37 is catalyzed by the tRNA methyltransferase TrmD, whereas in the eukaryotic and archaeal domains, it is catalyzed by Trm5. While both TrmD and Trm5 perform the same methyl transfer reaction, using S-adenosyl methionine (AdoMet) as the methyl donor, they are fundamentally different in structure, where TrmD is a member of the SpoU-TrmD family and Trm5 is a member of the Rossmann-fold family. TrmD and Trm5 also differ in virtually all aspects of the reaction mechanism
evolution
in the bacterial domain, the biosynthesis of m1G37 is catalyzed by the tRNA methyltransferase TrmD, whereas in the eukaryotic and archaeal domains, it is catalyzed by Trm5. While both TrmD and Trm5 perform the same methyl transfer reaction, using S-adenosyl methionine (AdoMet) as the methyl donor, they are fundamentally different in structure, where TrmD is a member of the SpoU-TrmD family and Trm5 is a member of the Rossmann-fold family. TrmD and Trm5 also differ in virtually all aspects of the reaction mechanism
evolution
phylogenetic analyses revealed that the archaeal Trm5s can be grouped into three categories: Trm5a, Trm5b, and Trm5c, which all perform the N1-methylation of tRNAPhe G37. Trm5a exists in all crenarchaea. On the other hand, Trm5b is ubiquitously found in euryarchaeota, and is regarded as the original Trm5. Trm5c can be originated from euryarchaeota by horizontal gene transfer and exists in two crenarchaeal orders. In addition, both aTrm5b and aTrm5c contain an N-terminal domain named D1, which is responsible for the G19:C56 base pair recognition but may be absent from most aTrm5as. Despite the differences at the N-termini, all Trm5s have the Rossmann fold at the C-termini for catalysis, with the consensus NPPY motif located in the fourth beta-strand. The motif is known to position the nitrogen atom of G37 from the substrate, but specific sequences may vary from this consensus. Structure comparison of Methanococcus jannaschii MjTrm5b and PaTrm5b, overview
evolution
the enzyme TrmD belongs to the 2'-O-methyltransferase family, previously SpoU family of enzymes, conserved motifs in the TrmH (SpoU) and TrmD families, overview. Comparisons of topological knot structures in TrmH (SpoU) and TrmD. AdoMet-dependent enzymes can be divided into more than five classes according to the structure of their catalytic domain. Most methyltransferases have a Rossman fold catalytic domain and are classified as class I enzymes. In contrast, members of SPOUT RNA methyltransferase superfamily are classified as class IV enzymes, whose catalytic domain forms a deep trefoil (topological) knot. TrmD from Aquifex aeolicus belongs to the m1G37 methyltransferases
evolution
the enzyme TrmD belongs to the 2'-O-methyltransferase family, previously SpoU family of enzymes, conserved motifs in the TrmH (SpoU) and TrmD families, overview. Comparisons of topological knot structures in TrmH (SpoU) and TrmD. AdoMet-dependent enzymes can be divided into more than five classes according to the structure of their catalytic domain. Most methyltransferases have a Rossman fold catalytic domain and are classified as class I enzymes. In contrast, members of SPOUT RNA methyltransferase superfamily are classified as class IV enzymes, whose catalytic domain forms a deep trefoil (topological) knot. TrmD from Escherichia coli belongs to the m1G37 methyltransferases
evolution
the enzyme TrmD belongs to the 2'-O-methyltransferase family, previously SpoU family of enzymes, conserved motifs in the TrmH (SpoU) and TrmD families, overview. Comparisons of topological knot structures in TrmH (SpoU) and TrmD. AdoMet-dependent enzymes can be divided into more than five classes according to the structure of their catalytic domain. Most methyltransferases have a Rossman fold catalytic domain and are classified as class I enzymes. In contrast, members of SPOUT RNA methyltransferase superfamily are classified as class IV enzymes, whose catalytic domain forms a deep trefoil (topological) knot. TrmD from Haemophilus influenzae belongs to the m1G37 methyltransferases
evolution
the N1-atom of guanosine at position 37 in transfer RNA (tRNA) is methylated by tRNA methyltransferase 5 (Trm5) in eukaryotes and archaea, and by tRNA methyltransferase D (TrmD) in bacteria. Trm5 and TrmD have completely distinct origins, and therefore bear different tertiary folds. Enzyme structure and function analysis and comparisons of Pyrococcus abyssi and Methanocaldococcus jannaschii Trm5 enzymes with Escherichia coli and Haemophilus influenzae TrmD enzymes, overview. TrmD requires not only G37 but also G36 as a substrate tRNA sequence, and the nine-base pair RNA duplex consisting of the anticodon and D stems with the anticodon loop can serve as its minimum substrate. In contrast, Trm5 requires G37 together with the entire tRNA structure. Enzyme TrmD belongs to the class IV methyltransferases
evolution
the N1-atom of guanosine at position 37 in transfer RNA (tRNA) is methylated by tRNA methyltransferase 5 (Trm5) in eukaryotes and archaea, and by tRNA methyltransferase D (TrmD) in bacteria. Trm5 and TrmD have completely distinct origins, and therefore bear different tertiary folds. Enzyme structure and function analysis and comparisons of Pyrococcus abyssi and Methanocaldococcus jannaschii Trm5 enzymes with Escherichia coli and Haemophilus influenzae TrmD enzymes, overview. TrmD requires not only G37 but also G36 as a substrate tRNA sequence, and the nine-base pair RNA duplex consisting of the anticodon and D stems with the anticodon loop can serve as its minimum substrate. In contrast, Trm5 requires G37 together with the entire tRNA structure. Enzyme TrmD belongs to the class IV methyltransferases.
evolution
the N1-atom of guanosine at position 37 in transfer RNA (tRNA) is methylated by tRNA methyltransferase 5 (Trm5) in eukaryotes and archaea, and by tRNA methyltransferase D (TrmD) in bacteria. Trm5 and TrmD have completely distinct origins, and therefore bear different tertiary folds. Enzyme structure and function analysis and comparisons of Pyrococcus abyssi and Methanocaldococcus jannaschii Trm5 enzymes with Escherichia coli and Haemophilus influenzae TrmD enzymes, overview. TrmD requires not only G37 but also G36 as a substrate tRNA sequence, and the nine-base pair RNA duplex consisting of the anticodon and D stems with the anticodon loop can serve as its minimum substrate. In contrast, Trm5 requires G37 together with the entire tRNA structure. Phylogenetic analyses reveals that the archaeal Trm5s can be classified into three categories: Trm5a, Trm5b, and Trm5c. Trm5a, Trm5b, and Trm5c all perform the N1-methylation of tRNA G37. Enzyme Trm5 belongs to the class I methyltransferases. The Methanocaldococcus jannaschii Trm5b residues involved in the G19:C56 recognition are not conserved in Pyroccocus abyssi Trm5a
evolution
the N1-atom of guanosine at position 37 in transfer RNA (tRNA) is methylated by tRNA methyltransferase 5 (Trm5) in eukaryotes and archaea, and by tRNA methyltransferase D (TrmD) in bacteria. Trm5 and TrmD have completely distinct origins, and therefore bear different tertiary folds. Enzyme structure and function analysis and comparisons of Pyrococcus abyssi and Methanocaldococcus jannaschii Trm5 enzymes with Escherichia coli and Haemophilus influenzae TrmD enzymes, overview. TrmD requires not only G37 but also G36 as a substrate tRNA sequence, and the nine-base pair RNA duplex consisting of the anticodon and D stems with the anticodon loop can serve as its minimum substrate. In contrast, Trm5 requires G37 together with the entire tRNA structure. Phylogenetic analyses reveals that the archaeal Trm5s can be classified into three categories: Trm5a, Trm5b, and Trm5c. Trm5a, Trm5b, and Trm5c all perform the N1-methylation of tRNA G37. In addition to the methylation of the N1-atom of guanosine, Trm5a catalyzes the methylation of the C7-atom of 4-demethylwyosine, which is the intermediate of the wyosine derivatives found at position 37 of archaeal tRNAPhe. Enzyme Trm5 belongs to the class I methyltransferases. The Methanocaldococcus jannaschii Trm5b residues involved in the G19:C56 recognition are not conserved in Pyroccocus abyssi Trm5a
evolution
the TrmD knot is closely related to the trefoil-knot in SpoU methyl transferases, which catalyze 2'-O-methylation to RNA ribose for wide-ranging activities. In virtually all aspects of the methyl transfer reaction, TrmD is distinct from related Trm5
evolution
TrmD is broadly conserved in sequence and structure among bacterial species, in both Gram (+) and Gram (-), but it is absent from the eukaryotic and archaeal domains. TrmD is strongly conserved in sequence among evolutionarily diverse bacterial species
evolution
TrmD is broadly conserved in sequence and structure among bacterial species, in both Gram (+) and Gram (-), but it is absent from the eukaryotic and archaeal domains. TrmD is strongly conserved in sequence among evolutionarily diverse bacterial species
evolution
TrmD is broadly conserved in sequence and structure among bacterial species, in both Gram (+) and Gram (-), but it is absent from the eukaryotic and archaeal domains. TrmD is strongly conserved in sequence among evolutionarily diverse bacterial species. In all of the available structures of the TrmD dimer, each monomeric chain is made up of three distinct domains: an N-terminal domain (residues 1-160 in HiTrmD and EcTrmD) for binding AdoMet, a C-terminal domain for binding tRNA (residues 169-246), and a flexible linker in between (residues 161-168)
evolution
TrmD is broadly conserved in sequence and structure among bacterial species, in both Gram (+) and Gram (-), but it is absent from the eukaryotic and archaeal domains. TrmD is strongly conserved in sequence among evolutionarily diverse bacterial species. In all of the available structures of the TrmD dimer, each monomeric chain is made up of three distinct domains: an N-terminal domain (residues 1-160 in HiTrmD and EcTrmD) for binding AdoMet, a C-terminal domain for binding tRNA (residues 169-246), and a flexible linker in between (residues 161-168)
evolution
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tRNA (m1G37) methyltransferase (TrmD), a member of the SpoU-TrmD (SPOUT) RNA methyltransferase family
evolution
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the N1-atom of guanosine at position 37 in transfer RNA (tRNA) is methylated by tRNA methyltransferase 5 (Trm5) in eukaryotes and archaea, and by tRNA methyltransferase D (TrmD) in bacteria. Trm5 and TrmD have completely distinct origins, and therefore bear different tertiary folds. Enzyme structure and function analysis and comparisons of Pyrococcus abyssi and Methanocaldococcus jannaschii Trm5 enzymes with Escherichia coli and Haemophilus influenzae TrmD enzymes, overview. TrmD requires not only G37 but also G36 as a substrate tRNA sequence, and the nine-base pair RNA duplex consisting of the anticodon and D stems with the anticodon loop can serve as its minimum substrate. In contrast, Trm5 requires G37 together with the entire tRNA structure. Phylogenetic analyses reveals that the archaeal Trm5s can be classified into three categories: Trm5a, Trm5b, and Trm5c. Trm5a, Trm5b, and Trm5c all perform the N1-methylation of tRNA G37. In addition to the methylation of the N1-atom of guanosine, Trm5a catalyzes the methylation of the C7-atom of 4-demethylwyosine, which is the intermediate of the wyosine derivatives found at position 37 of archaeal tRNAPhe. Enzyme Trm5 belongs to the class I methyltransferases. The Methanocaldococcus jannaschii Trm5b residues involved in the G19:C56 recognition are not conserved in Pyroccocus abyssi Trm5a
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evolution
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archaeal Trm5a, a member of the archaeal Trm5a/b/c family of enzymes involved in the biosynthesis of the wyosine derivatives, division of the family aTrm5 into three subfamilies aTrm5a (further divided into Taw21 and Taw22 which are monofunctional and bifunctional aTrm5a), aTrm5b, and aTrm5c. While the enzymes belonging to these subfamilies do not significantly differ in their AdoMet-binding site, small differences have been observed within the NPPY motif, which, in certain amino-methyltransferases, is involved in the positioning of the target nitrogen atom. In contrast, the N-terminal sequences of the aforementioned enzymes differ substantially, e.g. a small conservative domain called D1 is present in aTrm5b and aTrm5c but absent in most of the aTrm5a proteins. Evolution of tRNAPhe:imG2 methyltransferases involved in the biosynthesis of wyosine derivatives in Archaea. Amino acid sequence alignment of Trm5a/b/c/ family of proteins. Monofunctional and bifunctional aTrm5a enzymes, overview
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evolution
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TrmD is broadly conserved in sequence and structure among bacterial species, in both Gram (+) and Gram (-), but it is absent from the eukaryotic and archaeal domains. TrmD is strongly conserved in sequence among evolutionarily diverse bacterial species
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evolution
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in the bacterial domain, the biosynthesis of m1G37 is catalyzed by the tRNA methyltransferase TrmD, whereas in the eukaryotic and archaeal domains, it is catalyzed by Trm5. While both TrmD and Trm5 perform the same methyl transfer reaction, using S-adenosyl methionine (AdoMet) as the methyl donor, they are fundamentally different in structure, where TrmD is a member of the SpoU-TrmD family and Trm5 is a member of the Rossmann-fold family. TrmD and Trm5 also differ in virtually all aspects of the reaction mechanism
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evolution
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the N1-atom of guanosine at position 37 in transfer RNA (tRNA) is methylated by tRNA methyltransferase 5 (Trm5) in eukaryotes and archaea, and by tRNA methyltransferase D (TrmD) in bacteria. Trm5 and TrmD have completely distinct origins, and therefore bear different tertiary folds. Enzyme structure and function analysis and comparisons of Pyrococcus abyssi and Methanocaldococcus jannaschii Trm5 enzymes with Escherichia coli and Haemophilus influenzae TrmD enzymes, overview. TrmD requires not only G37 but also G36 as a substrate tRNA sequence, and the nine-base pair RNA duplex consisting of the anticodon and D stems with the anticodon loop can serve as its minimum substrate. In contrast, Trm5 requires G37 together with the entire tRNA structure. Phylogenetic analyses reveals that the archaeal Trm5s can be classified into three categories: Trm5a, Trm5b, and Trm5c. Trm5a, Trm5b, and Trm5c all perform the N1-methylation of tRNA G37. Enzyme Trm5 belongs to the class I methyltransferases. The Methanocaldococcus jannaschii Trm5b residues involved in the G19:C56 recognition are not conserved in Pyroccocus abyssi Trm5a
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evolution
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at least 5 classes (class I-V) of structurally distinct AdoMet-dependent methyltransferases have been identified. Trm5 belongs to the class I tRNA methyl transferases. Trm5 is an active monomer that uses the class I-fold. MjTrm5 is homologous to human Trm5
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evolution
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the N1-atom of guanosine at position 37 in transfer RNA (tRNA) is methylated by tRNA methyltransferase 5 (Trm5) in eukaryotes and archaea, and by tRNA methyltransferase D (TrmD) in bacteria. Trm5 and TrmD have completely distinct origins, and therefore bear different tertiary folds. Enzyme structure and function analysis and comparisons of Pyrococcus abyssi and Methanocaldococcus jannaschii Trm5 enzymes with Escherichia coli and Haemophilus influenzae TrmD enzymes, overview. TrmD requires not only G37 but also G36 as a substrate tRNA sequence, and the nine-base pair RNA duplex consisting of the anticodon and D stems with the anticodon loop can serve as its minimum substrate. In contrast, Trm5 requires G37 together with the entire tRNA structure. Enzyme TrmD belongs to the class IV methyltransferases
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evolution
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at least 5 classes (class I-V) of structurally distinct AdoMet-dependent methyltransferases have been identified. TrmD belongs to the class IV tRNA methyl transferases. TrmD is an obligated dimer that uses the class IV-fold for AdoMet binding. Escherichia coli EcTrmD is homologous to Haemophilus influenza TrmD
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evolution
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the N1-atom of guanosine at position 37 in transfer RNA (tRNA) is methylated by tRNA methyltransferase 5 (Trm5) in eukaryotes and archaea, and by tRNA methyltransferase D (TrmD) in bacteria. Trm5 and TrmD have completely distinct origins, and therefore bear different tertiary folds. Enzyme structure and function analysis and comparisons of Pyrococcus abyssi and Methanocaldococcus jannaschii Trm5 enzymes with Escherichia coli and Haemophilus influenzae TrmD enzymes, overview. TrmD requires not only G37 but also G36 as a substrate tRNA sequence, and the nine-base pair RNA duplex consisting of the anticodon and D stems with the anticodon loop can serve as its minimum substrate. In contrast, Trm5 requires G37 together with the entire tRNA structure. Phylogenetic analyses reveals that the archaeal Trm5s can be classified into three categories: Trm5a, Trm5b, and Trm5c. Trm5a, Trm5b, and Trm5c all perform the N1-methylation of tRNA G37. Enzyme Trm5 belongs to the class I methyltransferases. The Methanocaldococcus jannaschii Trm5b residues involved in the G19:C56 recognition are not conserved in Pyroccocus abyssi Trm5a
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evolution
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at least 5 classes (class I-V) of structurally distinct AdoMet-dependent methyltransferases have been identified. Trm5 belongs to the class I tRNA methyl transferases. Trm5 is an active monomer that uses the class I-fold. MjTrm5 is homologous to human Trm5
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evolution
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TrmD is broadly conserved in sequence and structure among bacterial species, in both Gram (+) and Gram (-), but it is absent from the eukaryotic and archaeal domains. TrmD is strongly conserved in sequence among evolutionarily diverse bacterial species
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evolution
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in the bacterial domain, the biosynthesis of m1G37 is catalyzed by the tRNA methyltransferase TrmD, whereas in the eukaryotic and archaeal domains, it is catalyzed by Trm5. While both TrmD and Trm5 perform the same methyl transfer reaction, using S-adenosyl methionine (AdoMet) as the methyl donor, they are fundamentally different in structure, where TrmD is a member of the SpoU-TrmD family and Trm5 is a member of the Rossmann-fold family. TrmD and Trm5 also differ in virtually all aspects of the reaction mechanism
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evolution
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the N1-atom of guanosine at position 37 in transfer RNA (tRNA) is methylated by tRNA methyltransferase 5 (Trm5) in eukaryotes and archaea, and by tRNA methyltransferase D (TrmD) in bacteria. Trm5 and TrmD have completely distinct origins, and therefore bear different tertiary folds. Enzyme structure and function analysis and comparisons of Pyrococcus abyssi and Methanocaldococcus jannaschii Trm5 enzymes with Escherichia coli and Haemophilus influenzae TrmD enzymes, overview. TrmD requires not only G37 but also G36 as a substrate tRNA sequence, and the nine-base pair RNA duplex consisting of the anticodon and D stems with the anticodon loop can serve as its minimum substrate. In contrast, Trm5 requires G37 together with the entire tRNA structure. Phylogenetic analyses reveals that the archaeal Trm5s can be classified into three categories: Trm5a, Trm5b, and Trm5c. Trm5a, Trm5b, and Trm5c all perform the N1-methylation of tRNA G37. Enzyme Trm5 belongs to the class I methyltransferases. The Methanocaldococcus jannaschii Trm5b residues involved in the G19:C56 recognition are not conserved in Pyroccocus abyssi Trm5a
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evolution
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at least 5 classes (class I-V) of structurally distinct AdoMet-dependent methyltransferases have been identified. Trm5 belongs to the class I tRNA methyl transferases. Trm5 is an active monomer that uses the class I-fold. MjTrm5 is homologous to human Trm5
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evolution
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the N1-atom of guanosine at position 37 in transfer RNA (tRNA) is methylated by tRNA methyltransferase 5 (Trm5) in eukaryotes and archaea, and by tRNA methyltransferase D (TrmD) in bacteria. Trm5 and TrmD have completely distinct origins, and therefore bear different tertiary folds. Enzyme structure and function analysis and comparisons of Pyrococcus abyssi and Methanocaldococcus jannaschii Trm5 enzymes with Escherichia coli and Haemophilus influenzae TrmD enzymes, overview. TrmD requires not only G37 but also G36 as a substrate tRNA sequence, and the nine-base pair RNA duplex consisting of the anticodon and D stems with the anticodon loop can serve as its minimum substrate. In contrast, Trm5 requires G37 together with the entire tRNA structure. Phylogenetic analyses reveals that the archaeal Trm5s can be classified into three categories: Trm5a, Trm5b, and Trm5c. Trm5a, Trm5b, and Trm5c all perform the N1-methylation of tRNA G37. Enzyme Trm5 belongs to the class I methyltransferases. The Methanocaldococcus jannaschii Trm5b residues involved in the G19:C56 recognition are not conserved in Pyroccocus abyssi Trm5a
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evolution
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at least 5 classes (class I-V) of structurally distinct AdoMet-dependent methyltransferases have been identified. Trm5 belongs to the class I tRNA methyl transferases. Trm5 is an active monomer that uses the class I-fold. MjTrm5 is homologous to human Trm5
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evolution
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in the bacterial domain, the biosynthesis of m1G37 is catalyzed by the tRNA methyltransferase TrmD, whereas in the eukaryotic and archaeal domains, it is catalyzed by Trm5. While both TrmD and Trm5 perform the same methyl transfer reaction, using S-adenosyl methionine (AdoMet) as the methyl donor, they are fundamentally different in structure, where TrmD is a member of the SpoU-TrmD family and Trm5 is a member of the Rossmann-fold family. TrmD and Trm5 also differ in virtually all aspects of the reaction mechanism
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evolution
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the deep trefoil knot architecture is unique to the SpoU and tRNA methyltransferase D (TrmD) (SPOUT) family of methyltransferases (MTases) in all three domains of life
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evolution
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the N1-atom of guanosine at position 37 in transfer RNA (tRNA) is methylated by tRNA methyltransferase 5 (Trm5) in eukaryotes and archaea, and by tRNA methyltransferase D (TrmD) in bacteria. Trm5 and TrmD have completely distinct origins, and therefore bear different tertiary folds. Enzyme structure and function analysis and comparisons of Pyrococcus abyssi and Methanocaldococcus jannaschii Trm5 enzymes with Escherichia coli and Haemophilus influenzae TrmD enzymes, overview. TrmD requires not only G37 but also G36 as a substrate tRNA sequence, and the nine-base pair RNA duplex consisting of the anticodon and D stems with the anticodon loop can serve as its minimum substrate. In contrast, Trm5 requires G37 together with the entire tRNA structure. Enzyme TrmD belongs to the class IV methyltransferases
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evolution
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at least 5 classes (class I-V) of structurally distinct AdoMet-dependent methyltransferases have been identified. TrmD belongs to the class IV tRNA methyl transferases. TrmD is an obligated dimer that uses the class IV-fold for AdoMet binding. Escherichia coli EcTrmD is homologous to Haemophilus influenza TrmD
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evolution
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the N1-atom of guanosine at position 37 in transfer RNA (tRNA) is methylated by tRNA methyltransferase 5 (Trm5) in eukaryotes and archaea, and by tRNA methyltransferase D (TrmD) in bacteria. Trm5 and TrmD have completely distinct origins, and therefore bear different tertiary folds. Enzyme structure and function analysis and comparisons of Pyrococcus abyssi and Methanocaldococcus jannaschii Trm5 enzymes with Escherichia coli and Haemophilus influenzae TrmD enzymes, overview. TrmD requires not only G37 but also G36 as a substrate tRNA sequence, and the nine-base pair RNA duplex consisting of the anticodon and D stems with the anticodon loop can serve as its minimum substrate. In contrast, Trm5 requires G37 together with the entire tRNA structure. Enzyme TrmD belongs to the class IV methyltransferases
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evolution
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at least 5 classes (class I-V) of structurally distinct AdoMet-dependent methyltransferases have been identified. TrmD belongs to the class IV tRNA methyl transferases. TrmD is an obligated dimer that uses the class IV-fold for AdoMet binding. Escherichia coli EcTrmD is homologous to Haemophilus influenza TrmD
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evolution
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the N1-atom of guanosine at position 37 in transfer RNA (tRNA) is methylated by tRNA methyltransferase 5 (Trm5) in eukaryotes and archaea, and by tRNA methyltransferase D (TrmD) in bacteria. Trm5 and TrmD have completely distinct origins, and therefore bear different tertiary folds. Enzyme structure and function analysis and comparisons of Pyrococcus abyssi and Methanocaldococcus jannaschii Trm5 enzymes with Escherichia coli and Haemophilus influenzae TrmD enzymes, overview. TrmD requires not only G37 but also G36 as a substrate tRNA sequence, and the nine-base pair RNA duplex consisting of the anticodon and D stems with the anticodon loop can serve as its minimum substrate. In contrast, Trm5 requires G37 together with the entire tRNA structure. Enzyme TrmD belongs to the class IV methyltransferases
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evolution
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at least 5 classes (class I-V) of structurally distinct AdoMet-dependent methyltransferases have been identified. TrmD belongs to the class IV tRNA methyl transferases. TrmD is an obligated dimer that uses the class IV-fold for AdoMet binding. Escherichia coli EcTrmD is homologous to Haemophilus influenza TrmD
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evolution
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the N1-atom of guanosine at position 37 in transfer RNA (tRNA) is methylated by tRNA methyltransferase 5 (Trm5) in eukaryotes and archaea, and by tRNA methyltransferase D (TrmD) in bacteria. Trm5 and TrmD have completely distinct origins, and therefore bear different tertiary folds. Enzyme structure and function analysis and comparisons of Pyrococcus abyssi and Methanocaldococcus jannaschii Trm5 enzymes with Escherichia coli and Haemophilus influenzae TrmD enzymes, overview. TrmD requires not only G37 but also G36 as a substrate tRNA sequence, and the nine-base pair RNA duplex consisting of the anticodon and D stems with the anticodon loop can serve as its minimum substrate. In contrast, Trm5 requires G37 together with the entire tRNA structure. Phylogenetic analyses reveals that the archaeal Trm5s can be classified into three categories: Trm5a, Trm5b, and Trm5c. Trm5a, Trm5b, and Trm5c all perform the N1-methylation of tRNA G37. Enzyme Trm5 belongs to the class I methyltransferases. The Methanocaldococcus jannaschii Trm5b residues involved in the G19:C56 recognition are not conserved in Pyroccocus abyssi Trm5a
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evolution
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at least 5 classes (class I-V) of structurally distinct AdoMet-dependent methyltransferases have been identified. Trm5 belongs to the class I tRNA methyl transferases. Trm5 is an active monomer that uses the class I-fold. MjTrm5 is homologous to human Trm5
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malfunction
efficiency or accuracy of mitochondrial protein synthesis is decreased in cells lacking m1G37 methylation of mitochondrial tRNAs
malfunction
downregulation of TRM5 by RNAi leads to the expected disappearance of m1G37, but with little effect on cytoplasmic translation. Lack of m1G37 does not globally affect cytosolic translation. On the contrary, lack of TRM5 causes a marked growth phenotype and a significant decrease in mitochondrial functions, including protein synthesis
malfunction
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mutations in TRMT5 are associated with the hypomodification of a guanosine residue at position 37 (G37) of mitochondrial tRNA, this hypomodification is particularly prominent in skeletal muscle. The patients show lactic acidosis and evidence of multiple mitochondrial respiratory-chain-complex deficiencies in skeletal muscle
malfunction
structure-guided mutational analysis of HsTrm5 in comparison to the archaeal enzyme from Methanococcus jannaschii, MjTrm5, overview. Validation of the MjTrm5 ternary structure as a useful model for HsTrm5
malfunction
the ts phenotype of an essential gene mutation S88L in gene trmD can be closely linked to the catalytic defect of the gene product
malfunction
Arabidopsis attrm5a mutants are dwarfed and have short filaments, which leads to reduced seed setting. Proteomics data indicate differences in the abundance of proteins involved in photosynthesis, ribosome biogenesis, oxidative phosphorylation and calcium signalling. Levels of phytohormone auxin and jasmonate are reduced in attrm5a mutant, as well as expression levels of genes involved in flowering, shoot apex cell fate determination, and hormone synthesis and signalling. Taken together, loss-of-function of AtTrm5a impaires m1G and m1I methylation and leads to aberrant protein translation, disturbed hormone homeostasis and developmental defects in Arabidopsis plants
malfunction
deletion of the D1 domain greatly reduces the affinity and activity of PaTrm5a toward its RNA substrate
malfunction
elimination of TrmD increases protein synthesis frameshifts and causes cell death
malfunction
Lack of m1G37 promotes the tRNA to make +1-frameshifts in a fast mechanism during tRNA translocation from the A- to the P-site on the ribosome, and also in a much slower mechanism during tRNA stalling on the P-site next to an empty A-site
malfunction
mutations in the TrmD knot block this intramolecular signaling and decrease the synthesis of m1G37-tRNA, prompting ribosomes to +1-frameshifts and premature termination of protein synthesis. Ribosome frameshifting in the absence of TrmD, overview
malfunction
mutations in the TrmD knot block this intramolecular signaling and decrease the synthesis of m1G37-tRNA, prompting ribosomes to +1-frameshifts and premature termination of protein synthesis. Ribosome frameshifting in the absence of TrmD, overview
malfunction
mutations in the TrmD knot block this intramolecular signaling and decrease the synthesis of m1G37-tRNA, prompting ribosomes to +1-frameshifts and premature termination of protein synthesis. Ribosome frameshifting in the absence of TrmD, overview
malfunction
mutations in the TrmD knot block this intramolecular signaling and decrease the synthesis of m1G37-tRNA, prompting ribosomes to +1-frameshifts and premature termination of protein synthesis. Ribosome frameshifting in the absence of TrmD, overview
malfunction
substitutions of individual conservative amino acids of Pyrococcus abyssi Taw22 (P260N, E173A, and R174A) have a differential effect on the formation of m1G/imG2, while replacement of R134, F165, E213, and P262 with alanine abolishes the formation of both derivatives of G37
malfunction
substitutions of individual conservative amino acids of Pyrococcus abyssi Taw22 (P260N, E173A, and R174A) have a differential effect on the formation of m1G/imG2, while replacement of R134, F165, E213, and P262 with alanine abolishes the formation of both derivatives of G37
malfunction
the tRNA mutations, that disrupt the G19:C56 base pair, reduce the activity of full-length Trm5 at 70°C by enhancing the KM values but maintaining the kcat values. The Trm5 mutant with alanine substitutions of the D1 residues, that interact with the tRNA outer corner, has a higher KM value than the wild-type Trm5
malfunction
the tRNA mutations, that disrupt the G19:C56 base pair, reduce the activity of full-length Trm5 at 70°C by enhancing the KM values but maintaining the kcat values. The Trm5 mutant with alanine substitutions of the D1 residues, that interact with the tRNA outer corner, has a higher KM value than the wild-type Trm5
malfunction
Truncation of the N-terminal D1 domain leads to reduced tRNA binding as well as the methyltransfer activity of PaTrm5b
malfunction
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the tRNA mutations, that disrupt the G19:C56 base pair, reduce the activity of full-length Trm5 at 70°C by enhancing the KM values but maintaining the kcat values. The Trm5 mutant with alanine substitutions of the D1 residues, that interact with the tRNA outer corner, has a higher KM value than the wild-type Trm5
-
malfunction
-
substitutions of individual conservative amino acids of Pyrococcus abyssi Taw22 (P260N, E173A, and R174A) have a differential effect on the formation of m1G/imG2, while replacement of R134, F165, E213, and P262 with alanine abolishes the formation of both derivatives of G37
-
malfunction
-
mutations in the TrmD knot block this intramolecular signaling and decrease the synthesis of m1G37-tRNA, prompting ribosomes to +1-frameshifts and premature termination of protein synthesis. Ribosome frameshifting in the absence of TrmD, overview
-
malfunction
-
the tRNA mutations, that disrupt the G19:C56 base pair, reduce the activity of full-length Trm5 at 70°C by enhancing the KM values but maintaining the kcat values. The Trm5 mutant with alanine substitutions of the D1 residues, that interact with the tRNA outer corner, has a higher KM value than the wild-type Trm5
-
malfunction
-
the tRNA mutations, that disrupt the G19:C56 base pair, reduce the activity of full-length Trm5 at 70°C by enhancing the KM values but maintaining the kcat values. The Trm5 mutant with alanine substitutions of the D1 residues, that interact with the tRNA outer corner, has a higher KM value than the wild-type Trm5
-
malfunction
-
mutations in the TrmD knot block this intramolecular signaling and decrease the synthesis of m1G37-tRNA, prompting ribosomes to +1-frameshifts and premature termination of protein synthesis. Ribosome frameshifting in the absence of TrmD, overview
-
malfunction
-
the tRNA mutations, that disrupt the G19:C56 base pair, reduce the activity of full-length Trm5 at 70°C by enhancing the KM values but maintaining the kcat values. The Trm5 mutant with alanine substitutions of the D1 residues, that interact with the tRNA outer corner, has a higher KM value than the wild-type Trm5
-
malfunction
-
the tRNA mutations, that disrupt the G19:C56 base pair, reduce the activity of full-length Trm5 at 70°C by enhancing the KM values but maintaining the kcat values. The Trm5 mutant with alanine substitutions of the D1 residues, that interact with the tRNA outer corner, has a higher KM value than the wild-type Trm5
-
malfunction
Trametes pubescens 927 / 4 GUTat10.1 / TREU927
-
downregulation of TRM5 by RNAi leads to the expected disappearance of m1G37, but with little effect on cytoplasmic translation. Lack of m1G37 does not globally affect cytosolic translation. On the contrary, lack of TRM5 causes a marked growth phenotype and a significant decrease in mitochondrial functions, including protein synthesis
-
malfunction
-
the tRNA mutations, that disrupt the G19:C56 base pair, reduce the activity of full-length Trm5 at 70°C by enhancing the KM values but maintaining the kcat values. The Trm5 mutant with alanine substitutions of the D1 residues, that interact with the tRNA outer corner, has a higher KM value than the wild-type Trm5
-
metabolism
a hypertension-associated mitochondrial DNA mutation introduces an m1G37 mutation 4435A->G into human mitochondrial tRNAMet, altering its structure and function, phenotype and pathogenic molecular mechanism, overview. The mutation affects a highly conserved adenosine at position 37, 3' adjacent to the tRNA's anticodon, which is important for the fidelity of codon recognition and stabilization. Defective nucleotide modifications of mitochondrial tRNAs are associated with several human diseases. Trm5 is one of the tRNA (m1G37)-methyltransferases that catalyzes the identical tRNA modification, m1G37
metabolism
putative enzymatic pathway leading to the formation of wyosine derivatives in Archaea
metabolism
putative enzymatic pathway leading to the formation of wyosine derivatives in Archaea
metabolism
the enzyme is part of the The biosynthetic pathway of mimG in Pyrococcus abyssi, overview. In archaea, G37 hypermodification in tRNAPhe leads to wyosine derivatives. They are important in reading-frame maintenance during protein synthesis, while the absence of such modifications results in elevated error rates in +1 frame-shifting. Among the modification products, 7-methylwyosine (mimG) is perhaps the earliest and minimalist version of the wyosine derivatives unique to some archaea, and 4-demethylwyosine (imG-14), isowyosine (imG2) have also been identified as intermediates along the pathway. The first biosynthetic step of mimG is the formation of m1G37, catalysed by the S-adenosine-L-methionine (SAM)-dependent tRNA methyltransferase named Trm5, which belongs to class-I methyltransferases. The second step is the complex radical-mediated formation of imG-14, catalyzed by the radical SAM enzyme Taw1. The Trm5 enzyme from the archaeon Pyrococcus abyssi (PaTrm5a) also catalyzes the methylation of C7 on imG-14 to produce imG2 (EC 2.1.1.282), which is further methylated on the N4 position of the imidazo-purine ring by Taw3 to form mimG
metabolism
the wyosine hypermodification found exclusively at G37 of tRNAPhe in eukaryotes and archaea is a very complicated process involving multiple steps and enzymes, and the derivatives are essential for the maintenance of the reading frame during translation. In the archaea Pyrococcus abyssi, two key enzymes from the Trm5 family, named PaTrm5a and PaTrm5b respectively, start the process by forming N1-methylated guanosine (m1G37). In addition, PaTrm5a catalyzes the further methylation of C7 on 4-demethylwyosine (imG-14) to produce isowyosine (imG2) at the same position (cf. EC 2.1.1.282)
metabolism
-
putative enzymatic pathway leading to the formation of wyosine derivatives in Archaea
-
metabolism
-
a hypertension-associated mitochondrial DNA mutation introduces an m1G37 mutation 4435A->G into human mitochondrial tRNAMet, altering its structure and function, phenotype and pathogenic molecular mechanism, overview. The mutation affects a highly conserved adenosine at position 37, 3' adjacent to the tRNA's anticodon, which is important for the fidelity of codon recognition and stabilization. Defective nucleotide modifications of mitochondrial tRNAs are associated with several human diseases. Trm5 is one of the tRNA (m1G37)-methyltransferases that catalyzes the identical tRNA modification, m1G37
-
metabolism
-
a hypertension-associated mitochondrial DNA mutation introduces an m1G37 mutation 4435A->G into human mitochondrial tRNAMet, altering its structure and function, phenotype and pathogenic molecular mechanism, overview. The mutation affects a highly conserved adenosine at position 37, 3' adjacent to the tRNA's anticodon, which is important for the fidelity of codon recognition and stabilization. Defective nucleotide modifications of mitochondrial tRNAs are associated with several human diseases. Trm5 is one of the tRNA (m1G37)-methyltransferases that catalyzes the identical tRNA modification, m1G37
-
metabolism
-
a hypertension-associated mitochondrial DNA mutation introduces an m1G37 mutation 4435A->G into human mitochondrial tRNAMet, altering its structure and function, phenotype and pathogenic molecular mechanism, overview. The mutation affects a highly conserved adenosine at position 37, 3' adjacent to the tRNA's anticodon, which is important for the fidelity of codon recognition and stabilization. Defective nucleotide modifications of mitochondrial tRNAs are associated with several human diseases. Trm5 is one of the tRNA (m1G37)-methyltransferases that catalyzes the identical tRNA modification, m1G37
-
metabolism
-
a hypertension-associated mitochondrial DNA mutation introduces an m1G37 mutation 4435A->G into human mitochondrial tRNAMet, altering its structure and function, phenotype and pathogenic molecular mechanism, overview. The mutation affects a highly conserved adenosine at position 37, 3' adjacent to the tRNA's anticodon, which is important for the fidelity of codon recognition and stabilization. Defective nucleotide modifications of mitochondrial tRNAs are associated with several human diseases. Trm5 is one of the tRNA (m1G37)-methyltransferases that catalyzes the identical tRNA modification, m1G37
-
metabolism
-
a hypertension-associated mitochondrial DNA mutation introduces an m1G37 mutation 4435A->G into human mitochondrial tRNAMet, altering its structure and function, phenotype and pathogenic molecular mechanism, overview. The mutation affects a highly conserved adenosine at position 37, 3' adjacent to the tRNA's anticodon, which is important for the fidelity of codon recognition and stabilization. Defective nucleotide modifications of mitochondrial tRNAs are associated with several human diseases. Trm5 is one of the tRNA (m1G37)-methyltransferases that catalyzes the identical tRNA modification, m1G37
-
physiological function
modification at guanine37 is important for maintaining the reading frame fidelity
physiological function
modified guanosine37 is adjacent to and 3' of the anticodon and is essential for the maintenance of the correct reading frame during translation
physiological function
-
the m1G37 modification prevents tRNA frameshifts on the ribosome by assuring correct codon-anticodon pairings, and thus is essential for the fidelity of protein synthesis
physiological function
the m1G37 modification prevents tRNA frameshifts on the ribosome by assuring correct codon-anticodon pairings, and thus is essential for the fidelity of protein synthesis
physiological function
the m1G37 tRNA modification plays an important role in reading frame maintenance in mitochondrial protein synthesis
physiological function
this protein is important for the maintenance of the correct reading frame during translation
physiological function
-
methylation of G37 to form m1G acts to sterically block Watson-Crick base pairing and thereby both maintain an open loop conformation, by blocking base pairing with nucleotides elsewhere in the anticodon loop, and protect against frame shifting by preventing its interaction with the mRNA
physiological function
-
S-adenosyl-L-methionine-dependent methyl transfer in one of the most crucial posttranscriptional modifications to tRNA
physiological function
-
the m1G37-modified tRNA functions properly to prevent +1 frameshift errors on the ribosome
physiological function
-
the m1G37-modified tRNA functions properly to prevent +1 frameshift errors on the ribosome
physiological function
TRM5 is responsible for m1G37 formation, m1G37 formation in mitochondria is important for respiration, and TbTRM5 is important for mitochondrial protein synthesis and biogenesis. Mitochondrial TRM5 may be needed to mature unmethylated tRNAs that reach the mitochondria and that can pose a problem for translational fidelity, lack of import specificity between some fully matured and potentially defective tRNA species
physiological function
among various RNA types, tRNA is the most frequently modified type. One such modification in tRNAPhe is the methylation at N1 of G37 (m1G37), which is conserved among all three domains of life. The presence of m1G37 allows effective and rapid aminoacylation of certain archaeal tRNA species by cognate aminoacyl-tRNA synthetases, and prevents misacylation by noncognate aminoacyl-tRNA synthetases, as well as +1 frameshift during translation on the ribosome
physiological function
-
bacterial tRNA (guanine37-N1)-methyltransferase (TrmD) catalyzes methyl transfer from S-adenosyl-L-methionine (SAM) to the guanine N1 at nucleotide position 37 in a subset of bacterial tRNA isoacceptors and has proven to be an essential enzyme in most bacterial species
physiological function
-
bacterial tRNA (guanine37-N1)-methyltransferase (TrmD) catalyzes methyl transfer from S-adenosyl-L-methionine (SAM) to the guanine N1 at nucleotide position 37 in a subset of bacterial tRNA isoacceptors and has proven to be an essential enzyme in most bacterial species
physiological function
-
bacterial tRNA (guanine37-N1)-methyltransferase (TrmD) catalyzes methyl transfer from S-adenosyl-L-methionine (SAM) to the guanine N1 at nucleotide position 37 in a subset of bacterial tRNA isoacceptors and has proven to be an essential enzyme in most bacterial species
physiological function
enzyme TrmD catalyzes the transfer of methyl group from AdoMet to N1-atom of G37 in tRNA to form m1G37
physiological function
enzyme TrmD catalyzes the transfer of methyl group from AdoMet to N1-atom of G37 in tRNA to form m1G37
physiological function
enzyme TrmD catalyzes the transfer of methyl group from AdoMet to N1-atom of G37 in tRNA to form m1G37
physiological function
he N1-atom of guanosine at position 37 in transfer RNA (tRNA) is methylated by tRNA methyltransferase 5 (Trm5) in eukaryotes and archaea, and by tRNA methyltransferase D (TrmD) in bacteria. The resultant modified nucleotide m1G37 positively regulates the aminoacylation of the tRNA, and simultaneously functions to prevent the +1 frameshift on the ribosome
physiological function
he N1-atom of guanosine at position 37 in transfer RNA (tRNA) is methylated by tRNA methyltransferase 5 (Trm5) in eukaryotes and archaea, and by tRNA methyltransferase D (TrmD) in bacteria. The resultant modified nucleotide m1G37 positively regulates the aminoacylation of the tRNA, and simultaneously functions to prevent the +1 frameshift on the ribosome
physiological function
he N1-atom of guanosine at position 37 in transfer RNA (tRNA) is methylated by tRNA methyltransferase 5 (Trm5) in eukaryotes and archaea, and by tRNA methyltransferase D (TrmD) in bacteria. The resultant modified nucleotide m1G37 positively regulates the aminoacylation of the tRNA, and simultaneously functions to prevent the +1 frameshift on the ribosome
physiological function
he N1-atom of guanosine at position 37 in transfer RNA (tRNA) is methylated by tRNA methyltransferase 5 (Trm5) in eukaryotes and archaea, and by tRNA methyltransferase D (TrmD) in bacteria. The resultant modified nucleotide m1G37 positively regulates the aminoacylation of the tRNA, and simultaneously functions to prevent the +1 frameshift on the ribosome. Enzyme Trm5a performs the N1-methylation of tRNA G37, but in addition it also catalyzes the methylation of the C7-atom of 4-demethylwyosine, which is the intermediate of the wyosine derivatives found at position 37 of archaeal tRNAPhe
physiological function
in bacteria, TrmD is a methyl transferase that uses a knotted protein fold to catalyze methyl transfer from S-adenosyl methionine (AdoMet) to G37-tRNA. The product m1G37-tRNA is essential for life as a determinant to maintain protein synthesis reading-frame
physiological function
m1G37 tRNA methyltransferase TrmD catalyzes m1G formation at position 37 in many tRNA isoacceptors and is essential
physiological function
methylation is to the G37 base on the 3' side of the anticodon to generate m1G37-tRNA suppresses frameshift errors during protein synthesis and is therefore essential for cell growth in all three domains of life. This methylation is catalyzed by TrmD in bacteria and by Trm5 in eukaryotes and archaea. Although TrmD and Trm5 catalyze the same methylation reaction, kinetic analysis reveal that these two enzymes are unrelated to each other and are distinct in their reaction mechanism. Both TrmD and Trm5 are essential for cell growth, because their reaction product m1G37 occurring on the 3' side of the tRNA anticodon is necessary to suppress +1-frameshift errors on the ribosome
physiological function
methylation is to the G37 base on the 3' side of the anticodon to generate m1G37-tRNA suppresses frameshift errors during protein synthesis and is therefore essential for cell growth in all three domains of life. This methylation is catalyzed by TrmD in bacteria and by Trm5 in eukaryotes and archaea. Although TrmD and Trm5 catalyze the same methylation reaction, kinetic analysis reveal that these two enzymes are unrelated to each other and are distinct in their reaction mechanism. Both TrmD and Trm5 are essential for cell growth, because their reaction product m1G37 occurring on the 3' side of the tRNA anticodon is necessary to suppress +1-frameshift errors on the ribosome
physiological function
methylation is to the G37 base on the 3' side of the anticodon to generate m1G37-tRNA suppresses frameshift errors during protein synthesis and is therefore essential for cell growth in all three domains of life. This methylation is catalyzed by TrmD in bacteria and by Trm5 in eukaryotes and archaea. Although TrmD and Trm5 catalyze the same methylation reaction, kinetic analysis reveal that these two enzymes are unrelated to each other and are distinct in their reaction mechanism. Both TrmD and Trm5 are essential for cell growth, because their reaction product m1G37 occurring on the 3' side of the tRNA anticodon is necessary to suppress +1-frameshift errors on the ribosome
physiological function
methylation is to the G37 base on the 3' side of the anticodon to generate m1G37-tRNA suppresses frameshift errors during protein synthesis and is therefore essential for cell growth in all three domains of life. This methylation is catalyzed by TrmD in bacteria and by Trm5 in eukaryotes and archaea. Although TrmD and Trm5 catalyze the same methylation reaction, kinetic analysis reveal that these two enzymes are unrelated to each other and are distinct in their reaction mechanism. Both TrmD and Trm5 are essential for cell growth, because their reaction product m1G37 occurring on the 3' side of the tRNA anticodon is necessary to suppress +1-frameshift errors on the ribosome
physiological function
methylation of guanine at position 37 in RNA is critical for bacterial growth, as this reaction is essential for preventing reading frame shifts during translation and therefore for maintaining the fidelity of protein synthesis. This methylation is catalyzed by the tRNA (guanine37-N1)-methyltransferase (TrmD). TrmD uses S-adenosyl-l-methionine (SAM) as a cofactor and transfers the methyl group to the N1 atom of G37 in tRNA. Bacterial tRNA (guanine37-N1)-methyltransferase (TrmD) plays important roles in translation. and is critical for growth of Pseudomonas aeruginosa
physiological function
modified nucleosides on tRNA are critical for decoding processes and protein translation. tRNAs can be modified through 1-methylguanosine (m1G) on position 37, a function mediated by Trm5 homologues. Enzyme AtTrm5a catalyses 1-methylguanosine and 1-methylinosine formation on tRNAs and is important for vegetative and reproductive growth in Arabidopsis thaliana. The importance of m1G37 is highlighted by its direct function in the decoding process
physiological function
the methyltransferase Trm5a from Pyrococcus abyssi (PaTrm5a) plays a key role in this hypermodification process in generating m1G37 (EC 2.1.1.228) and imG2 (EC 2.1.1.282), two products of the wyosine biosynthetic pathway, through two methyl transfers to distinct substrates
physiological function
the N1-methylation of G37 on the 3'-side of the tRNA anticodon, generating m1G37, which as a single methylated nucleobase is not only essential for life but is also conserved in evolution present in all three domains of life. Codon-specific translation by m1G37 methylation of tRNA, mechanism, overview. Maintenance of protein synthesis reading frame by m1G37-tRNA. The maintenance of protein synthesis reading frame in normal cellular conditions is achieved with unexpectedly high fidelity. Due to the dependence on m1G37 for cell survival, Trm5 is required for growth in the single-cell eukaryote Saccharomyces cerevisiae, where it provides the important role of preventing mis-charging of tRNA
physiological function
the N1-methylation of G37 on the 3'-side of the tRNA anticodon, generating m1G37, which as a single methylated nucleobase is not only essential for life but is also conserved in evolution present in all three domains of life. Codon-specific translation by m1G37 methylation of tRNA, mechanism, overview. Maintenance of protein synthesis reading frame by m1G37-tRNA. The maintenance of protein synthesis reading frame in normal cellular conditions is achieved with unexpectedly high fidelity. Due to the dependence on m1G37 for cell survival, TrmD is required for growth in several bacterial species, including Escherichia coli and Salmonella
physiological function
the N1-methylation of G37 on the 3'-side of the tRNA anticodon, generating m1G37, which as a single methylated nucleobase is not only essential for life but is also conserved in evolution present in all three domains of life. Codon-specific translation by m1G37 methylation of tRNA, mechanism, overview. Maintenance of protein synthesis reading frame by m1G37-tRNA. The maintenance of protein synthesis reading frame in normal cellular conditions is achieved with unexpectedly high fidelity. Due to the dependence on m1G37 for cell survival, TrmD is required for growth in several bacterial species, including Escherichia coli and Salmonella
physiological function
tricyclic wyosine derivatives are found at position 37 of eukaryotic and archaeal tRNAPhe. In Archaea, the intermediate imG-14 is targeted by three different enzymes that catalyze the formation of yW-86, imG, and imG2. Methyltransferase aTrm5a/Taw22 likely catalyzes two distinct reactions: N1-methylation of guanosine to yield m1G (EC 2.1.1.228), and C7-methylation of imG-14 to yield imG2 (EC 2.1.1.282)
physiological function
tricyclic wyosine derivatives are found at position 37 of eukaryotic and archaeal tRNAPhe. In Archaea, the intermediate imG-14 is targeted by three different enzymes that catalyze the formation of yW-86, imG, and imG2. Methyltransferase aTrm5a/Taw22 likely catalyzes two distinct reactions: N1-methylation of guanosine to yield m1G (EC 2.1.1.228), and C7-methylation of imG-14 to yield imG2 (EC 2.1.1.282)
physiological function
-
TrmD catalyzes the transfer of a methyl group from S-adenosyl methionine (SAM) to the N1 position of guanosine 37 in bacterial tRNA when preceded by another guanosine in the sequence. The addition of this marker immediately adjacent to the anticodon acts to improve reading frame maintenance on the ribosome, preventing frameshift errors that would result in truncated and inactive peptides. TrmD is essential for growth in a range of bacterial species from Staphylococcus aureus and Pseudomonas aeruginosa to mycobacteria, including Mycobacterium tuberculosis (Mtb) and Mycobacterium abscessus (Mab)
physiological function
tRNA methyltransferase Trm5 catalyses the transfer of a methyl group from S-adenosyl-L-methionine to G37 in eukaryotes and archaea. The N1-methylated guanosine is the product of the initial step of the wyosine hypermodification, which is essential for the maintenance of the reading frame during translation. As a unique member of this enzyme family, Trm5a from Pyrococcus abyssi (PaTrm5a) catalyses not only the methylation of N1, but also the further methylation of C7 on 4-demethylwyosine at position 37 to produce isowyosine
physiological function
while the greatest majority of the tRNA modifying enzymes are nonessential for life, acting for example as a chaperone to modulate tRNA activity, a very small number of these enzymes are absolutely required for cell growth and survival. TrmD is an example of one of these essential enzymes, responsible for methyl transfer from AdoMet to the N1 position of the G37 base to synthesize m1G37 on tRNA. The methylated m1G37 is on the 3?-side of the anticodon, and it is necessary for suppressing tRNA frameshifting during protein synthesis on the ribosome TrmD is an S-adenosyl methionine (AdoMet)-dependent methyl transferase that synthesizes the methylated m1G37 in tRNA. TrmD is specific to and essential for bacterial growth, and it is fundamentally distinct from its eukaryotic and archaeal counterpart Trm5. TrmD is unusual by using a topological protein knot to bind AdoMet. Despite its restricted mobility, the TrmD knot has complex dynamics necessary to transmit the signal of AdoMet binding to promote tRNA binding and methyl transfer. TrmD is unique among AdoMet-dependent methyl transferases in that it requires Mg2+ in the catalytic mechanism. The Mg2+ dependence is important for regulating Mg2+ transport to Salmonella for survival of the pathogen in the host cell. The trefoil knot of TrmD is required for the catalytic mechanism in three ways. Synthesis of m1G37-tRNA by TrmD is a posttranscriptional event
physiological function
while the greatest majority of the tRNA modifying enzymes are nonessential for life, acting for example as a chaperone to modulate tRNA activity, a very small number of these enzymes are absolutely required for cell growth and survival. TrmD is an example of one of these essential enzymes, responsible for methyl transfer from AdoMet to the N1 position of the G37 base to synthesize m1G37 on tRNA. TrmD is an S-adenosyl methionine (AdoMet)-dependent methyl transferase that synthesizes the methylated m1G37 in tRNA. TrmD is specific to and essential for bacterial growth, and it is fundamentally distinct from its eukaryotic and archaeal counterpart Trm5. TrmD is unusual by using a topological protein knot to bind AdoMet. Despite its restricted mobility, the TrmD knot has complex dynamics necessary to transmit the signal of AdoMet binding to promote tRNA binding and methyl transfer. TrmD is unique among AdoMet-dependent methyl transferases in that it requires Mg2+ in the catalytic mechanism
physiological function
while the greatest majority of the tRNA modifying enzymes are nonessential for life, acting for example as a chaperone to modulate tRNA activity, a very small number of these enzymes are absolutely required for cell growth and survival. TrmD is an example of one of these essential enzymes, responsible for methyl transfer from AdoMet to the N1 position of the G37 base to synthesize m1G37 on tRNA. TrmD is an S-adenosyl methionine (AdoMet)-dependent methyl transferase that synthesizes the methylated m1G37 in tRNA. TrmD is specific to and essential for bacterial growth, and it is fundamentally distinct from its eukaryotic and archaeal counterpart Trm5. TrmD is unusual by using a topological protein knot to bind AdoMet. Despite its restricted mobility, the TrmD knot has complex dynamics necessary to transmit the signal of AdoMet binding to promote tRNA binding and methyl transfer. TrmD is unique among AdoMet-dependent methyl transferases in that it requires Mg2+ in the catalytic mechanism. The trefoil knot of TrmD is required for the catalytic mechanism in three ways. Synthesis of m1G37-tRNA by TrmD is a posttranscriptional event
physiological function
while the greatest majority of the tRNA modifying enzymes are nonessential for life, acting for example as a chaperone to modulate tRNA activity, a very small number of these enzymes are absolutely required for cell growth and survival. TrmD is an example of one of these essential enzymes, responsible for methyl transfer from AdoMet to the N1 position of the G37 base to synthesize m1G37 on tRNA. TrmD is an S-adenosyl methionine (AdoMet)-dependent methyl transferase that synthesizes the methylated m1G37 in tRNA. TrmD is specific to and essential for bacterial growth, and it is fundamentally distinct from its eukaryotic and archaeal counterpart Trm5. TrmD is unusual by using a topological protein knot to bind AdoMet. Despite its restricted mobility, the TrmD knot has complex dynamics necessary to transmit the signal of AdoMet binding to promote tRNA binding and methyl transfer. TrmD is unique among AdoMet-dependent methyl transferases in that it requires Mg2+ in the catalytic mechanism. The trefoil knot of TrmD is required for the catalytic mechanism in three ways. Synthesis of m1G37-tRNA by TrmD is a posttranscriptional event
physiological function
-
he N1-atom of guanosine at position 37 in transfer RNA (tRNA) is methylated by tRNA methyltransferase 5 (Trm5) in eukaryotes and archaea, and by tRNA methyltransferase D (TrmD) in bacteria. The resultant modified nucleotide m1G37 positively regulates the aminoacylation of the tRNA, and simultaneously functions to prevent the +1 frameshift on the ribosome. Enzyme Trm5a performs the N1-methylation of tRNA G37, but in addition it also catalyzes the methylation of the C7-atom of 4-demethylwyosine, which is the intermediate of the wyosine derivatives found at position 37 of archaeal tRNAPhe
-
physiological function
-
tricyclic wyosine derivatives are found at position 37 of eukaryotic and archaeal tRNAPhe. In Archaea, the intermediate imG-14 is targeted by three different enzymes that catalyze the formation of yW-86, imG, and imG2. Methyltransferase aTrm5a/Taw22 likely catalyzes two distinct reactions: N1-methylation of guanosine to yield m1G (EC 2.1.1.228), and C7-methylation of imG-14 to yield imG2 (EC 2.1.1.282)
-
physiological function
-
while the greatest majority of the tRNA modifying enzymes are nonessential for life, acting for example as a chaperone to modulate tRNA activity, a very small number of these enzymes are absolutely required for cell growth and survival. TrmD is an example of one of these essential enzymes, responsible for methyl transfer from AdoMet to the N1 position of the G37 base to synthesize m1G37 on tRNA. The methylated m1G37 is on the 3?-side of the anticodon, and it is necessary for suppressing tRNA frameshifting during protein synthesis on the ribosome TrmD is an S-adenosyl methionine (AdoMet)-dependent methyl transferase that synthesizes the methylated m1G37 in tRNA. TrmD is specific to and essential for bacterial growth, and it is fundamentally distinct from its eukaryotic and archaeal counterpart Trm5. TrmD is unusual by using a topological protein knot to bind AdoMet. Despite its restricted mobility, the TrmD knot has complex dynamics necessary to transmit the signal of AdoMet binding to promote tRNA binding and methyl transfer. TrmD is unique among AdoMet-dependent methyl transferases in that it requires Mg2+ in the catalytic mechanism. The Mg2+ dependence is important for regulating Mg2+ transport to Salmonella for survival of the pathogen in the host cell. The trefoil knot of TrmD is required for the catalytic mechanism in three ways. Synthesis of m1G37-tRNA by TrmD is a posttranscriptional event
-
physiological function
-
the N1-methylation of G37 on the 3'-side of the tRNA anticodon, generating m1G37, which as a single methylated nucleobase is not only essential for life but is also conserved in evolution present in all three domains of life. Codon-specific translation by m1G37 methylation of tRNA, mechanism, overview. Maintenance of protein synthesis reading frame by m1G37-tRNA. The maintenance of protein synthesis reading frame in normal cellular conditions is achieved with unexpectedly high fidelity. Due to the dependence on m1G37 for cell survival, TrmD is required for growth in several bacterial species, including Escherichia coli and Salmonella
-
physiological function
-
he N1-atom of guanosine at position 37 in transfer RNA (tRNA) is methylated by tRNA methyltransferase 5 (Trm5) in eukaryotes and archaea, and by tRNA methyltransferase D (TrmD) in bacteria. The resultant modified nucleotide m1G37 positively regulates the aminoacylation of the tRNA, and simultaneously functions to prevent the +1 frameshift on the ribosome
-
physiological function
-
methylation is to the G37 base on the 3' side of the anticodon to generate m1G37-tRNA suppresses frameshift errors during protein synthesis and is therefore essential for cell growth in all three domains of life. This methylation is catalyzed by TrmD in bacteria and by Trm5 in eukaryotes and archaea. Although TrmD and Trm5 catalyze the same methylation reaction, kinetic analysis reveal that these two enzymes are unrelated to each other and are distinct in their reaction mechanism. Both TrmD and Trm5 are essential for cell growth, because their reaction product m1G37 occurring on the 3' side of the tRNA anticodon is necessary to suppress +1-frameshift errors on the ribosome
-
physiological function
-
he N1-atom of guanosine at position 37 in transfer RNA (tRNA) is methylated by tRNA methyltransferase 5 (Trm5) in eukaryotes and archaea, and by tRNA methyltransferase D (TrmD) in bacteria. The resultant modified nucleotide m1G37 positively regulates the aminoacylation of the tRNA, and simultaneously functions to prevent the +1 frameshift on the ribosome
-
physiological function
-
methylation is to the G37 base on the 3' side of the anticodon to generate m1G37-tRNA suppresses frameshift errors during protein synthesis and is therefore essential for cell growth in all three domains of life. This methylation is catalyzed by TrmD in bacteria and by Trm5 in eukaryotes and archaea. Although TrmD and Trm5 catalyze the same methylation reaction, kinetic analysis reveal that these two enzymes are unrelated to each other and are distinct in their reaction mechanism. Both TrmD and Trm5 are essential for cell growth, because their reaction product m1G37 occurring on the 3' side of the tRNA anticodon is necessary to suppress +1-frameshift errors on the ribosome
-
physiological function
-
he N1-atom of guanosine at position 37 in transfer RNA (tRNA) is methylated by tRNA methyltransferase 5 (Trm5) in eukaryotes and archaea, and by tRNA methyltransferase D (TrmD) in bacteria. The resultant modified nucleotide m1G37 positively regulates the aminoacylation of the tRNA, and simultaneously functions to prevent the +1 frameshift on the ribosome
-
physiological function
-
methylation is to the G37 base on the 3' side of the anticodon to generate m1G37-tRNA suppresses frameshift errors during protein synthesis and is therefore essential for cell growth in all three domains of life. This methylation is catalyzed by TrmD in bacteria and by Trm5 in eukaryotes and archaea. Although TrmD and Trm5 catalyze the same methylation reaction, kinetic analysis reveal that these two enzymes are unrelated to each other and are distinct in their reaction mechanism. Both TrmD and Trm5 are essential for cell growth, because their reaction product m1G37 occurring on the 3' side of the tRNA anticodon is necessary to suppress +1-frameshift errors on the ribosome
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physiological function
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while the greatest majority of the tRNA modifying enzymes are nonessential for life, acting for example as a chaperone to modulate tRNA activity, a very small number of these enzymes are absolutely required for cell growth and survival. TrmD is an example of one of these essential enzymes, responsible for methyl transfer from AdoMet to the N1 position of the G37 base to synthesize m1G37 on tRNA. The methylated m1G37 is on the 3?-side of the anticodon, and it is necessary for suppressing tRNA frameshifting during protein synthesis on the ribosome TrmD is an S-adenosyl methionine (AdoMet)-dependent methyl transferase that synthesizes the methylated m1G37 in tRNA. TrmD is specific to and essential for bacterial growth, and it is fundamentally distinct from its eukaryotic and archaeal counterpart Trm5. TrmD is unusual by using a topological protein knot to bind AdoMet. Despite its restricted mobility, the TrmD knot has complex dynamics necessary to transmit the signal of AdoMet binding to promote tRNA binding and methyl transfer. TrmD is unique among AdoMet-dependent methyl transferases in that it requires Mg2+ in the catalytic mechanism. The Mg2+ dependence is important for regulating Mg2+ transport to Salmonella for survival of the pathogen in the host cell. The trefoil knot of TrmD is required for the catalytic mechanism in three ways. Synthesis of m1G37-tRNA by TrmD is a posttranscriptional event
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physiological function
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the N1-methylation of G37 on the 3'-side of the tRNA anticodon, generating m1G37, which as a single methylated nucleobase is not only essential for life but is also conserved in evolution present in all three domains of life. Codon-specific translation by m1G37 methylation of tRNA, mechanism, overview. Maintenance of protein synthesis reading frame by m1G37-tRNA. The maintenance of protein synthesis reading frame in normal cellular conditions is achieved with unexpectedly high fidelity. Due to the dependence on m1G37 for cell survival, TrmD is required for growth in several bacterial species, including Escherichia coli and Salmonella
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physiological function
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he N1-atom of guanosine at position 37 in transfer RNA (tRNA) is methylated by tRNA methyltransferase 5 (Trm5) in eukaryotes and archaea, and by tRNA methyltransferase D (TrmD) in bacteria. The resultant modified nucleotide m1G37 positively regulates the aminoacylation of the tRNA, and simultaneously functions to prevent the +1 frameshift on the ribosome
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physiological function
-
methylation is to the G37 base on the 3' side of the anticodon to generate m1G37-tRNA suppresses frameshift errors during protein synthesis and is therefore essential for cell growth in all three domains of life. This methylation is catalyzed by TrmD in bacteria and by Trm5 in eukaryotes and archaea. Although TrmD and Trm5 catalyze the same methylation reaction, kinetic analysis reveal that these two enzymes are unrelated to each other and are distinct in their reaction mechanism. Both TrmD and Trm5 are essential for cell growth, because their reaction product m1G37 occurring on the 3' side of the tRNA anticodon is necessary to suppress +1-frameshift errors on the ribosome
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physiological function
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he N1-atom of guanosine at position 37 in transfer RNA (tRNA) is methylated by tRNA methyltransferase 5 (Trm5) in eukaryotes and archaea, and by tRNA methyltransferase D (TrmD) in bacteria. The resultant modified nucleotide m1G37 positively regulates the aminoacylation of the tRNA, and simultaneously functions to prevent the +1 frameshift on the ribosome
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physiological function
-
methylation is to the G37 base on the 3' side of the anticodon to generate m1G37-tRNA suppresses frameshift errors during protein synthesis and is therefore essential for cell growth in all three domains of life. This methylation is catalyzed by TrmD in bacteria and by Trm5 in eukaryotes and archaea. Although TrmD and Trm5 catalyze the same methylation reaction, kinetic analysis reveal that these two enzymes are unrelated to each other and are distinct in their reaction mechanism. Both TrmD and Trm5 are essential for cell growth, because their reaction product m1G37 occurring on the 3' side of the tRNA anticodon is necessary to suppress +1-frameshift errors on the ribosome
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physiological function
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the N1-methylation of G37 on the 3'-side of the tRNA anticodon, generating m1G37, which as a single methylated nucleobase is not only essential for life but is also conserved in evolution present in all three domains of life. Codon-specific translation by m1G37 methylation of tRNA, mechanism, overview. Maintenance of protein synthesis reading frame by m1G37-tRNA. The maintenance of protein synthesis reading frame in normal cellular conditions is achieved with unexpectedly high fidelity. Due to the dependence on m1G37 for cell survival, Trm5 is required for growth in the single-cell eukaryote Saccharomyces cerevisiae, where it provides the important role of preventing mis-charging of tRNA
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physiological function
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the m1G37-modified tRNA functions properly to prevent +1 frameshift errors on the ribosome
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physiological function
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he N1-atom of guanosine at position 37 in transfer RNA (tRNA) is methylated by tRNA methyltransferase 5 (Trm5) in eukaryotes and archaea, and by tRNA methyltransferase D (TrmD) in bacteria. The resultant modified nucleotide m1G37 positively regulates the aminoacylation of the tRNA, and simultaneously functions to prevent the +1 frameshift on the ribosome
-
physiological function
-
methylation is to the G37 base on the 3' side of the anticodon to generate m1G37-tRNA suppresses frameshift errors during protein synthesis and is therefore essential for cell growth in all three domains of life. This methylation is catalyzed by TrmD in bacteria and by Trm5 in eukaryotes and archaea. Although TrmD and Trm5 catalyze the same methylation reaction, kinetic analysis reveal that these two enzymes are unrelated to each other and are distinct in their reaction mechanism. Both TrmD and Trm5 are essential for cell growth, because their reaction product m1G37 occurring on the 3' side of the tRNA anticodon is necessary to suppress +1-frameshift errors on the ribosome
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physiological function
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he N1-atom of guanosine at position 37 in transfer RNA (tRNA) is methylated by tRNA methyltransferase 5 (Trm5) in eukaryotes and archaea, and by tRNA methyltransferase D (TrmD) in bacteria. The resultant modified nucleotide m1G37 positively regulates the aminoacylation of the tRNA, and simultaneously functions to prevent the +1 frameshift on the ribosome
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physiological function
-
methylation is to the G37 base on the 3' side of the anticodon to generate m1G37-tRNA suppresses frameshift errors during protein synthesis and is therefore essential for cell growth in all three domains of life. This methylation is catalyzed by TrmD in bacteria and by Trm5 in eukaryotes and archaea. Although TrmD and Trm5 catalyze the same methylation reaction, kinetic analysis reveal that these two enzymes are unrelated to each other and are distinct in their reaction mechanism. Both TrmD and Trm5 are essential for cell growth, because their reaction product m1G37 occurring on the 3' side of the tRNA anticodon is necessary to suppress +1-frameshift errors on the ribosome
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physiological function
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methylation of guanine at position 37 in RNA is critical for bacterial growth, as this reaction is essential for preventing reading frame shifts during translation and therefore for maintaining the fidelity of protein synthesis. This methylation is catalyzed by the tRNA (guanine37-N1)-methyltransferase (TrmD). TrmD uses S-adenosyl-l-methionine (SAM) as a cofactor and transfers the methyl group to the N1 atom of G37 in tRNA. Bacterial tRNA (guanine37-N1)-methyltransferase (TrmD) plays important roles in translation. and is critical for growth of Pseudomonas aeruginosa
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physiological function
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m1G37 tRNA methyltransferase TrmD catalyzes m1G formation at position 37 in many tRNA isoacceptors and is essential
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physiological function
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he N1-atom of guanosine at position 37 in transfer RNA (tRNA) is methylated by tRNA methyltransferase 5 (Trm5) in eukaryotes and archaea, and by tRNA methyltransferase D (TrmD) in bacteria. The resultant modified nucleotide m1G37 positively regulates the aminoacylation of the tRNA, and simultaneously functions to prevent the +1 frameshift on the ribosome
-
physiological function
-
methylation is to the G37 base on the 3' side of the anticodon to generate m1G37-tRNA suppresses frameshift errors during protein synthesis and is therefore essential for cell growth in all three domains of life. This methylation is catalyzed by TrmD in bacteria and by Trm5 in eukaryotes and archaea. Although TrmD and Trm5 catalyze the same methylation reaction, kinetic analysis reveal that these two enzymes are unrelated to each other and are distinct in their reaction mechanism. Both TrmD and Trm5 are essential for cell growth, because their reaction product m1G37 occurring on the 3' side of the tRNA anticodon is necessary to suppress +1-frameshift errors on the ribosome
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physiological function
Trametes pubescens 927 / 4 GUTat10.1 / TREU927
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TRM5 is responsible for m1G37 formation, m1G37 formation in mitochondria is important for respiration, and TbTRM5 is important for mitochondrial protein synthesis and biogenesis. Mitochondrial TRM5 may be needed to mature unmethylated tRNAs that reach the mitochondria and that can pose a problem for translational fidelity, lack of import specificity between some fully matured and potentially defective tRNA species
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physiological function
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he N1-atom of guanosine at position 37 in transfer RNA (tRNA) is methylated by tRNA methyltransferase 5 (Trm5) in eukaryotes and archaea, and by tRNA methyltransferase D (TrmD) in bacteria. The resultant modified nucleotide m1G37 positively regulates the aminoacylation of the tRNA, and simultaneously functions to prevent the +1 frameshift on the ribosome
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physiological function
-
methylation is to the G37 base on the 3' side of the anticodon to generate m1G37-tRNA suppresses frameshift errors during protein synthesis and is therefore essential for cell growth in all three domains of life. This methylation is catalyzed by TrmD in bacteria and by Trm5 in eukaryotes and archaea. Although TrmD and Trm5 catalyze the same methylation reaction, kinetic analysis reveal that these two enzymes are unrelated to each other and are distinct in their reaction mechanism. Both TrmD and Trm5 are essential for cell growth, because their reaction product m1G37 occurring on the 3' side of the tRNA anticodon is necessary to suppress +1-frameshift errors on the ribosome
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additional information
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S-adenosyl-methionine-dependent m1G37-tRNA methyltransferases rapidly screen tRNA by direct recognition of G37 in order to monitor the global state of m1G37-tRNA
additional information
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S-adenosyl-methionine-dependent m1G37-tRNA methyltransferases rapidly screen tRNA by direct recognition of G37 in order to monitor the global state of m1G37-tRNA
additional information
active-site structure and overall structure analysis, molecular modeling using structure PdB ID 2ZZN, overview
additional information
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active-site structure and overall structure analysis, molecular modeling using structure PdB ID 2ZZN, overview
additional information
in the cross-subunit active site, S-adenosyl-L-methionine is bound to the trefoil knot fold in the N-terminal domain, whereas the target G37 is predicted to bind to the flexible linker
additional information
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in the cross-subunit active site, S-adenosyl-L-methionine is bound to the trefoil knot fold in the N-terminal domain, whereas the target G37 is predicted to bind to the flexible linker
additional information
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three-dimensional enzyme model, overview
additional information
active site structure in complex with S-adenosyl-L-methionine, overview
additional information
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active site structure in complex with S-adenosyl-L-methionine, overview
additional information
Aquifex aeolicus TrmD can methylate G37 in the A36G37 sequence, showing that purine36 is a positive determinant for the TrmD. Formation of a disulfide bond between the two subunits stabilizes the dimer structure of Aquifex aeolicus TrmD and is required for enzymatic activity at high temperatures
additional information
backbone NMR resonance assignments for the full length TrmD protein of Pseudomonas aeruginosa and secondary structure analysis
additional information
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backbone NMR resonance assignments for the full length TrmD protein of Pseudomonas aeruginosa and secondary structure analysis
additional information
codon-specific translation in Mg2+ homeostasis, overview. Mg2+ homeostasis in Salmonella is maintained by the membrane-bound two-component system PhoPQ sensing of the external low Mg2+, which activates transcription of the major transporter gene mgtA. Transcription of mgtA is determined by ribosomal translation of the 5'-leader ORF, which contains several m1G37-dependent Pro codons
additional information
enzyme structure comparisons
additional information
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enzyme structure comparisons
additional information
evaluation of the kinetic assays that are used to reveal the distinction between TrmD and Trm5, overview
additional information
evaluation of the kinetic assays that are used to reveal the distinction between TrmD and Trm5, overview
additional information
evaluation of the kinetic assays that are used to reveal the distinction between TrmD and Trm5, overview
additional information
evaluation of the kinetic assays that are used to reveal the distinction between TrmD and Trm5, overview
additional information
structure comparison of the Pyrococcus abyssii Trm5a enzyme structure (PDB IDs 5HJJ and 5WT1) with the structure of its orthologue Trm5b (MjTrm5b, PDB IDs 2YX1 and 3AY0) from Methanococcus jannaschii, overview
additional information
structure comparison of the Pyrococcus abyssii Trm5a enzyme structure (PDB IDs 5HJJ and 5WT1) with the structure of its orthologue Trm5b (MjTrm5b, PDB IDs 2YX1 and 3AY0) from Methanococcus jannaschii, overview
additional information
the m1G37 methylation by TrmD does not need any other prior modification, aminoacylation, or even CCA addition to tRNA. Transient nature of Mg2+ is consistent with the proposed catalytic mechanism involving G37-tRNA. In this mechanism, D169 is the general base to abstract the N1 proton from G37, while the deprotonation is accompanied by developing electron density on the O6 of G37. The developing negative charge on O6 of G37 is stabilized through coordination with Mg2+ and by hydrogen-bond interaction with the side chain of R154. The charge stabilization of O6 in turn facilitates Mg2+ to coordinate with the general base D169 and to help it to align more properly for proton abstraction. The activated N1 nucleophile is then poised for nucleophilic attack on the sulfonium center of AdoMet, resulting in synthesis of m1G37-tRNA and release of AdoHcy. The rate-limiting step is assigned to the action of D169, rather than to the protonation of the leaving group, due to the importance of D169 and the increase of activity as the proton concentration is lowered
additional information
the m1G37 methylation by TrmD does not need any other prior modification, aminoacylation, or even CCA addition to tRNA. Transient nature of Mg2+ is consistent with the proposed catalytic mechanism involving G37-tRNA. In this mechanism, D169 is the general base to abstract the N1 proton from G37, while the deprotonation is accompanied by developing electron density on the O6 of G37. The developing negative charge on O6 of G37 is stabilized through coordination with Mg2+ and by hydrogen-bond interaction with the side chain of R154. The charge stabilization of O6 in turn facilitates Mg2+ to coordinate with the general base D169 and to help it to align more properly for proton abstraction. The activated N1 nucleophile is then poised for nucleophilic attack on the sulfonium center of AdoMet, resulting in synthesis of m1G37-tRNA and release of AdoHcy. The rate-limiting step is assigned to the action of D169, rather than to the protonation of the leaving group, due to the importance of D169 and the increase of activity as the proton concentration is lowered
additional information
the m1G37 methylation by TrmD does not need any other prior modification, aminoacylation, or even CCA addition to tRNA. Transient nature of Mg2+ is consistent with the proposed catalytic mechanism involving G37-tRNA. In this mechanism, D169 is the general base to abstract the N1 proton from G37, while the deprotonation is accompanied by developing electron density on the O6 of G37. The developing negative charge on O6 of G37 is stabilized through coordination with Mg2+ and by hydrogen-bond interaction with the side chain of R154. The charge stabilization of O6 in turn facilitates Mg2+ to coordinate with the general base D169 and to help it to align more properly for proton abstraction. The activated N1 nucleophile is then poised for nucleophilic attack on the sulfonium center of AdoMet, resulting in synthesis of m1G37-tRNA and release of AdoHcy. The rate-limiting step is assigned to the action of D169, rather than to the protonation of the leaving group, due to the importance of D169 and the increase of activity as the proton concentration is lowered
additional information
the m1G37 methylation by TrmD does not need any other prior modification, aminoacylation, or even CCA addition to tRNA. Transient nature of Mg2+ is consistent with the proposed catalytic mechanism involving G37-tRNA. In this mechanism, D169 is the general base to abstract the N1 proton from G37, while the deprotonation is accompanied by developing electron density on the O6 of G37. The developing negative charge on O6 of G37 is stabilized through coordination with Mg2+ and by hydrogen-bond interaction with the side chain of R154. The charge stabilization of O6 in turn facilitates Mg2+ to coordinate with the general base D169 and to help it to align more properly for proton abstraction. The activated N1 nucleophile is then poised for nucleophilic attack on the sulfonium center of AdoMet, resulting in synthesis of m1G37-tRNA and release of AdoHcy. The rate-limiting step is assigned to the action of D169, rather than to the protonation of the leaving group, due to the importance of D169 and the increase of activity as the proton concentration is lowered
additional information
the N-terminal domain (NTD) contains the S-adenosyl-L-methionine (SAM) binding region, this domain binds to SAM, S-adenosyl-L-homocysteine (SAH), and active-site inhibitors such as the SAM analogue sinefungin. Metabolites such as SAM, SAH and MTA enhance the thermostability of NTD by increasing its melting temperature (Tm), dynamics and ligand binding of NTD
additional information
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the N-terminal domain (NTD) contains the S-adenosyl-L-methionine (SAM) binding region, this domain binds to SAM, S-adenosyl-L-homocysteine (SAH), and active-site inhibitors such as the SAM analogue sinefungin. Metabolites such as SAM, SAH and MTA enhance the thermostability of NTD by increasing its melting temperature (Tm), dynamics and ligand binding of NTD
additional information
the structurally constrained TrmD knot is required for its catalytic activity. The TrmD knot has complex internal movements that respond to AdoMet binding and signaling. Most of the signaling propagates the free energy of AdoMet binding to stabilize tRNA binding and to assemble the active site. Principles of knots as an organized structure that captures the free energies of substrate binding to facilitate catalysis, overview
additional information
Trm5 consists of three structural domains: domain 1 (D1), domain 2 (D2), and domain 3 (D3). D1 corresponds to the less-conserved region among Trm5 enzymes from all species, while D2 corresponds to the conserved region. The structure of D2 shares homology with that of TYW2, the tRNA-wybutosine (yW) synthesizing enzyme-2. D3 corresponds to the Rossmann-fold domain containing the AdoMet binding site, and is conserved among the class-I MTases. The D2-D3 fragment alone possesses methyl-transfer activity comparable to that of the full-length enzyme, although the presence of D1 lowers and enhances the KM and kcat values (the Michaelis and catalytic rate constants, respectively, in the Michaelis-Menten equation) for tRNA, respectively, as compared to the D2-D3 fragment. Function of D1, overview. The interaction between the outer-corner of the tRNA and Trm5 D1 is essential to confer sufficiently robust affinity for the tRNA at physiological temperatures
additional information
Trm5 consists of three structural domains: domain 1 (D1), domain 2 (D2), and domain 3 (D3). D1 corresponds to the less-conserved region among Trm5 enzymes from all species, while D2 corresponds to the conserved region. The structures of Pyrococcus abyssi D1 and D2-D3 are similar to those of Methanocaldococcus jannaschii Trm5. The D1 of Pyrococcus abyssi Trm5a behaves independently from D2-D3, as suggested by the fluorescence resonance energy transfer (FRET) analysis. Function of D1, overview. The interaction between the outer-corner of the tRNA and Trm5 D1 is essential to confer sufficiently robust affinity for the tRNA at physiological temperatures
additional information
TrmD catalytic mechanism, overview. PaTrmD catalyzes the formation of m1G37 in tRNA by a ternary-complex mechanism in which tRNA and S-adenosyl-L-methionine can bind the protein independently. PaTrmD shares functionally important amino acid residues involved in cofactor binding (Ser93-Gly96, Gly118, Ile123, Ser137, Gly145), tRNA binding (Gly60, Gly64, Ser203-His206) and catalytic activity (Asp54, Arg159, and Asp174). Conformational changes are required to form a ternary complex with tRNA. PaTrmD catalyzes only the m1G modification in PA14 tRNAs that possess a G36G37 motif, the G36G37 motif is a substrate of PaTrmD. PaTrmD catalyzes m1G formation in synthetic tRNA substrates indicating that PaTrmD can use G36G37 containing tRNAs without other modifications as substrates. Enzyme structure modelling, overview
additional information
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TrmD catalytic mechanism, overview. PaTrmD catalyzes the formation of m1G37 in tRNA by a ternary-complex mechanism in which tRNA and S-adenosyl-L-methionine can bind the protein independently. PaTrmD shares functionally important amino acid residues involved in cofactor binding (Ser93-Gly96, Gly118, Ile123, Ser137, Gly145), tRNA binding (Gly60, Gly64, Ser203-His206) and catalytic activity (Asp54, Arg159, and Asp174). Conformational changes are required to form a ternary complex with tRNA. PaTrmD catalyzes only the m1G modification in PA14 tRNAs that possess a G36G37 motif, the G36G37 motif is a substrate of PaTrmD. PaTrmD catalyzes m1G formation in synthetic tRNA substrates indicating that PaTrmD can use G36G37 containing tRNAs without other modifications as substrates. Enzyme structure modelling, overview
additional information
TrmD consists of the N-terminal domain (NTD, the SPOUT domain) and the TrmD-specific C-terminal domain (CTD). These domains are connected by the interdomain linker. TrmD forms a homodimer, and the interdomain linkers are disordered in both monomers. The trefoil knot at the C-terminal region in the SPOUT domain provides the AdoMet-binding site. Structural changes of TrmD upon AdoMet accommodation. Structure-function analysis, overview
additional information
TrmD consists of the N-terminal domain (NTD, the SPOUT domain) and the TrmD-specific C-terminal domain (CTD). These domains are connected by the interdomain linker. TrmD forms a homodimer, and the interdomain linkers are disordered in both monomers. The trefoil knot at the C-terminal region in the SPOUT domain provides the AdoMet-binding site. Structural changes of TrmD upon AdoMet accommodation. Structure-function analysis, overview
additional information
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Trm5 consists of three structural domains: domain 1 (D1), domain 2 (D2), and domain 3 (D3). D1 corresponds to the less-conserved region among Trm5 enzymes from all species, while D2 corresponds to the conserved region. The structures of Pyrococcus abyssi D1 and D2-D3 are similar to those of Methanocaldococcus jannaschii Trm5. The D1 of Pyrococcus abyssi Trm5a behaves independently from D2-D3, as suggested by the fluorescence resonance energy transfer (FRET) analysis. Function of D1, overview. The interaction between the outer-corner of the tRNA and Trm5 D1 is essential to confer sufficiently robust affinity for the tRNA at physiological temperatures
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additional information
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the m1G37 methylation by TrmD does not need any other prior modification, aminoacylation, or even CCA addition to tRNA. Transient nature of Mg2+ is consistent with the proposed catalytic mechanism involving G37-tRNA. In this mechanism, D169 is the general base to abstract the N1 proton from G37, while the deprotonation is accompanied by developing electron density on the O6 of G37. The developing negative charge on O6 of G37 is stabilized through coordination with Mg2+ and by hydrogen-bond interaction with the side chain of R154. The charge stabilization of O6 in turn facilitates Mg2+ to coordinate with the general base D169 and to help it to align more properly for proton abstraction. The activated N1 nucleophile is then poised for nucleophilic attack on the sulfonium center of AdoMet, resulting in synthesis of m1G37-tRNA and release of AdoHcy. The rate-limiting step is assigned to the action of D169, rather than to the protonation of the leaving group, due to the importance of D169 and the increase of activity as the proton concentration is lowered
-
additional information
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codon-specific translation in Mg2+ homeostasis, overview. Mg2+ homeostasis in Salmonella is maintained by the membrane-bound two-component system PhoPQ sensing of the external low Mg2+, which activates transcription of the major transporter gene mgtA. Transcription of mgtA is determined by ribosomal translation of the 5'-leader ORF, which contains several m1G37-dependent Pro codons
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additional information
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Trm5 consists of three structural domains: domain 1 (D1), domain 2 (D2), and domain 3 (D3). D1 corresponds to the less-conserved region among Trm5 enzymes from all species, while D2 corresponds to the conserved region. The structure of D2 shares homology with that of TYW2, the tRNA-wybutosine (yW) synthesizing enzyme-2. D3 corresponds to the Rossmann-fold domain containing the AdoMet binding site, and is conserved among the class-I MTases. The D2-D3 fragment alone possesses methyl-transfer activity comparable to that of the full-length enzyme, although the presence of D1 lowers and enhances the KM and kcat values (the Michaelis and catalytic rate constants, respectively, in the Michaelis-Menten equation) for tRNA, respectively, as compared to the D2-D3 fragment. Function of D1, overview. The interaction between the outer-corner of the tRNA and Trm5 D1 is essential to confer sufficiently robust affinity for the tRNA at physiological temperatures
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additional information
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evaluation of the kinetic assays that are used to reveal the distinction between TrmD and Trm5, overview
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additional information
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TrmD consists of the N-terminal domain (NTD, the SPOUT domain) and the TrmD-specific C-terminal domain (CTD). These domains are connected by the interdomain linker. TrmD forms a homodimer, and the interdomain linkers are disordered in both monomers. The trefoil knot at the C-terminal region in the SPOUT domain provides the AdoMet-binding site. Structural changes of TrmD upon AdoMet accommodation. Structure-function analysis, overview
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additional information
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evaluation of the kinetic assays that are used to reveal the distinction between TrmD and Trm5, overview
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additional information
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structure comparison of the Pyrococcus abyssii Trm5a enzyme structure (PDB IDs 5HJJ and 5WT1) with the structure of its orthologue Trm5b (MjTrm5b, PDB IDs 2YX1 and 3AY0) from Methanococcus jannaschii, overview
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additional information
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Trm5 consists of three structural domains: domain 1 (D1), domain 2 (D2), and domain 3 (D3). D1 corresponds to the less-conserved region among Trm5 enzymes from all species, while D2 corresponds to the conserved region. The structure of D2 shares homology with that of TYW2, the tRNA-wybutosine (yW) synthesizing enzyme-2. D3 corresponds to the Rossmann-fold domain containing the AdoMet binding site, and is conserved among the class-I MTases. The D2-D3 fragment alone possesses methyl-transfer activity comparable to that of the full-length enzyme, although the presence of D1 lowers and enhances the KM and kcat values (the Michaelis and catalytic rate constants, respectively, in the Michaelis-Menten equation) for tRNA, respectively, as compared to the D2-D3 fragment. Function of D1, overview. The interaction between the outer-corner of the tRNA and Trm5 D1 is essential to confer sufficiently robust affinity for the tRNA at physiological temperatures
-
additional information
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evaluation of the kinetic assays that are used to reveal the distinction between TrmD and Trm5, overview
-
additional information
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the m1G37 methylation by TrmD does not need any other prior modification, aminoacylation, or even CCA addition to tRNA. Transient nature of Mg2+ is consistent with the proposed catalytic mechanism involving G37-tRNA. In this mechanism, D169 is the general base to abstract the N1 proton from G37, while the deprotonation is accompanied by developing electron density on the O6 of G37. The developing negative charge on O6 of G37 is stabilized through coordination with Mg2+ and by hydrogen-bond interaction with the side chain of R154. The charge stabilization of O6 in turn facilitates Mg2+ to coordinate with the general base D169 and to help it to align more properly for proton abstraction. The activated N1 nucleophile is then poised for nucleophilic attack on the sulfonium center of AdoMet, resulting in synthesis of m1G37-tRNA and release of AdoHcy. The rate-limiting step is assigned to the action of D169, rather than to the protonation of the leaving group, due to the importance of D169 and the increase of activity as the proton concentration is lowered
-
additional information
-
codon-specific translation in Mg2+ homeostasis, overview. Mg2+ homeostasis in Salmonella is maintained by the membrane-bound two-component system PhoPQ sensing of the external low Mg2+, which activates transcription of the major transporter gene mgtA. Transcription of mgtA is determined by ribosomal translation of the 5'-leader ORF, which contains several m1G37-dependent Pro codons
-
additional information
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Trm5 consists of three structural domains: domain 1 (D1), domain 2 (D2), and domain 3 (D3). D1 corresponds to the less-conserved region among Trm5 enzymes from all species, while D2 corresponds to the conserved region. The structure of D2 shares homology with that of TYW2, the tRNA-wybutosine (yW) synthesizing enzyme-2. D3 corresponds to the Rossmann-fold domain containing the AdoMet binding site, and is conserved among the class-I MTases. The D2-D3 fragment alone possesses methyl-transfer activity comparable to that of the full-length enzyme, although the presence of D1 lowers and enhances the KM and kcat values (the Michaelis and catalytic rate constants, respectively, in the Michaelis-Menten equation) for tRNA, respectively, as compared to the D2-D3 fragment. Function of D1, overview. The interaction between the outer-corner of the tRNA and Trm5 D1 is essential to confer sufficiently robust affinity for the tRNA at physiological temperatures
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additional information
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evaluation of the kinetic assays that are used to reveal the distinction between TrmD and Trm5, overview
-
additional information
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Trm5 consists of three structural domains: domain 1 (D1), domain 2 (D2), and domain 3 (D3). D1 corresponds to the less-conserved region among Trm5 enzymes from all species, while D2 corresponds to the conserved region. The structure of D2 shares homology with that of TYW2, the tRNA-wybutosine (yW) synthesizing enzyme-2. D3 corresponds to the Rossmann-fold domain containing the AdoMet binding site, and is conserved among the class-I MTases. The D2-D3 fragment alone possesses methyl-transfer activity comparable to that of the full-length enzyme, although the presence of D1 lowers and enhances the KM and kcat values (the Michaelis and catalytic rate constants, respectively, in the Michaelis-Menten equation) for tRNA, respectively, as compared to the D2-D3 fragment. Function of D1, overview. The interaction between the outer-corner of the tRNA and Trm5 D1 is essential to confer sufficiently robust affinity for the tRNA at physiological temperatures
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additional information
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evaluation of the kinetic assays that are used to reveal the distinction between TrmD and Trm5, overview
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additional information
-
TrmD consists of the N-terminal domain (NTD, the SPOUT domain) and the TrmD-specific C-terminal domain (CTD). These domains are connected by the interdomain linker. TrmD forms a homodimer, and the interdomain linkers are disordered in both monomers. The trefoil knot at the C-terminal region in the SPOUT domain provides the AdoMet-binding site. Structural changes of TrmD upon AdoMet accommodation. Structure-function analysis, overview
-
additional information
-
evaluation of the kinetic assays that are used to reveal the distinction between TrmD and Trm5, overview
-
additional information
-
TrmD consists of the N-terminal domain (NTD, the SPOUT domain) and the TrmD-specific C-terminal domain (CTD). These domains are connected by the interdomain linker. TrmD forms a homodimer, and the interdomain linkers are disordered in both monomers. The trefoil knot at the C-terminal region in the SPOUT domain provides the AdoMet-binding site. Structural changes of TrmD upon AdoMet accommodation. Structure-function analysis, overview
-
additional information
-
evaluation of the kinetic assays that are used to reveal the distinction between TrmD and Trm5, overview
-
additional information
-
active site structure in complex with S-adenosyl-L-methionine, overview
-
additional information
-
backbone NMR resonance assignments for the full length TrmD protein of Pseudomonas aeruginosa and secondary structure analysis
-
additional information
-
the N-terminal domain (NTD) contains the S-adenosyl-L-methionine (SAM) binding region, this domain binds to SAM, S-adenosyl-L-homocysteine (SAH), and active-site inhibitors such as the SAM analogue sinefungin. Metabolites such as SAM, SAH and MTA enhance the thermostability of NTD by increasing its melting temperature (Tm), dynamics and ligand binding of NTD
-
additional information
-
TrmD catalytic mechanism, overview. PaTrmD catalyzes the formation of m1G37 in tRNA by a ternary-complex mechanism in which tRNA and S-adenosyl-L-methionine can bind the protein independently. PaTrmD shares functionally important amino acid residues involved in cofactor binding (Ser93-Gly96, Gly118, Ile123, Ser137, Gly145), tRNA binding (Gly60, Gly64, Ser203-His206) and catalytic activity (Asp54, Arg159, and Asp174). Conformational changes are required to form a ternary complex with tRNA. PaTrmD catalyzes only the m1G modification in PA14 tRNAs that possess a G36G37 motif, the G36G37 motif is a substrate of PaTrmD. PaTrmD catalyzes m1G formation in synthetic tRNA substrates indicating that PaTrmD can use G36G37 containing tRNAs without other modifications as substrates. Enzyme structure modelling, overview
-
additional information
-
TrmD consists of the N-terminal domain (NTD, the SPOUT domain) and the TrmD-specific C-terminal domain (CTD). These domains are connected by the interdomain linker. TrmD forms a homodimer, and the interdomain linkers are disordered in both monomers. The trefoil knot at the C-terminal region in the SPOUT domain provides the AdoMet-binding site. Structural changes of TrmD upon AdoMet accommodation. Structure-function analysis, overview
-
additional information
-
evaluation of the kinetic assays that are used to reveal the distinction between TrmD and Trm5, overview
-
additional information
-
Trm5 consists of three structural domains: domain 1 (D1), domain 2 (D2), and domain 3 (D3). D1 corresponds to the less-conserved region among Trm5 enzymes from all species, while D2 corresponds to the conserved region. The structure of D2 shares homology with that of TYW2, the tRNA-wybutosine (yW) synthesizing enzyme-2. D3 corresponds to the Rossmann-fold domain containing the AdoMet binding site, and is conserved among the class-I MTases. The D2-D3 fragment alone possesses methyl-transfer activity comparable to that of the full-length enzyme, although the presence of D1 lowers and enhances the KM and kcat values (the Michaelis and catalytic rate constants, respectively, in the Michaelis-Menten equation) for tRNA, respectively, as compared to the D2-D3 fragment. Function of D1, overview. The interaction between the outer-corner of the tRNA and Trm5 D1 is essential to confer sufficiently robust affinity for the tRNA at physiological temperatures
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additional information
-
evaluation of the kinetic assays that are used to reveal the distinction between TrmD and Trm5, overview
-
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C20S
the C20S mutant protein forms a dimer structure even though it is missing the Cys20Cys20 disulfide bond between its two subunits. Incubation at 85°C for 20 min causes the precipitation of more than half of the C20S protein, while more than 70% of the wild-type enzyme is soluble at that temperature. Methyl-transfer activity of the C20S mutant protein is slightly less than that of the wild-type enzyme at 70°C. Comparison of the CD-spectra of wild-type and C20S proteins reveals that some of the alpha-helices in the C20S mutant protein are less tightly packed than the alpha-helices of the wild-type enzyme at 70°C
A202S
Km/Vmax for tRNA is 2fold higher than wild-type value
A25S
Km/Vmax for tRNA is 2.9fold higher than wild-type value
A70S
Km/Vmax for tRNA is 4fold higher than wild-type value
C112A
Km/Vmax for tRNA is 7.6fold higher than wild-type value
D119A
inactive mutant enzyme
D128A
inactive mutant enzyme
D135A
inactive mutant enzyme
D169A
inactive mutant enzyme
D169E
Km/Vmax for tRNA is 1.4fold higher than wild-type value
D50A
Km/Vmax for tRNA is 4fold higher than wild-type value
E116A
Km/Vmax for tRNA is 2fold higher than wild-type value
E130A
Km/Vmax for tRNA is 2fold higher than wild-type value
E142A
Km/Vmax for tRNA is 3.1fold higher than wild-type value
G113A
Km/Vmax for tRNA is 5.3fold higher than wild-type value
G117A
inactive mutant enzyme
G134A
Km/Vmax for tRNA is 6.8fold higher than wild-type value
G140A
Km/Vmax for tRNA is 8.5fold higher than wild-type value
G141A
Km/Vmax for tRNA is 1.5fold lower than wild-type value
G189A
Km/Vmax for tRNA is 8fold higher than wild-type value
G55A
Km/Vmax for tRNA is 4.8fold higher than wild-type value
G59A
inactive mutant enzyme
G91A
inactive mutant enzyme
H180A
Km/Vmax for tRNA is 5 fold higher than wild-type value
I204A
inactive mutant enzyme
L138A
Km/Vmax for tRNA is 1,7fold higher than wild-type value
L196A
inactive mutant enzyme
L197A
inactive mutant enzyme
M60A
Km/Vmax for tRNA is 2.7fold higher than wild-type value
P184A
inactive mutant enzyme
P193A
inactive mutant enzyme
P53A
Km/Vmax for tRNA is 2fold higher than wild-type value
R114A
inactive mutant enzyme
R121A
inactive mutant enzyme
R154A
inactive mutant enzyme
R208A
inactive mutant enzyme
R215A
Km/Vmax for tRNA is 5fold higher than wild-type value
R219A
Km/Vmax for tRNA is 4fold higher than wild-type value
S132A
Km/Vmax for tRNA is 1.5fold higher than wild-type value
S88L
naturally occuring mutation of trmD, the mutation confers thermal lability to the enzyme with a minor effect. The mutation decreases the catalytic efficiency of the enzyme to 1% of wild-type activity at permissive temperature. At nonpermissive temperature, it renders further deterioration of activity to 0.1%. These changes are accompanied by losses of both the quantity and quality of tRNA methylation, leading to the potential of cellular pleiotropic effects
V192A
inactive mutant enzyme
W131A
Km/Vmax for tRNA is 1.3fold higher than wild-type value
W207A
inactive mutant enzyme
W207F
Km/Vmax for tRNA is 4fold higher than wild-type value
W207H
Km/Vmax for tRNA is 5.6fold higher than wild-type value
Y136A
Km/Vmax for tRNA is 7.3fold higher than wild-type value
D275A
site-directed mutagenesis, the mutation leads to significantly reduced activity
E288A
site-directed mutagenesis, the mutation at the general base position leads to highly reduced activity
E394K
site-directed mutagenesis, the mutation facilitates enzyme expression in Escherichia coli
H289A
site-directed mutagenesis, the mutation C-terminally adjacent to the general base does not affect the enzyme activity
H289R
site-directed mutagenesis, the mutation C-terminally adjacent to the general base does not affect the enzyme activity
M261L
site-directed mutagenesis, the single M261L substitution that recapitulates the archaeal residue minimizes the 27-kDa protease product upon enzyme expression in Escherichia coli, indicating improved stability
M261L/T261I
site-directed mutagenesis, the double M261L substitution also shows improved stability
M386V
-
naturally occuring TRMT5 mutation, the mutant shows diminished G37 modification of a mitochondrial tRNA and a pathogenic phenotype
R291H
-
naturally occuring TRMT5 mutation, the mutant shows diminished G37 modification of a mitochondrial tRNA and a pathogenic phenotype
T263I
site-directed mutagenesis, the mutation does not affect the enzyme
D201A
59% activity realtive to the wild-type
D223E
site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme
D223L
site-directed mutagenesis, the mutant shows complete loss of activity
D223N
site-directed mutagenesis, the mutant shows complete loss of activity
E185A
site-directed mutagenesis, the mutant shows complete loss of activity
E185D
site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme
E185Q
site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme
K137A
site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme
K318A
site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme
N225A
kcat/Km for guanine37 in Methanocaldococcus jannaschii tRNACys is 5% of the wild-type value
N265H
site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme
N265Q
site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme
P226A
kcat/Km for guanine37 in Methanocaldococcus jannaschii tRNACys is 6% of the wild-type value
R144A
kcat/Km for guanine37 in Methanocaldococcus jannaschii tRNACys is 6% of the wild-type value
R145A
site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme
R181A
site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme
R186A
site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme
Y176A
kcat/Km for guanine37 in Methanocaldococcus jannaschii tRNACys is 5% of the wild-type value
Y177A
site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme
Y177F
site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme
C301S/C308S/C326S
site-directed mutagenesis
D243A
site-directed mutagenesis, substrate binding compared to wild-type enzyme
E173A
site-directed mutagenesis, the mutant shows 9 and 26% of wild-type activity for imG and imG2 formation, respectively
F165A
site-directed mutagenesis, inactive mutant
H128A
site-directed mutagenesis, substrate binding compared to wild-type enzyme
P260N
site-directed mutagenesis, the mutant shows no and 114% of wild-type activity for imG and imG2 formation, respectively
P262A
site-directed mutagenesis, the mutant shows 5 and 8% of wild-type activity for imG and imG2 formation, respectively
R133A
site-directed mutagenesis, substrate binding compared to wild-type enzyme
R134A
site-directed mutagenesis, the mutant shows 2 and 4% of wild-type activity for imG and imG2 formation, respectively
R135A
site-directed mutagenesis, substrate binding compared to wild-type enzyme
V21C/C301S/C308S/K314C/C326S
site-directed mutagenesis
Y318A
site-directed mutagenesis, substrate binding compared to wild-type enzyme
E173A
-
site-directed mutagenesis, the mutant shows 9 and 26% of wild-type activity for imG and imG2 formation, respectively
-
E213A
-
site-directed mutagenesis, inactive mutant
-
F165A
-
site-directed mutagenesis, inactive mutant
-
R134A
-
site-directed mutagenesis, the mutant shows 2 and 4% of wild-type activity for imG and imG2 formation, respectively
-
R174A
-
site-directed mutagenesis, the mutant shows 8 and 69% of wild-type activity for imG and imG2 formation, respectively
-
D223A
6.2% activity realtive to the wild-type
D223A
kcat/Km for guanine37 in Methanocaldococcus jannaschii tRNACys is 1% of the wild-type value
D223A
site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme
G205A/G207A
12.3% activity realtive to the wild-type
G205A/G207A
kcat/Km for guanine37 in Methanocaldococcus jannaschii tRNACys is 3% of the wild-type value
N265A
11.2% activity realtive to the wild-type
N265A
kcat/Km for guanine37 in Methanocaldococcus jannaschii tRNACys is 1% of the wild-type value
N265A
site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme
P267A
1.3% activity realtive to the wild-type
P267A
kcat/Km for guanine37 in Methanocaldococcus jannaschii tRNACys is 0.1% of the wild-type value
P267A
site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme
E213A
site-directed mutagenesis, inactive mutant
E213A
site-directed mutagenesis, substrate binding compared to wild-type enzyme
R174A
site-directed mutagenesis, substrate binding compared to wild-type enzyme
R174A
site-directed mutagenesis, the mutant shows 8 and 69% of wild-type activity for imG and imG2 formation, respectively
S88L
mutant trmD harbors a mutation near the AdoMet binding site, the mutation prevents the enzyme from binding to the methyl donor and from performing the Mg2C-dependent methyl transfer. The reported observation supports a model of codon-specific translation in the 5'-leader ORF
S88L
-
mutant trmD harbors a mutation near the AdoMet binding site, the mutation prevents the enzyme from binding to the methyl donor and from performing the Mg2C-dependent methyl transfer. The reported observation supports a model of codon-specific translation in the 5'-leader ORF
-
S88L
-
mutant trmD harbors a mutation near the AdoMet binding site, the mutation prevents the enzyme from binding to the methyl donor and from performing the Mg2C-dependent methyl transfer. The reported observation supports a model of codon-specific translation in the 5'-leader ORF
-
additional information
generation of T-DNA insertion attrm5a deletion mutants, phenotypes, overview
additional information
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generation of T-DNA insertion attrm5a deletion mutants, phenotypes, overview
additional information
-
identification of TRMT5 enzyme mutants in patients, the loss of m1G37 does not appear to impact tRNA stability, phenotype, overview
additional information
structure-guided mutational analysis of HsTrm5 in comparison to the archaeal enzyme from Methanococcus jannaschii, MjTrm5, overview. Validation of the MjTrm5 ternary structure as a useful model for HsTrm5
additional information
-
structure-guided mutational analysis of HsTrm5 in comparison to the archaeal enzyme from Methanococcus jannaschii, MjTrm5, overview. Validation of the MjTrm5 ternary structure as a useful model for HsTrm5
additional information
proline at position 267 is a critical residue for catalysis, because substitution of this residue severely decreases kcat of the methylation reaction in steady-state kinetic analysis. However, substitution of P267 has milder effect on Km and little effect on Kd of either substrate. Because P267 has no functional side chain that can directly participate in the chemistry of methyl transfer, we suggest that its role in catalysis is to stabilize conformations of enzyme and substrates for proper alignment of reactive groups at the enzyme active site. Sequence analysis shows that P267 is embedded in a peptide motif that is conserved among the Trm5 family, but absent from the TrmD family, supporting the notion that the two families are descendants of unrelated protein structures
additional information
the m.4435A->G mutation introduces an m1G37 modification of tRNAMet, altering its structure and function. Primer extension and methylation activity assays indeed confirm that the m.4435A3G mutation creates a tRNA methyltransferase 5 (TRMT5)-catalyzed m1G37 modification of tRNAMet
additional information
-
the m.4435A->G mutation introduces an m1G37 modification of tRNAMet, altering its structure and function. Primer extension and methylation activity assays indeed confirm that the m.4435A3G mutation creates a tRNA methyltransferase 5 (TRMT5)-catalyzed m1G37 modification of tRNAMet
-
additional information
-
the m.4435A->G mutation introduces an m1G37 modification of tRNAMet, altering its structure and function. Primer extension and methylation activity assays indeed confirm that the m.4435A3G mutation creates a tRNA methyltransferase 5 (TRMT5)-catalyzed m1G37 modification of tRNAMet
-
additional information
-
the m.4435A->G mutation introduces an m1G37 modification of tRNAMet, altering its structure and function. Primer extension and methylation activity assays indeed confirm that the m.4435A3G mutation creates a tRNA methyltransferase 5 (TRMT5)-catalyzed m1G37 modification of tRNAMet
-
additional information
-
the m.4435A->G mutation introduces an m1G37 modification of tRNAMet, altering its structure and function. Primer extension and methylation activity assays indeed confirm that the m.4435A3G mutation creates a tRNA methyltransferase 5 (TRMT5)-catalyzed m1G37 modification of tRNAMet
-
additional information
-
the m.4435A->G mutation introduces an m1G37 modification of tRNAMet, altering its structure and function. Primer extension and methylation activity assays indeed confirm that the m.4435A3G mutation creates a tRNA methyltransferase 5 (TRMT5)-catalyzed m1G37 modification of tRNAMet
-
additional information
attempts to construct a PA14_15990/trmD mutant in Pseudomonas aeruginosa strain PA14 using homologous recombination are not successful, due to the fact that the enzyme is essential in Pseudomonas aeruginosa. A temperature-sensitive allele of a Pseudomonas replicon, mSFts1 is used, to regulate expression of extra chromosomal trmD. Wild-type strain PA14 containing pBBR-trmD-mSFts1 and the trmD conditional knockout strain (trmD::Gm/pBBR-trmD-mSFts1) are both grown at a permissive temperature to maintain the stability of the plasmid (28 and 37°C) or at a non-permissive temperature to cause plasmid loss (46°C). The growth of the trmD conditional knockout strain at the permissive temperature is similar to wild-type PA14, while growth of the knockout strain is no longer observed at the non-permissive temperature
additional information
-
attempts to construct a PA14_15990/trmD mutant in Pseudomonas aeruginosa strain PA14 using homologous recombination are not successful, due to the fact that the enzyme is essential in Pseudomonas aeruginosa. A temperature-sensitive allele of a Pseudomonas replicon, mSFts1 is used, to regulate expression of extra chromosomal trmD. Wild-type strain PA14 containing pBBR-trmD-mSFts1 and the trmD conditional knockout strain (trmD::Gm/pBBR-trmD-mSFts1) are both grown at a permissive temperature to maintain the stability of the plasmid (28 and 37°C) or at a non-permissive temperature to cause plasmid loss (46°C). The growth of the trmD conditional knockout strain at the permissive temperature is similar to wild-type PA14, while growth of the knockout strain is no longer observed at the non-permissive temperature
additional information
-
attempts to construct a PA14_15990/trmD mutant in Pseudomonas aeruginosa strain PA14 using homologous recombination are not successful, due to the fact that the enzyme is essential in Pseudomonas aeruginosa. A temperature-sensitive allele of a Pseudomonas replicon, mSFts1 is used, to regulate expression of extra chromosomal trmD. Wild-type strain PA14 containing pBBR-trmD-mSFts1 and the trmD conditional knockout strain (trmD::Gm/pBBR-trmD-mSFts1) are both grown at a permissive temperature to maintain the stability of the plasmid (28 and 37°C) or at a non-permissive temperature to cause plasmid loss (46°C). The growth of the trmD conditional knockout strain at the permissive temperature is similar to wild-type PA14, while growth of the knockout strain is no longer observed at the non-permissive temperature
-
additional information
construction of the D1-truncated PaTrm5b73-330 mutant using full-length Trm5b as the template
additional information
-
construction of the D1-truncated PaTrm5b73-330 mutant using full-length Trm5b as the template
additional information
Trametes pubescens 927 / 4 GUTat10.1 / TREU927
-
generation of enzyme knockout lines using a TbTRM5 RNAi plasmid in procyclic Trypanosoma brucei 29-13 cells
-
additional information
generation of enzyme knockout lines using a TbTRM5 RNAi plasmid in procyclic Trypanosoma brucei 29-13 cells
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Brule, H.; Elliott, M.; Redlak, M.; Zehner, Z.E.; Holmes, W.M.
Isolation and characterization of the human tRNA-(N1G37) methyltransferase (TRM5) and comparison to the Escherichia coli TrmD protein
Biochemistry
43
9243-9255
2004
Escherichia coli (P0A873), Escherichia coli, Homo sapiens (Q32P41), Homo sapiens
brenda
Ahn, H.J.; Kim, H.W.; Yoon, H.J.; Lee, B.I.; Suh, S.W.; Yang, J.K.
Crystal structure of tRNA(m1G37)methyltransferase: insights into tRNA recognition
EMBO J.
22
2593-2603
2003
Haemophilus influenzae (P43912), Haemophilus influenzae
brenda
O'Dwyer, K.; Watts, J.M.; Biswas, S.; Ambrad, J.; Barber, M.; Brule, H.; Petit, C.; Holmes, D.J.; Zalacain, M.; Holmes, W.M.
Characterization of Streptococcus pneumoniae TrmD, a tRNA methyltransferase essential for growth
J. Bacteriol.
186
2346-2354
2004
Streptococcus pneumoniae
brenda
Christian, T.; Evilia, C.; Williams, S.; Hou, Y.M.
Distinct origins of tRNA(m1G37) methyltransferase
J. Mol. Biol.
339
707-719
2004
Methanocaldococcus jannaschii (Q58293), Methanocaldococcus jannaschii
brenda
Takeda, H.; Toyooka, T.; Ikeuchi, Y.; Yokobori, S.; Okadome, K.; Takano, F.; Oshima, T.; Suzuki, T.; Endo, Y.; Hori, H.
The substrate specificity of tRNA (m1G37) methyltransferase (TrmD) from Aquifex aeolicus
Genes Cells
11
1353-1365
2006
Aquifex aeolicus
brenda
Lee, C.; Kramer, G.; Graham, D.E.; Appling, D.R.
Yeast mitochondrial initiator tRNA is methylated at guanosine 37 by the Trm5-encoded tRNA (guanine-N1-)-methyltransferase
J. Biol. Chem.
282
27744-27753
2007
Saccharomyces cerevisiae (P38793), Saccharomyces cerevisiae
brenda
Goto-Ito, S.; Ito, T.; Ishii, R.; Muto, Y.; Bessho, Y.; Yokoyama, S.
Crystal structure of archaeal tRNA(m(1)G37)methyltransferase aTrm5
Proteins
72
1274-1289
2008
Methanocaldococcus jannaschii (Q58293), Methanocaldococcus jannaschii
brenda
Kim, H.W.; Ahn, H.J., Yoon, H.J.; Kim, H.W., Baek, S.H.; Suh, S.W.
Crystallization and preliminary X-ray crystallographic analysis of tRNA(m1G37)methyltransferase from Haemophilus influenzae
Acta Crystallogr. Sect. D
59
183-184
2002
Haemophilus influenzae
brenda
Christian, T.; Evilia, C.; Hou, Y.M.
Catalysis by the second class of tRNA(m1G37) methyl transferase requires a conserved proline
Biochemistry
45
7463-7473
2006
Methanocaldococcus jannaschii (Q58293)
brenda
Toyooka, T.; Awai, T.; Kanai, T.; Imanaka, T.; Hori, H.
Stabilization of tRNA (mG37) methyltransferase [TrmD] from Aquifex aeolicus by an intersubunit disulfide bond formation
Genes Cells
13
807-816
2008
Aquifex aeolicus (O67463)
brenda
Elkins, P.A.; Watts, J.M.; Zalacain, M.; van Thiel, A.; Vitazka, P.R.; Redlak, M.; Andraos-Selim, C.; Rastinejad, F.; Holmes, W.M.
Insights into catalysis by a knotted TrmD tRNA methyltransferase
J. Mol. Biol.
333
931-949
2003
Escherichia coli (P0A873), Escherichia coli
brenda
Christian, T.; Hou, Y.M.
Distinct determinants of tRNA recognition by the TrmD and Trm5 methyl transferases
J. Mol. Biol.
373
623-632
2007
Escherichia coli, Methanocaldococcus jannaschii (Q58293)
brenda
Liu, J.; Wang, W.; Shin, D.H.; Yokota, H.; Kim, R., Kim, S.H.
Crystal structure of tRNA (m1G37) methyltransferase from Aquifex aeolicus at 2.6 A resolution: a novel methyltransferase fold
Proteins
53
326-328
2003
Aquifex aeolicus (O67463), Aquifex aeolicus
brenda
Christian, T.; Lahoud, G.; Liu, C.; Hou, Y.M.
Control of catalytic cycle by a pair of analogous tRNA modification enzymes
J. Mol. Biol.
400
204-217
2010
Escherichia coli, Methanocaldococcus jannaschii
brenda
Christian, T.; Lahoud, G.; Liu, C.; Hoffmann, K.; Perona, J.J.; Hou, Y.M.
Mechanism of N-methylation by the tRNA m1G37 methyltransferase Trm5
RNA
16
2484-2492
2010
Methanocaldococcus jannaschii (Q58293)
brenda
Lahoud, G.; Goto-Ito, S.; Yoshida, K.; Ito, T.; Yokoyama, S.; Hou, Y.M.
Differentiating analogous tRNA methyltransferases by fragments of the methyl donor
RNA
17
1236-1246
2011
Escherichia coli, Methanocaldococcus jannaschii
brenda
Sakaguchi, R.; Giessing, A.; Dai, Q.; Lahoud, G.; Liutkeviciute, Z.; Klimasauskas, S.; Piccirilli, J.; Kirpekar, F.; Hou, Y.M.
Recognition of guanosine by dissimilar tRNA methyltransferases
RNA
18
1687-1701
2012
Escherichia coli, Methanocaldococcus jannaschii
brenda
Kawamura, T.; Anraku, R.; Hasegawa, T.; Tomikawa, C.; Hori, H.
Transfer RNA methyltransferases from Thermoplasma acidophilum, a thermoacidophilic archaeon
Int. J. Mol. Sci.
16
91-113
2014
Thermoplasma acidophilum, Thermoplasma acidophilum HO-62
brenda
Powell, C.A.; Kopajtich, R.; DSouza, A.R.; Rorbach, J.; Kremer, L.S.; Husain, R.A.; Dallabona, C.; Donnini, C.; Alston, C.L.; Griffin, H.; Pyle, A.; Chinnery, P.F.; Strom, T.M.; Meitinger, T.; Rodenburg, R.J.; Schottmann, G.; Schuelke, M.; Romain, N.; Haller, R.G.; Ferrero, I.; Haack, T.B.; Taylor, R.W.; Pr, P.r.o.
TRMT5 mutations cause a defect in post-transcriptional modification of mitochondrial tRNA associated with multiple respiratory-chain deficiencies
Am. J. Hum. Genet.
97
319-328
2015
Homo sapiens
brenda
Sakaguchi, R.; Lahoud, G.; Christian, T.; Gamper, H.; Hou, Y.M.
A divalent metal ion-dependent N1-methyl transfer to G37-tRNA
Chem. Biol.
21
1351-1360
2014
Escherichia coli
brenda
Masuda, I.; Sakaguchi, R.; Liu, C.; Gamper, H.; Hou, Y.M.
The temperature sensitivity of a mutation in the essential tRNA modification enzyme tRNA methyltransferase D (TrmD)
J. Biol. Chem.
288
28987-28996
2013
Escherichia coli (P0A873), Escherichia coli
brenda
Ito, T.; Masuda, I.; Yoshida, K.; Goto-Ito, S.; Sekine, S.; Suh, S.W.; Hou, Y.M.; Yokoyama, S.
Structural basis for methyl-donor-dependent and sequence-specific binding to tRNA substrates by knotted methyltransferase TrmD
Proc. Natl. Acad. Sci. USA
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E4197-E4205
2015
Haemophilus influenzae, Thermotoga maritima, Haemophilus influenzae DSM 11121
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Christian, T.; Gamper, H.; Hou, Y.M.
Conservation of structure and mechanism by Trm5 enzymes
RNA
19
1192-1199
2013
Homo sapiens (Q32P41), Homo sapiens
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Paris, Z.; Horakova, E.; Rubio, M.A.; Sample, P.; Fleming, I.M.; Armocida, S.; Lukes, J.; Alfonzo, J.D.
The T. brucei TRM5 methyltransferase plays an essential role in mitochondrial protein synthesis and function
RNA
19
649-658
2013
Trypanosoma brucei brucei (Q57X10), Trametes pubescens 927 / 4 GUTat10.1 / TREU927 (Q57X10)
brenda
Zhong, W.; Koay, A.; Ngo, A.; Li, Y.; Nah, Q.; Wong, Y.H.; Chionh, Y.H.; Ng, H.Q.; Koh-Stenta, X.; Poulsen, A.; Foo, K.; McBee, M.; Choong, M.L.; El Sahili, A.; Kang, C.; Matter, A.; Lescar, J.; Hill, J.; Dedon, P.
Targeting the bacterial epitranscriptome for antibiotic development discovery of novel tRNA-(N1G37) methyltransferase (TrmD) inhibitors
ACS Infect. Dis.
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326-335
2019
Pseudomonas aeruginosa (Q02RL6), Pseudomonas aeruginosa, Pseudomonas aeruginosa UCBPP-PA14 (Q02RL6)
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Wu, J.; Jia, Q.; Wu, S.; Zeng, H.; Sun, Y.; Wang, C.; Ge, R.; Xie, W.
The crystal structure of the Pyrococcus abyssi mono-functional methyltransferase PaTrm5b
Biochem. Biophys. Res. Commun.
493
240-245
2017
Pyrococcus abyssi (Q9V0Q0), Pyrococcus abyssi
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Li, Y.; Zhong, W.; Koay, A.Z.; Ng, H.Q.; Nah, Q.; Wong, Y.H.; Hill, J.; Lescar, J.; Dedon, P.C.; Kang, C.
Backbone resonance assignment for the full length tRNA-(N1G37) methyltransferase of Pseudomonas aeruginosa
Biomol. NMR Assign.
13
327-332
2019
Pseudomonas aeruginosa (Q02RL6), Pseudomonas aeruginosa, Pseudomonas aeruginosa UCBPP-PA14 (Q02RL6)
brenda
Li, Y.; Zhong, W.; Koay, A.Z.; Ng, H.Q.; Koh-Stenta, X.; Nah, Q.; Lim, S.H.; Larsson, A.; Lescar, J.; Hill, J.; Dedon, P.C.; Kang, C.
Backbone resonance assignment for the N-terminal region of bacterial tRNA-(N1G37) methyltransferase
Biomol. NMR Assign.
13
49-53
2019
Pseudomonas aeruginosa (Q02RL6), Pseudomonas aeruginosa, Pseudomonas aeruginosa UCBPP-PA14 (Q02RL6)
brenda
Goto-Ito, S.; Ito, T.; Yokoyama, S.
Trm5 and TrmD two enzymes from distinct origins catalyze the identical tRNA modification, m1G37
Biomolecules
7
32
2017
Escherichia coli (P0A873), Haemophilus influenzae (P43912), Methanocaldococcus jannaschii (Q58293), Pyrococcus abyssi (Q9V2G1), Pyrococcus abyssi Orsay (Q9V2G1), Methanocaldococcus jannaschii NBRC 100440 (Q58293), Haemophilus influenzae RD (P43912), Methanocaldococcus jannaschii DSM 2661 (Q58293), Methanocaldococcus jannaschii ATCC 43067 (Q58293), Methanocaldococcus jannaschii JAL-1 (Q58293), Haemophilus influenzae DSM 11121 (P43912), Haemophilus influenzae KW20 (P43912), Haemophilus influenzae ATCC 51907 (P43912), Methanocaldococcus jannaschii JCM 10045 (Q58293)
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Hori, H.
Transfer RNA methyltransferases with a SpoU-TrmD (SPOUT) fold and their modified nucleosides in tRNA
Biomolecules
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E23
2017
Haemophilus influenzae (A0A0D0GZF5), Aquifex aeolicus (O67463), Escherichia coli (P0A873)
brenda
Hou, Y.; Matsubara, R.; Takase, R.; Masuda, I.; Sulkowska, J.
TrmD A methyl transferase for tRNA methylation with m1G37
Enzymes
41
89-115
2017
Haemophilus influenzae (A0A0D0GZF5), Aquifex aeolicus (O67463), Escherichia coli (P0A873), Salmonella enterica subsp. enterica serovar Typhimurium (P36245), Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412 (P36245), Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 (P36245)
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Hou, Y.; Masuda, I.; Gamper, H.
Codon-specific translation by m1G37 methylation of tRNA
Front. Genet.
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713
2019
Escherichia coli (P0A873), Salmonella enterica subsp. enterica serovar Typhimurium (P36245), Saccharomyces cerevisiae (P38793), Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412 (P36245), Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 (P36245), Saccharomyces cerevisiae ATCC 204508 (P38793)
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Zhou, M.; Xue, L.; Chen, Y.; Li, H.; He, Q.; Wang, B.; Meng, F.; Wang, M.; Guan, M.X.
A hypertension-associated mitochondrial DNA mutation introduces an m1G37 modification into tRNAMet, altering its structure and function
J. Biol. Chem.
293
1425-1438
2018
Methanocaldococcus jannaschii (Q58293), Methanocaldococcus jannaschii NBRC 100440 (Q58293), Methanocaldococcus jannaschii DSM 2661 (Q58293), Methanocaldococcus jannaschii ATCC 43067 (Q58293), Methanocaldococcus jannaschii JAL-1 (Q58293), Methanocaldococcus jannaschii JCM 10045 (Q58293)
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Whitehouse, A.J.; Thomas, S.E.; Brown, K.P.; Fanourakis, A.; Chan, D.S.; Libardo, M.D.J.; Mendes, V.; Boshoff, H.I.M.; Floto, R.A.; Abell, C.; Blundell, T.L.; Coyne, A.G.
Development of inhibitors against Mycobacterium abscessus tRNA (m1G37) methyltransferase (TrmD) using fragment-based approaches
J. Med. Chem.
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7210-7232
2019
Mycobacteroides abscessus
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Zhong, W.; Pasunooti, K.K.; Balamkundu, S.; Wong, Y.H.; Nah, Q.; Gadi, V.; Gnanakalai, S.; Chionh, Y.H.; McBee, M.E.; Gopal, P.; Lim, S.H.; Olivier, N.; Buurman, E.T.; Dick, T.; Liu, C.F.; Lescar, J.; Dedon, P.C.
Thienopyrimidinone derivatives that inhibit bacterial tRNA (guanine37-N1)-methyltransferase (TrmD) by restructuring the active site with a tyrosine-flipping mechanism
J. Med. Chem.
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7788-7805
2019
Staphylococcus aureus, Mycobacterium tuberculosis, Pseudomonas aeruginosa
brenda
Hou, Y.M.; Masuda, I.
Kinetic analysis of tRNA methyltransferases
Methods Enzymol.
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91-116
2015
Escherichia coli (P0A873), Haemophilus influenzae (P43912), Homo sapiens (Q32P41), Methanocaldococcus jannaschii (Q58293), Methanocaldococcus jannaschii NBRC 100440 (Q58293), Haemophilus influenzae RD (P43912), Methanocaldococcus jannaschii DSM 2661 (Q58293), Methanocaldococcus jannaschii ATCC 43067 (Q58293), Methanocaldococcus jannaschii JAL-1 (Q58293), Haemophilus influenzae DSM 11121 (P43912), Haemophilus influenzae KW20 (P43912), Haemophilus influenzae ATCC 51907 (P43912), Methanocaldococcus jannaschii JCM 10045 (Q58293)
brenda
Christian, T.; Sakaguchi, R.; Perlinska, A.; Lahoud, G.; Ito, T.; Taylor, E.; Yokoyama, S.; Sulkowska, J.; Hou, Y.
Methyl transfer by substrate signaling from a knotted protein fold
Nat. Struct. Mol. Biol.
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941-948
2016
Haemophilus influenzae (A0A0D0GZF5)
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Jin, X.; Lv, Z.; Gao, J.; Zhang, R.; Zheng, T.; Yin, P.; Li, D.; Peng, L.; Cao, X.; Qin, Y.; Persson, S.; Zheng, B.; Chen, P.
AtTrm5a catalyses 1-methylguanosine and 1-methylinosine formation on tRNAs and is important for vegetative and reproductive growth in Arabidopsis thaliana
Nucleic Acids Res.
47
883-898
2019
Arabidopsis thaliana (Q93YU6), Arabidopsis thaliana
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Urbonavicius, J.; Rutkiene, R.; Lopato, A.; Tauraite, D.; Stankeviciute, J.; Aucynaite, A.; Kaliniene, L.; van Tilbeurgh, H.; Meskys, R.
Evolution of tRNAPhe imG2 methyltransferases involved in the biosynthesis of wyosine derivatives in Archaea
RNA
22
1871-1883
2016
Nanoarchaeum equitans (Q74NE4), Pyrococcus abyssi (Q9V2G1), Pyrococcus abyssi Orsay (Q9V2G1)
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Jaroensuk, J.; Wong, Y.H.; Zhong, W.; Liew, C.W.; Maenpuen, S.; Sahili, A.E.; Atichartpongkul, S.; Chionh, Y.H.; Nah, Q.; Thongdee, N.; McBee, M.E.; Prestwich, E.G.; DeMott, M.S.; Chaiyen, P.; Mongkolsuk, S.; Dedon, P.C.; Lescar, J.; Fuangthong, M.
Crystal structure and catalytic mechanism of the essential m1G37 tRNA methyltransferase TrmD from Pseudomonas aeruginosa
RNA
25
1481-1496
2019
Pseudomonas aeruginosa (Q02RL6), Pseudomonas aeruginosa, Pseudomonas aeruginosa UCBPP-PA14 (Q02RL6)
brenda
Wang, C.; Jia, Q.; Zeng, J.; Chen, R.; Xie, W.
Structural insight into the methyltransfer mechanism of the bifunctional Trm5
Sci. Adv.
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e1700195
2017
Methanocaldococcus jannaschii (Q58293), Pyrococcus abyssi (Q9V2G1), Methanocaldococcus jannaschii DSM 2661 (Q58293)
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Wang, C.; Jia, Q.; Chen, R.; Wei, Y.; Li, J.; Ma, J.; Xie, W.
Crystal structures of the bifunctional tRNA methyltransferase Trm5a
Sci. Rep.
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33553
2016
Pyrococcus abyssi (Q9V2G1), Pyrococcus abyssi
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