6.1.1.10: methionine-tRNA ligase
This is an abbreviated version!
For detailed information about methionine-tRNA ligase, go to the full flat file.
Word Map on EC 6.1.1.10
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6.1.1.10
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synthetases
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aminoacyl-trna
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aminoacylation
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anticodons
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homocysteine
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trnafmet
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thiolactone
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aarss
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isoleucyl-trna
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trypsin-modified
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isoleucylation
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noncognate
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tyrosyl-trna
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arc1p
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atp-ppi
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formylmethionine
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medicine
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leucyl-trna
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kmsks
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misacylation
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hcy-thiolactone
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ilers
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lysyl-trna
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trna-binding
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valrs
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valyl-trna
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cysteinyl-trna
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drug development
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pharmacology
- 6.1.1.10
- synthetases
- aminoacyl-trna
- aminoacylation
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anticodons
- homocysteine
- trnafmet
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thiolactone
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aarss
-
isoleucyl-trna
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trypsin-modified
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isoleucylation
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noncognate
- tyrosyl-trna
- arc1p
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atp-ppi
- formylmethionine
- medicine
- leucyl-trna
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kmsks
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misacylation
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hcy-thiolactone
- ilers
- lysyl-trna
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trna-binding
- valrs
- valyl-trna
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cysteinyl-trna
- drug development
- pharmacology
Reaction
Synonyms
hcMetRS, hmMetRS, let-65, MARS, mars-1, MetG, Methionine translase, Methionine--tRNA ligase, Methionyl tRNA synthetase, Methionyl-transfer ribonucleate synthetase, Methionyl-transfer ribonucleic acid synthetase, Methionyl-transfer RNA synthetase, methionyl-tRNA synthetase, methionyl-tRNA synthetase1, methionyl-tRNA-synthetase, MetRS, MetRS1, MetRS2, MetS, More, MRS, MRSapi, MRScyt, Synthetase, methionyl-transfer ribonucleate
ECTree
6.1.1.10 methionine-tRNA ligaseAdvanced search results
results (
results (KM Value
KM Value on EC 6.1.1.10 - methionine-tRNA ligase
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KM VALUE [mM] 
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
15.68
(S)-2-aminohex-5-enoic acid
ATP-diphosphate exchange reaction, pH 7.6
2.42
(S)-2-aminohex-5-ynoic acid
ATP-diphosphate exchange reaction, pH 7.6
4.56
L-trans-alpha-crotylglycine
ATP-diphosphate exchange reaction, pH 7.6
0.029
ATP
mutant D666A, pH and temperature not specified in the publication
0.375
ATP
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wild-type, first step of reaction, methionyl-adenylate formation
0.44
ATP
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mutant G54S, first step of reaction, methionyl-adenylate formation
0.475
ATP
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mutant H101N/G213C, first step of reaction, methionyl-adenylate formation
0.7
ATP
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mutant H101D, first step of reaction, methionyl-adenylate formation
0.78
ATP
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mutant V216A, first step of reaction, methionyl-adenylate formation
0.85
ATP
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mutant V216F/L203S, first step of reaction, methionyl-adenylate formation
0.98
ATP
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mutant D229E, first step of reaction, methionyl-adenylate formation
1
ATP
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mutant I57N, first step of reaction, methionyl-adenylate formation
1.35
ATP
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mutant G54S/L203S, first step of reaction, methionyl-adenylate formation
1.75
ATP
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mutant I57N/H101N, first step of reaction, methionyl-adenylate formation
1.2
CoA
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methionylation reaction, cytoplasmic isozyme, pH 7.8, 25°C
6.3
CoA
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methionylation reaction, mitochondrial isozyme, pH 7.8, 25°C
1.8
L-homocysteine
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editing reaction, mitochondrial isozyme, pH 7.8, 25°C
3.1
L-homocysteine
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editing reaction, cytoplasmic isozyme, pH 7.8, 25°C
0.006
L-methionine
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mutant I57N, first step of reaction, methionyl-adenylate formation
0.017
L-methionine
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mutant V216A, first step of reaction, methionyl-adenylate formation
0.02
L-methionine
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mutant I57N/V242F, ATP:diphosphate exchange reaction
0.025
L-methionine
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mutant V216F/L203S, first step of reaction, methionyl-adenylate formation
0.025
L-methionine
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wild-type, first step of reaction, methionyl-adenylate formation
0.055
L-methionine
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mutant G54S/L203S, first step of reaction, methionyl-adenylate formation
0.064
L-methionine
mutant D666A, pH and temperature not specified in the publication
0.085
L-methionine
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mutant I57N/I238F, ATP:diphosphate exchange reaction
0.092
L-methionine
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mutant D229E, first step of reaction, methionyl-adenylate formation
0.16
L-methionine
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mutant G54S, first step of reaction, methionyl-adenylate formation
0.19
L-methionine
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mutant I57N/H101N, first step of reaction, methionyl-adenylate formation
0.25
L-methionine
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mutant I57N/A247E, ATP:diphosphate exchange reaction
0.36
L-methionine
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mutant I57N/G54S, ATP:diphosphate exchange reaction
1.07
L-methionine
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mutant G54A/A64P, ATP:diphosphate exchange reaction
1.55
L-methionine
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mutant H101N/G213C, first step of reaction, methionyl-adenylate formation
14.8
L-methionine
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mutant H101D, first step of reaction, methionyl-adenylate formation
0.038
selenomethionine
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selenomethionine-dependent ATP-diphosphate exchange
0.0007
tRNA fraction from Saccharomyces cerevisiae
pH 7.5, 25°C, wild-type enzyme
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0.00075
tRNA fraction from Saccharomyces cerevisiae
pH 7.5, 25°C, truncated mutant
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0.00015
tRNAMet
pH 8.2, 37°C, mitochondrial tRNAMet from Bos taurus, recombinant enzyme
0.00016
tRNAMet
pH 8.2, 37°C, human mitochondrial wild-type tRNAMet, recombinant enzyme
0.0004
tRNAMet
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recombinant mitochondrial isozyme as GST-fusion protein, pH 7.8, 25°C
0.00055
tRNAMet
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wild-type, second step of reaction, tRNA aminoacylation
0.00064
tRNAMet
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mutant G54S/L203S, second step of reaction, tRNA aminoacylation
0.00065
tRNAMet
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mutant D229E, second step of reaction, tRNA aminoacylation
0.00066
tRNAMet
in vitro synthesized tRNAMet from Saccharomyces cerevisiae, pH 7.5, 25°C, wild-type enzyme
0.0008
tRNAMet
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mutant V216A, second step of reaction, tRNA aminoacylation
0.00096
tRNAMet
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mutant V216F/L203S, second step of reaction, tRNA aminoacylation
0.00102
tRNAMet
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mutant G54S, second step of reaction, tRNA aminoacylation
0.00121
tRNAMet
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mutant I57N/H101N, second step of reaction, tRNA aminoacylation
0.0021
tRNAMet
pH 8.2, 37°C, initiator tRNA from Escherichia coli, recombinant enzyme
0.0026
tRNAMet
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mutant I57N, second step of reaction, tRNA aminoacylation
0.0039
tRNAMet
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wild-type enzyme in the multi-enzyme complex and mutant K866A, pH 7.5, 25°C
0.0065
tRNAMet
in vitro synthesized tRNAMet from Saccharomyces cerevisiae, pH 7.5, 25°C, truncated mutant
0.015
tRNAMet
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recombinant cytoplasmic isozyme as GST-fusion protein, pH 7.8, 25°C
0.022
tRNAMet
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ATP-diphosphate exchange reaction, C-terminally truncated mutant
additional information
additional information
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Km-values of mutant enzymes in aminoacylation
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additional information
additional information
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Km-values of mutant enzymes in ATP-diphosphate exchange reaction
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additional information
additional information
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dissociation constants for wild-type and mutant enzymes
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additional information
additional information
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kinetics with Escherichia coli native tRNAMet and initiator tRNAMet, and Saccharomyces cerevisiae native tRNAMet and initiator tRNAMet, overview
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additional information
additional information
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steady-state kinetic parameters for tRNAMet aminoacylation and for MetRS-catalyzed diphosphate exchange of wild-type enzyme and mutants, overview
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