Information on EC 2.1.1.228 - tRNA (guanine37-N1)-methyltransferase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY hide
2.1.1.228
-
RECOMMENDED NAME
GeneOntology No.
tRNA (guanine37-N1)-methyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + guanine37 in tRNA = S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
7-(3-amino-3-carboxypropyl)-wyosine biosynthesis
-
-
methylwyosine biosynthesis
-
-
tRNA methylation (yeast)
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:tRNA (guanine37-N1)-methyltransferase
This enzyme is important for the maintenance of the correct reading frame during translation. Unlike TrmD from Escherichia coli, which recognizes the G36pG37 motif preferentially, the human enzyme (encoded by TRMT5) also methylates inosine at position 37 [4].
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + guanine36 in tRNALeu
S-adenosyl-L-homocysteine + N1-methylguanine36 in tRNALeu
show the reaction diagram
S-adenosyl-L-methionine + guanine37 in Aquifex aeolicus tRNAArg(ACG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in Aquifex aeolicus tRNAArg(ACG)
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in Aquifex aeolicus tRNAArg(CCG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in Aquifex aeolicus tRNAArg(CCG)
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in Aquifex aeolicus tRNAGln(UUG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in Aquifex aeolicus tRNAGln(UUG)
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in Aquifex aeolicus tRNAHis(GUG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in Aquifex aeolicus tRNAHis(GUG)
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in Aquifex aeolicus tRNALeu(CAG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in Aquifex aeolicus tRNALeu(CAG)
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in Aquifex aeolicus tRNAPro(GGG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in Aquifex aeolicus tRNAPro(GGG)
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in elongator tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in elongator tRNA
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in Escherichia coli tRNA1Leu
S-adenosyl-L-homocysteine + N1-methylguanine37 in Escherichia coli tRNA1Leu
show the reaction diagram
S-adenosyl-L-methionine + guanine37 in Escherichia coli tRNAPro
S-adenosyl-L-homocysteine + N1-methylguanine37 in Escherichia coli tRNAPro
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in Haloferax volcanii tRNACys(GCA)
S-adenosyl-L-homocysteine + N1-methylguanine37 in Haloferax volcanii tRNACys(GCA)
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in Haloferax volcanii tRNALeu(CAA)
S-adenosyl-L-homocysteine + N1-methylguanine37 in Haloferax volcanii tRNALeu(CAA)
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in Haloferax volcanii tRNATrp(CCA)
S-adenosyl-L-homocysteine + N1-methylguanine37 in Haloferax volcanii tRNATrp(CCA)
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in Haloferax volcanii tRNATyr(GUA)
S-adenosyl-L-homocysteine + N1-methylguanine37 in Haloferax volcanii tRNATyr(GUA)
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in human mitochondrial tRNAPro
S-adenosyl-L-homocysteine + N1-methylguanine37 in human mitochondrial tRNAPro
show the reaction diagram
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
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + guanine37 in in Escherichia coli tRNALeu(CAG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in in Escherichia coli tRNALeu(CAG)
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in Methanocaldococcus jannaschii tRNA(Cys)
S-adenosyl-L-homocysteine + N1-methylguanine37 in Methanocaldococcus jannaschii tRNA(Cys)
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in Methanocaldococcus jannaschii tRNAArg(UCG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in Methanocaldococcus jannaschii tRNAArg(UCG)
show the reaction diagram
possessing the sequence G36G37
-
-
?
S-adenosyl-L-methionine + guanine37 in Methanocaldococcus jannaschii tRNACys
S-adenosyl-L-homocysteine + N1-methylguanine37 in Methanocaldococcus jannaschii tRNACys
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in Methanocaldococcus jannaschii tRNACys(GCA)
S-adenosyl-L-homocysteine + N1-methylguanine37 in Methanocaldococcus jannaschii tRNACys(GCA)
show the reaction diagram
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)
show the reaction diagram
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)
show the reaction diagram
possessing the sequence G36G37
-
-
?
S-adenosyl-L-methionine + guanine37 in Methanocaldococcus jannaschii tRNAPro
S-adenosyl-L-homocysteine + N1-methylguanine37 in Methanocaldococcus jannaschii tRNAPro
show the reaction diagram
S-adenosyl-L-methionine + guanine37 in Methanocaldococcus jannaschii tRNAPro(GGG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in Methanocaldococcus jannaschii tRNAPro(GGG)
show the reaction diagram
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)
show the reaction diagram
possessing the sequence G36G37
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
show the reaction diagram
S-adenosyl-L-methionine + guanine37 in tRNAArg
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAArg
show the reaction diagram
S-adenosyl-L-methionine + guanine37 in tRNAArgCCG
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAArgCCG
show the reaction diagram
S-adenosyl-L-methionine + guanine37 in tRNACys
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNACys
show the reaction diagram
S-adenosyl-L-methionine + guanine37 in tRNACysGCA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNACysGCA
show the reaction diagram
S-adenosyl-L-methionine + guanine37 in tRNAGlnCUG
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAGlnCUG
show the reaction diagram
S-adenosyl-L-methionine + guanine37 in tRNAGlnG36A
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAGlnG36A
show the reaction diagram
-
tRNA substrate from Thermotoga maritima
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAGlnG36C
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAGlnG36C
show the reaction diagram
-
tRNA substrate from Thermotoga maritima
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAGlnG36U
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAGlnG36U
show the reaction diagram
-
tRNA substrate from Thermotoga maritima
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAHisGUG
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAHisGUG
show the reaction diagram
S-adenosyl-L-methionine + guanine37 in tRNAIleUaU
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAIleUaU
show the reaction diagram
S-adenosyl-L-methionine + guanine37 in tRNALeu
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNALeu
show the reaction diagram
S-adenosyl-L-methionine + guanine37 in tRNALeu(GAC)
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNALeu(GAC)
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNALeuCAG
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNALeuCAG
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAPro
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPro
show the reaction diagram
S-adenosyl-L-methionine + guanine37 in tRNAProAGG
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAProAGG
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + guanine37 in yeast tRNAPhe(GAA)
S-adenosyl-L-homocysteine + N1-methylguanine37 in yeast tRNAPhe(GAA)
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
show the reaction diagram
S-adenosyl-L-methionine + guanine37 in tRNAIleUaU
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAIleUaU
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KCl
TRM5 enzyme is stimulated 4fold by 100 mM KCl. TRM5 tends to lose all activity in 600 mM KCl
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5'-[(2-aminoethyl)thio]-5'-deoxy-adenosine
6-Chloropurine
adenosine
AdoButyn
AdoPropen
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
Inosine
methionine
methylthioadenosine
S-adenosyl-L-homocysteine
S-methyl-L-cysteine
sinefungin
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
glycerol
TRM5 performs best between 25 and 30% glycerol, and is less active at lower concentrations. The enzyme retains 45% of its activity in the presence of 50% glycerol
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0006
guanine37 in Aquifex aeolicus tRNAArg(ACG)
-
pH 7.6, 60C
-
0.0008
guanine37 in Aquifex aeolicus tRNAArg(CCG)
-
pH 7.6, 60C
-
0.0004
guanine37 in Aquifex aeolicus tRNAGln(UUG)
-
pH 7.6, 60C
-
0.0006
guanine37 in Aquifex aeolicus tRNAHis(GUG)
-
pH 7.6, 60C
-
0.0009
guanine37 in Aquifex aeolicus tRNALeu(CAG)
-
pH 7.6, 60C
-
0.0007
guanine37 in Aquifex aeolicus tRNAPro(GGG)
-
pH 7.6, 60C
-
0.0000546 - 0.0057
guanine37 in Escherichia coli tRNA1Leu
-
0.0028
guanine37 in Escherichia coli tRNAPro
-
pH 8.0, 37C
-
0.002
guanine37 in Haloferax volcanii tRNACys(GCA)
-
pH 7.6, 60C
-
0.0005
guanine37 in Haloferax volcanii tRNALeu(CAA)
-
pH 7.6, 60C
-
0.0023
guanine37 in Haloferax volcanii tRNATrp(CCA)
-
pH 7.6, 60C
-
0.0019
guanine37 in Haloferax volcanii tRNATyr(GUA)
-
pH 7.6, 60C
-
0.00546 - 0.0086
guanine37 in human mitochondrial tRNAPro
-
0.018
guanine37 in human mitochondrial tRNAPro possessing an A36G37 sequence
pH 8.0, 37C
-
0.0033
guanine37 in in Escherichia coli tRNALeu(CAG)
-
pH 7.6, 60C
-
0.00028
guanine37 in Methanocaldococcus jannaschii tRNA(Cys)
-
pH 8.0, 50C
-
0.0007 - 0.0083
guanine37 in Methanocaldococcus jannaschii tRNACys
-
0.0012 - 0.0073
guanine37 in Methanocaldococcus jannaschii tRNAPro
-
0.027
guanine37 in tRNAArg
-
pH 8.0, temperature not specified in the publication
-
0.00047
guanine37 in tRNACys
recombinant enzyme, pH 7.3, 37C
-
0.00082 - 0.067
guanine37 in tRNAGlnCUG
-
0.0027
guanine37 in tRNAGlnG36A
-
pH 8.0, temperature not specified in the publication
-
0.184
guanine37 in tRNAGlnG36C
-
pH 8.0, temperature not specified in the publication
-
0.114
guanine37 in tRNAGlnG36U
-
pH 8.0, temperature not specified in the publication
-
0.0024 - 0.0625
guanine37 in tRNALeu
-
0.0043
guanine37 in tRNALeu(GAC)
-
pH 8.5, 37C
-
0.001
guanine37 in tRNAPro
-
pH 8.0, temperature not specified in the publication
-
0.000075
guanine37 in yeast tRNAAsp possessing a C36G37 sequence
pH 8.0, 37C
-
0.000244 - 0.019
guanine37 in yeast tRNAAsp possessing a G36G37 sequence
-
0.00059 - 0.046
guanine37 in yeast tRNAAsp possessing an A36G37 sequence
-
0.00058
guanine37 in yeast tRNAAsp possessing an U36G37 sequence
pH 8.0, 37C
-
0.0000457
guanine37 in yeast tRNAPhe possessing an A36G37 sequence
pH 8.0, 37C
-
0.0008
guanine37 in yeast tRNAPhe(GAA)
-
pH 7.6, 60C
-
0.00123
inosine37 in yeast tRNAAsp possessing a G36I37 sequence
below 0.00123 pH 8.0, 37C
-
0.0007
S-adenosyl-L-homocysteine
-
pH 8.5, 37C
0.00042 - 0.001
S-adenosyl-L-methionine
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.017
guanine37 in Escherichia coli tRNAPro
Escherichia coli
-
pH 8.0, 37C
-
0.01
guanine37 in Methanocaldococcus jannaschii tRNA(Cys)
Methanocaldococcus jannaschii
-
pH 8.0, 50C
-
0.0001 - 0.0083
guanine37 in Methanocaldococcus jannaschii tRNACys
-
0.0086 - 0.01
guanine37 in Methanocaldococcus jannaschii tRNAPro
-
0.078
guanine37 in tRNAArg
Haemophilus influenzae
-
pH 8.0, temperature not specified in the publication
-
0.023
guanine37 in tRNACys
Homo sapiens
Q32P41
recombinant enzyme, pH 7.3, 37C
-
0.0014 - 0.34
guanine37 in tRNAGlnCUG
-
0.36
guanine37 in tRNAGlnG36A, guanine37 in tRNAGlnG36C
Haemophilus influenzae
-
pH 8.0, temperature not specified in the publication
-
0.17
guanine37 in tRNAGlnG36U
Haemophilus influenzae
-
pH 8.0, temperature not specified in the publication
-
0.0015 - 0.32
guanine37 in tRNALeu
-
0.25
guanine37 in tRNALeu(GAC)
Streptococcus pneumoniae
-
pH 8.5, 37C
-
0.13
guanine37 in tRNAPro
Haemophilus influenzae
-
pH 8.0, temperature not specified in the publication
-
0.25
S-adenosyl-L-homocysteine
Streptococcus pneumoniae
-
pH 8.5, 37C
0.0001 - 0.09
S-adenosyl-L-methionine
additional information
additional information
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.1
guanine37 in Escherichia coli tRNAPro
Escherichia coli
-
pH 8.0, 37C
41324
36.9
guanine37 in Methanocaldococcus jannaschii tRNA(Cys)
Methanocaldococcus jannaschii
-
pH 8.0, 50C
41325
0.017 - 11.9
guanine37 in Methanocaldococcus jannaschii tRNACys
3953
1.7 - 7.22
guanine37 in Methanocaldococcus jannaschii tRNAPro
19385
29
guanine37 in tRNAArg
Haemophilus influenzae
-
pH 8.0, temperature not specified in the publication
210530
50
guanine37 in tRNACys
Homo sapiens
Q32P41
recombinant enzyme, pH 7.3, 37C
170887
0.000078 - 280
guanine37 in tRNAGlnCUG
210525
130
guanine37 in tRNAGlnG36A
Haemophilus influenzae
-
pH 8.0, temperature not specified in the publication
210526
2
guanine37 in tRNAGlnG36C
Haemophilus influenzae
-
pH 8.0, temperature not specified in the publication
210527
15
guanine37 in tRNAGlnG36U
Haemophilus influenzae
-
pH 8.0, temperature not specified in the publication
210528
0.024 - 40
guanine37 in tRNALeu
170888
357
guanine37 in tRNALeu(GAC)
Streptococcus pneumoniae
-
pH 8.5, 37C
41320
130
guanine37 in tRNAPro
Haemophilus influenzae
-
pH 8.0, temperature not specified in the publication
210529
58
S-adenosyl-L-homocysteine
Streptococcus pneumoniae
-
pH 8.5, 37C
36
0.2 - 12.2
S-adenosyl-L-methionine
24
additional information
additional information
2
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01 - 0.014
5'-[(2-aminoethyl)thio]-5'-deoxy-adenosine
0.405 - 0.461
6-Chloropurine
0.0347 - 0.0642
adenosine
0.0031 - 0.0079
AdoButyn
0.00143 - 0.0259
AdoPropen
0.488 - 13.4
Inosine
6.7 - 18.2
methionine
0.0012 - 0.03
methylthioadenosine
0.00049 - 0.0042
S-adenosyl-L-homocysteine
33 - 44
S-methyl-L-cysteine
0.00033 - 0.00062
sinefungin
additional information
additional information
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9.8
-
preincubation of Trm5 at pH 6.0, followed by adjustment of the solution to pH 8.0, does not cause irreversible inactivation of the enzyme. Enzyme treated in this manner retained equivalent activity in single-turnover assay
6 - 8.5
-
pH 6.0: about 50% of maximal activity, pH 8.5: about 75% of maximal activity
6.4 - 8.4
6.5 - 9.5
pH-activity profile
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 43
assay at
60
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
-
85C is the optimal growth temperature
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Anaplasma phagocytophilum (strain HZ)
Anaplasma phagocytophilum (strain HZ)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 / STM815)
Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 / STM815)
Pyrococcus abyssi (strain GE5 / Orsay)
Pyrococcus abyssi (strain GE5 / Orsay)
Pyrococcus abyssi (strain GE5 / Orsay)
Pyrococcus abyssi (strain GE5 / Orsay)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30586
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2 * 30586, calculated from sequence
32000
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2 * 32000
42000
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x * 42000, SDS-PAGE
60500
gel filtration
62000
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gel filtration
64000
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dynamic light-scattering
65000
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dynamic light scattering
69000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 42000, SDS-PAGE
homodimer
monomer
1 * 60500, SDS-PAGE
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure at 2.6 A resolution
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crystal structure of TrmD complexed with S-adenosyl homocysteine, determined at 2.5 A resolution
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crystal structures of TrmD from Haemophilus influenzae, as binary complexes with either S-adenosyl-L-methionine or S-adenosyl-L-homocysteine, as a ternary complex with S-adenosyl-L-homocysteine and phosphate, and as an apo form
purified enzyme in ternary complex with Thermotoga maritima wild-type and mutant tRNA substrates, e.g. tRNAGlnCUG, and the S-adenosyl-L-methionine analogue sinefungin, and enzyme in TrmD-AdoMet and TrmD-sinefungin binary complexes, 0.0012 ml of 10 mg/ml protein and 1 mM AdoMet or sinefungin, is mixed with 0.0012 ml of reservoir solution, consisting of 0.8-0.85 M sodium citrate and 0.1 M N-cyclohexyl-2-minoethanesulfonic acid, pH 8.0-8.4, 20C, for the trinary complex 5 mg/ml protein is mixed with tRNA in a 5:1 ratio, and 1 mM sinefungin, 0.0012 ml are mixed with 0.0015 ml of reservoir solution containing 0.1 M sodium acetate trihydrate, pH 4.6, 0.8 M ammonium phosphate monobasic, and 4% w/v PEG 20,000, X-ray diffraction structure determination and analysis at 3.0 A, 1.55 A, and 1.6 A resolutions, respectively, structure modeling
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TrmD from Haemophilus influenzae with both N- and C-terminal tags is crystallized at 24C using sodium acetate as a precipitant. Native X-ray diffraction data are collected to 1.85 A resolution. The crystals are rhombohedral, belonging to the space group R32, with unit-cell parameters a = b = 98.05, c = 176.79 A, alpha = beta = 90, gamma = 120
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analysis of the crystal structure of the Trm5-tRNA-AdoMet ternary complex
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crystal structure of Trm5 in complex with the methyl donor analogue sinefungin at 2.2 A resolution, vapor diffusion method at 20C
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purified enzyme in complex with Thermotoga maritima wild-type and mutant tRNA substrates, e.g. tRNAGlnCUG, and the S-adenosyl-L-methionine analogue sinefungin, X-ray crystal structure analysis, PDB ID 3AKZ
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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the Cys20Cys20 disulfide bond between its two subunits enhances the protein stability at 85C
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant C-terminally His-tagged enzyme, lacking the N-terminal peptide V2LWILWRP9, from Escherichia coli by metal ion affinity chromatography and anion exchange chromatography
recombinant enzyme
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recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by affinity chromatography
recombinant N-terminally His-tagged wild-type and S88L mutant enzymes from Escherichia coli strain SG13009 by nickel affinity chromatography
recombinant protein
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Trm5p is purified as a fusion protein with maltose-binding protein
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli by using a His-tagged T7 expression vector
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expression in Escherichia coli
expression in Escherichia coli as a fusion protein with maltose-binding protein
gene TRM5, recombinant expression of C-terminally His-tagged enzyme, lacking the N-terminal peptide V2LWILWRP9, in Escherichia coli
gene trm5, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene trmD, recombinant expression of N-terminally His-tagged wild-type and S88L mutant enzymes in Escherichia coli strain SG13009
gene TRMT5, genetic structure and genotyping
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recombinant TrmD from Haemophilus influenzae with both N- and C-terminal tags is overexpressed in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C20S
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the C20S mutant protein forms a dimer structure even though it is missing the Cys20Cys20 disulfide bond between its two subunits. Incubation at 85C 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 70C. 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 70C
A202S
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Km/Vmax for tRNA is 2fold higher than wild-type value
A25S
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Km/Vmax for tRNA is 2.9fold higher than wild-type value
A70S
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Km/Vmax for tRNA is 4fold higher than wild-type value
C112A
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Km/Vmax for tRNA is 7.6fold higher than wild-type value
D119A
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inactive mutant enzyme
D128A
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inactive mutant enzyme
D135A
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inactive mutant enzyme
D169A
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inactive mutant enzyme
D169E
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Km/Vmax for tRNA is 1.4fold higher than wild-type value
D50A
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Km/Vmax for tRNA is 4fold higher than wild-type value
E116A
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Km/Vmax for tRNA is 2fold higher than wild-type value
E130A
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Km/Vmax for tRNA is 2fold higher than wild-type value
E142A
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Km/Vmax for tRNA is 3.1fold higher than wild-type value
G113A
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Km/Vmax for tRNA is 5.3fold higher than wild-type value
G117A
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inactive mutant enzyme
G134A
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Km/Vmax for tRNA is 6.8fold higher than wild-type value
G140A
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Km/Vmax for tRNA is 8.5fold higher than wild-type value
G141A
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Km/Vmax for tRNA is 1.5fold lower than wild-type value
G189A
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Km/Vmax for tRNA is 8fold higher than wild-type value
G55A
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Km/Vmax for tRNA is 4.8fold higher than wild-type value
G59A
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inactive mutant enzyme
G91A
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inactive mutant enzyme
H180A
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Km/Vmax for tRNA is 5 fold higher than wild-type value
I204A
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inactive mutant enzyme
L138A
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Km/Vmax for tRNA is 1,7fold higher than wild-type value
L196A
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inactive mutant enzyme
L197A
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inactive mutant enzyme
M60A
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Km/Vmax for tRNA is 2.7fold higher than wild-type value
P184A
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inactive mutant enzyme
P193A
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inactive mutant enzyme
P53A
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Km/Vmax for tRNA is 2fold higher than wild-type value
R114A
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inactive mutant enzyme
R121A
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inactive mutant enzyme
R154A
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inactive mutant enzyme
R208A
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inactive mutant enzyme
R215A
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Km/Vmax for tRNA is 5fold higher than wild-type value
R219A
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Km/Vmax for tRNA is 4fold higher than wild-type value
S132A
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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
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inactive mutant enzyme
W131A
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Km/Vmax for tRNA is 1.3fold higher than wild-type value
W207A
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inactive mutant enzyme
W207F
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Km/Vmax for tRNA is 4fold higher than wild-type value
W207H
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Km/Vmax for tRNA is 5.6fold higher than wild-type value
Y136A
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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
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naturally occuring TRMT5 mutation, the mutant shows diminished G37 modification of a mitochondrial tRNA and a pathogenic phenotype
R291H
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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
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59% activity realtive to the wild-type
D223E
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site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme
D223L
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site-directed mutagenesis, the mutant shows complete loss of activity
D223N
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site-directed mutagenesis, the mutant shows complete loss of activity
E185A
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site-directed mutagenesis, the mutant shows complete loss of activity
E185D
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site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme
E185Q
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site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme
G205A/G207A
K137A
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site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme
K318A
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site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme
N225A
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kcat/Km for guanine37 in Methanocaldococcus jannaschii tRNACys is 5% of the wild-type value
N265H
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site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme
N265Q
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site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme
P226A
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kcat/Km for guanine37 in Methanocaldococcus jannaschii tRNACys is 6% of the wild-type value
R144A
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kcat/Km for guanine37 in Methanocaldococcus jannaschii tRNACys is 6% of the wild-type value
R145A
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site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme
R181A
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site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme
R186A
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site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme
Y176A
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kcat/Km for guanine37 in Methanocaldococcus jannaschii tRNACys is 5% of the wild-type value
Y177A
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site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme
Y177F
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site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
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TrmD has potential as a drug target
medicine
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the sequence and structural distinction of bacterial TrmD from the eukaryotic Trm5 suggests that strategies can be developed to specifically inhibit TrmD without a deleterious effect on humans
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