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Results 1 - 10 of 16 > >>
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EC Number Substrates Commentary Substrates Organism Products Commentary (Products) Reversibility
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.268more Trm140 interacts with Ses1, a cytoplasmic serine-tRNA ligase (EC 6.1.1.11). Ses1 stimulates m3C formation of tRNASer species Saccharomyces cerevisiae ? - -
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.268more substrate specificity of enzyme Trm140 in vitro and in vivo, overview. An XGU anticodon and t6A37 are necessary and sufficient for m3C modification of tRNAThr species. tRNAThr(CGU) scaffold used for analysis of tRNAThr variants is fully functional and efficiently modified to m3C. For the tRNAThr(CGU) 28,50 variants, substitution of G35 or U36 with each of the other three nucleotides almost completely abolishes the copurification of tRNA, whereas substitution of C34 with other nucleotides leads to high levels of variant copurification. Trm140 binds tRNAs with a G35-U36 anticodon. G35 and U36 of tRNAThr(CGU) are required for m3C formation. Trm140 specifically binds tRNAThr substrates, activities with tRNAThr variants, overview Saccharomyces cerevisiae ? - -
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.268more Trm140 interacts with Ses1, a cytoplasmic serine-tRNA ligase (EC 6.1.1.11). Ses1 stimulates m3C formation of tRNASer species Saccharomyces cerevisiae ATCC 204508 ? - -
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.268more substrate specificity of enzyme Trm140 in vitro and in vivo, overview. An XGU anticodon and t6A37 are necessary and sufficient for m3C modification of tRNAThr species. tRNAThr(CGU) scaffold used for analysis of tRNAThr variants is fully functional and efficiently modified to m3C. For the tRNAThr(CGU) 28,50 variants, substitution of G35 or U36 with each of the other three nucleotides almost completely abolishes the copurification of tRNA, whereas substitution of C34 with other nucleotides leads to high levels of variant copurification. Trm140 binds tRNAs with a G35-U36 anticodon. G35 and U36 of tRNAThr(CGU) are required for m3C formation. Trm140 specifically binds tRNAThr substrates, activities with tRNAThr variants, overview Saccharomyces cerevisiae ATCC 204508 ? - -
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.268S-adenosyl-L-methionine + cytosine32 in tRNA1Ser tRNASer1 = tRNASer(UGA). Because position 32 of tRNA has an important role in accurate codon recognition, N3-methylcytosine32 formation in tRNAThr1 or tRNASer1 might play a role in modulating codon recognition and translational efficiency Saccharomyces cerevisiae S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNA1Ser - ?
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.268S-adenosyl-L-methionine + cytosine32 in tRNA1Ser tRNAThr1 = tRNAThr(IGU). ABP140 is identified as the protein responsible for N3-methylcytosine32 formation in both tRNAThr1 and tRNASer1 by systematic reverse genetic approach combined with mass spectrometry (ribonucleome analysis). N3-Methylcytosine32 formation in tRNAThr1 can be reconstituted using recombinant Abp140p in the presence of S-adenosyl-L-methionine, whereas N3-methylcytosine32 does not form in tRNASer1 in vitro, indicating the absence of a factor(s) required for tRNASer1 N3-methylcytosine32 formation Saccharomyces cerevisiae S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNA1Ser - ?
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.268S-adenosyl-L-methionine + cytosine32 in tRNA1Thr tRNAThr1 = tRNAThr(IGU). Because position 32 of tRNA has an important role in accurate codon recognition, N3-methylcytosine32 formation in tRNAThr1 or tRNASer1 might play a role in modulating codon recognition and translational efficiency Saccharomyces cerevisiae S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNA1Thr - ?
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.268S-adenosyl-L-methionine + cytosine32 in tRNA1Thr tRNAThr1 = tRNAThr(IGU). ABP140 is identified as the protein responsible for N3-methylcytosine32 formation in both tRNAThr1 and tRNASer1 by systematic reverse genetic approach combined with mass spectrometry (ribonucleome analysis). N3-Methylcytosine32 formation in tRNAThr1 can be reconstituted using recombinant Abp140p in the presence of S-adenosyl-L-methionine, whereas N3-methylcytosine32 does not form in tRNASer1 in vitro, indicating the absence of a factor(s) required for tRNASer1 N3-methylcytosine32 formation Saccharomyces cerevisiae S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNA1Thr - ?
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.268S-adenosyl-L-methionine + cytosine32 in tRNA1Thr tRNAThr1 = tRNAThr(IGU). Trm140p does not have detectable activity on a tRNAThr(IGU) transcript with a C32A mutation. No activity with tRNAPhe. It is demonstrated directly that ABP140 is required for the m3C modification of tRNAThr(IGU) in yeast, and it is infered that ABP140 is required for m3C32 formation for all six tRNAThr and tRNASer species for which m3C is documented Saccharomyces cerevisiae S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNA1Thr - ?
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.268S-adenosyl-L-methionine + cytosine32 in tRNASer - Saccharomyces cerevisiae S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNASer - ?
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