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Information on EC 6.1.1.10 - methionine-tRNA ligase and Organism(s) Escherichia coli and UniProt Accession P00959

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IUBMB Comments
In those organisms producing N-formylmethionyl-tRNAfMet for translation initiation, this enzyme also recognizes the initiator tRNAfMet and catalyses the formation of L-methionyl-tRNAfMet, the substrate for EC 2.1.2.9, methionyl-tRNA formyltransferase.
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Escherichia coli
UNIPROT: P00959
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The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Synonyms
methionyl-trna synthetase, metrs, methionyl trna synthetase, mars-1, metrs2, metrs1, hcmetrs, methionyl-trna-synthetase, let-65, methionine-trna ligase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Methionine translase
-
Methionine--tRNA ligase
-
Methionyl tRNA synthetase
-
Methionyl-transfer ribonucleate synthetase
-
Methionyl-transfer ribonucleic acid synthetase
-
Methionyl-transfer RNA synthetase
-
methionyl-tRNA synthetase
-
Synthetase, methionyl-transfer ribonucleate
-
Methionine translase
Methionine--tRNA ligase
Methionyl tRNA synthetase
Methionyl-transfer ribonucleate synthetase
Methionyl-transfer ribonucleic acid synthetase
Methionyl-transfer RNA synthetase
methionyl-tRNA synthetase
-
-
MetRS
Synthetase, methionyl-transfer ribonucleate
additional information
-
the enzyme is a class I aminoacyl-tRNA synthetase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + L-methionine + tRNAMet = AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
substrate binding and mechanism
ATP + L-methionine + tRNAMet = AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
esterification
-
esterification
Acylation
-
-
Aminoacylation
SYSTEMATIC NAME
IUBMB Comments
L-methionine:tRNAMet ligase (AMP-forming)
In those organisms producing N-formylmethionyl-tRNAfMet for translation initiation, this enzyme also recognizes the initiator tRNAfMet and catalyses the formation of L-methionyl-tRNAfMet, the substrate for EC 2.1.2.9, methionyl-tRNA formyltransferase.
CAS REGISTRY NUMBER
COMMENTARY hide
9033-22-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + (S)-2-aminohex-5-enoic acid + tRNAMet
AMP + diphosphate + (S)-2-aminohex-5-enoyl-tRNAMet
show the reaction diagram
ATP + (S)-2-aminohex-5-ynoic acid + tRNAMet
AMP + diphosphate + 2(S)-aminohex-5-ynoyl-tRNAMet
show the reaction diagram
500fold reduced activity compared to L-methionine
-
?
ATP + azidonorleucine + tRNAMet
AMP + diphosphate + azidonorleucinyl-tRNAMet
show the reaction diagram
MetRS SLL-mutant
-
-
?
ATP + azidonorleucine + tRNAMet
AMP + diphosphate + azidonorleucyl-tRNAMet
show the reaction diagram
activity of mutant L13G, overview
-
-
?
ATP + L-methionine + tRNAArg(CCU)
?
show the reaction diagram
tRNA mismethionylation
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
ATP + L-methionine + tRNAThr(CGU)
?
show the reaction diagram
tRNA mismethionylation
-
-
?
ATP + L-norleucine + tRNAMet
AMP + diphosphate + L-norleucyl-tRNAMet
show the reaction diagram
1050fold reduced activity compared to L-methionine
-
?
ATP + L-trans-alpha-crotylglycine + tRNAMet
AMP + diphosphate + L-trans-alpha-crotylglycyl-tRNAMet
show the reaction diagram
4700fold reduced activity compared to L-methionine
-
?
AMP + diphosphate + L-methionyl-tRNAMet
ATP + L-methionine + tRNAMet
show the reaction diagram
-
-
-
-
r
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + azidonorleucine + tRNAMet
AMP + diphosphate + azidonorleucyl-tRNAMet
show the reaction diagram
activity of mutant L13G, overview
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
-
enzyme binds 2 Mn2+ per dimer, no binding with the trypsin-modified monomer
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(S)-2-amino-heptanoic acid
L-methionine analogue, competitive
(S)-2-aminohex-5-enoic acid
L-methionine analogue, competitive
(S)-2-aminohex-5-ynoic acid
L-methionine analogue, competitive
L-6,6,6-trifluoronorleucine
L-methionine analogue, competitive
L-cis-alpha-crotylglycine
L-methionine analogue, competitive
L-norleucine
L-methionine analogue, competitive
L-norvaline
L-methionine analogue, competitive
L-trans-alpha-crotylglycine
L-methionine analogue, competitive
1,10-phenanthroline
-
little or no inhibition by 1,7-phenanthroline and 4,7-phenanthroline
2,2'-dipyridyl
-
-
4-[(E)-[([[N-(thiophen-2-ylcarbonyl)glycyl]amino]methyl)imino]methyl]benzoic acid
-
structure molecular modeling, binding mode, detailed overview
adenosine
-
maximal inhibition at MgCl2 concentration from 4.0 mM to 10 mM, effective inhibition at high concentration of diphosphate
ester analogues of L-methionyl adenylate
-
overview, modeling of interaction with the active site
hydroxamate analogues of L-methionyl adenylate
-
overview, modeling of the interaction with the active site
isovanilloid analogues of L-methionyl adenylate
-
overview, containing ribose biooisosteres
L-methionine hydroxamate
-
substrate analogue, inhibition mechanism, no inhibition of mutant T10M
NH4+
-
ATP-diphosphate exchange
Periodate-oxidized ATP
-
-
-
Periodate-oxidized tRNA
-
-
-
REP3123
-
-
REP8839
-
-
vanilloid analogues of L-methionyl adenylate
-
overview, containing ribose biooisosteres
additional information
-
large scale MetRS inhibitor screening, diverse compounds, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
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
0.0243
L-methionine
ATP-diphosphate exchange reaction, pH 7.6
4.12
L-norleucine
ATP-diphosphate exchange reaction, pH 7.6
4.56
L-trans-alpha-crotylglycine
ATP-diphosphate exchange reaction, pH 7.6
0.41 - 58
ATP
7.9 - 58
L-methionine
0.00303 - 0.04183
L-methionyl-tRNAMet
0.02 - 1.63
Met
0.0009 - 1
tRNAMet
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.35
(S)-2-aminohex-5-enoic acid
ATP-diphosphate exchange reaction, pH 7.6
2.6
(S)-2-aminohex-5-ynoic acid
ATP-diphosphate exchange reaction, pH 7.6
13.3
L-methionine
ATP-diphosphate exchange reaction, pH 7.6
2.15
L-norleucine
ATP-diphosphate exchange reaction, pH 7.6
1.82 - 2.94
L-trans-alpha-crotylglycine
3.4 - 5.6
ATP
3.4 - 5.6
L-methionine
0.011 - 0.157
L-methionyl-tRNAMet
0.037 - 47
tRNAMet
additional information
additional information
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.5 - 51
L-methionyl-tRNAMet
2 - 250
tRNAMet
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0196
L-methionine hydroxamate
-
pH 8.0
0.0019
REP3123
-
-
0.000225
REP8839
-
-
additional information
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000237
4-[(E)-[([[N-(thiophen-2-ylcarbonyl)glycyl]amino]methyl)imino]methyl]benzoic acid
Escherichia coli
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
66.7
-
ATP-diphosphate exchange
additional information
incorporation level of L-methionine into proteins
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
8
-
tRNA aminoacylation assay
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
tRNA aminoacylation assay at room temperature for 30 min for IC50 determinations
25
-
assay at
30
-
tRNA aminoacylation assay at 30°C for 1 to 7.5 min for initial rate determination
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
enzyme-mediated methionine-misacylation reduces intracellular reactive oxygen species levels and protects cells from oxidative damage
additional information
-
the catalytic domains of class I aminoacyl-tRNA synthetases are built around a conserved Rossmann nucleotide binding fold, with additional polypeptide domains responsible for tRNA binding or hydrolytic editing of misacylated substrates, structural comparisons of class Ia and Ib enzymes, overview. Structural integrity of the helix-turn-strand-helix motif contributes more to tRNA aminoacylation than does amino acid identity
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
76000
-
2 * 76000
76127
-
x * 76127, calculation from nucleotide sequence
85000
-
2 * 85000, SDS-PAGE after boiling the enzyme in 2% SDS and 1% mercaptoethanol, reduction and carboxymethylation in 6 M guanidine hydrochloride
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 76127, calculation from nucleotide sequence
dimer
monomer
additional information
-
three-dimensional solution structure
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
-
the enzyme is phosphorylated at Ser209 and Ser825 by extracellular signal-related kinase during oxidative stress
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals of purified free enzyme and enzyme complexed with L-methionine are diffused by several methionine analogues, i.e. L-difluoromethionine, L-trifluoromethionine, D,L-phosphomethionine and D,L-iodo-methionine, X-ray diffraction structure determination at 1.9 A resolution and analysis
the crystal structure of the mutated MetRS is determined in the apo form as well as complexed with methionine or azidonorleucine to 1.4 to 1.7 A resolution
at 2.5 A resolution
-
crystal structure analysis, catalytic core, tertiary structure of the C-terminal tRNA-binding appendices determined by binding analysis of catalytically inactive tRNA homologous binding proteins: tRNA-binding protein 111 and endothelial monocyte-activating polypeptide II, i.e. EMAPII, comparison of structure with other aminoacyl tRNA synthetases from other organism
-
crystal structure determination by X-ray diffraction at 2.0 A resolution, 3D-structure of the C-terminally truncated enzyme, species-specific knuckle structures are determined
-
crystal structure of the tryptic fragment of the enzyme complexed with ATP, at 2.5 A resolution
-
crystals of active fragment of MW 64000 obtained by controlled proteolysis
-
purified enzyme complexed with L-methionine, protein solution: 8 mg/ml protein, 10 mM KH2PO4, pH 7.3, 10 mM 2-mercaptoethanol, initiating by microseeding with crystals from the free enzyme at 20°C, in 1.1 ammonium citrate, 0.5% v/v methyl-2,4-pentanediol, 0.6 mM L-methionine, 2 mM 2-mercaptoethanol, 30 mM phosphate buffer, pH 7.0, 1 day, X-ray diffraction structure determination at 1.8 A resolution, structure analysis and modeling
-
truncated form
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C477S
the mutant shows at least a 2fold increase in mismethionylation percentage compared to the wild type enzyme
D369A
the mutant displays at least a 6fold reduction in mismethionylation percentage compared to the wild type enzyme
F277L
the mutant displays at least a 6fold reduction in mismethionylation percentage compared to the wild type enzyme
L13G
saturation mutagenesis, three mutant clones from screening of a saturation mutagenesis library, the mutants are capable of incorporating the long-chain amino acid azidonorleucine into recombinant proteins with modest efficiency
L13S/Y260L/H301L
MetRS SLL-mutant with modified substrate specificity
Q211
the mutant shows at least a 2fold increase in mismethionylation percentage compared to the wild type enzyme
Q213A
the mutant shows at least a 2fold increase in mismethionylation percentage compared to the wild type enzyme
T489A
the mutant shows at least a 2fold increase in mismethionylation percentage compared to the wild type enzyme
W221A
the mutant displays at least a 6fold reduction in mismethionylation percentage compared to the wild type enzyme
W461D
the mutant displays at least a 6fold reduction in mismethionylation percentage compared to the wild type enzyme
Y490A
the mutant shows at least a 2fold increase in mismethionylation percentage compared to the wild type enzyme
A256X
D369A
-
site-directed mutagenesis in the MetRS SCF, the mutant shows reduced transfer RNA aminoacylation and 125fold loss in tRNAMet aminoacylation efficiency compared to the wild-type enzyme
D369K/K295D
-
site-directed mutagenesis in the MetRS SCF, the mutant shows reduced transfer RNA aminoacylation compared to the wild-type enzyme
D369N
-
site-directed mutagenesis in the MetRS SCF, the mutant shows reduced transfer RNA aminoacylation and 60fold loss in tRNAMet aminoacylation efficiency compared to the wild-type enzyme
D666A
-
activity is similar to the wild-type enzyme
G23A
-
mutant enzymes: L22A variant, G23A variant, G23P variant, H21N variant, H21Q variant, H24N variant, and H24Q variant, with reduced catalytic efficience and lowered maximal rate
G23P
-
mutant enzymes: L22A variant, G23A variant, G23P variant, H21N variant, H21Q variant, H24N variant, and H24Q variant, with reduced catalytic efficience and lowered maximal rate
H21N
-
mutant enzymes: L22A variant, G23A variant, G23P variant, H21N variant, H21Q variant, H24N variant, and H24Q variant, with reduced catalytic efficience and lowered maximal rate
H21Q
-
mutant enzymes: L22A variant, G23A variant, G23P variant, H21N variant, H21Q variant, H24N variant, and H24Q variant, with reduced catalytic efficience and lowered maximal rate
H24N
-
mutant enzymes: L22A variant, G23A variant, G23P variant, H21N variant, H21Q variant, H24N variant, and H24Q variant, with reduced catalytic efficience and lowered maximal rate
H24Q
-
mutant enzymes: L22A variant, G23A variant, G23P variant, H21N variant, H21Q variant, H24N variant, and H24Q variant, with reduced catalytic efficience and lowered maximal rate
H301L
-
saturation mutagenesis, the mutant shows altered amino acid substrate binding compared to the wild-type enzyme
K295A
-
site-directed mutagenesis in the MetRS SCF, the mutant shows reduced transfer RNA aminoacylation compared to the wild-type enzyme
K295V
-
site-directed mutagenesis in the MetRS SCF, the mutant shows reduced transfer RNA aminoacylation compared to the wild-type enzyme
K335Q
-
mutants produced by site-directed mutagenesis, Lys335-Gln substitution results in a complete loss of activity, similar loss of activity is observed when Lys335 is changed into alanine, glutamic acid, or arginine
L13N/Y260L/H301L
-
the mutant enzyme enables cells to use the methionine surrogate azidonorleucine in protein synthesis
L13S
-
saturation mutagenesis, the mutant shows altered amino acid substrate binding compared to the wild-type enzyme
L22A
-
mutant enzymes: L22A variant, G23A variant, G23P variant, H21N variant, H21Q variant, H24N variant, and H24Q variant, with reduced catalytic efficience and lowered maximal rate
M218A
M233I
P257X
-
saturation mutagenesis, the mutant shows altered amino acid substrate binding compared to the wild-type enzyme
S209A/S825A
-
the mutant shows minimal phosphorylation upon incubation with extracellular signal-related kinase and leads to reduced activity compared to the wild type enzyme
S209D/S825D
-
the mutation mimicks dual phosphorylation and leads to reduced activity compared to the wild type enzyme
T10M
-
natural mutant, 5% activity compared to the wild-type, complementation of an enzyme-deficient Escherichia coli strain, no inhibition by L-methionine hydroxamate
Y15A
-
natural mutant, very low residual activity, complementation of an enzyme-deficient Escherichia coli strain
Y260L
-
saturation mutagenesis, the mutant shows altered amino acid substrate binding compared to the wild-type enzyme
Y94H
-
natural mutant, unstable, no complementation of an enzyme-deficient Escherichia coli strain
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
51
-
wild-type enzyme, half-life 16 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
several cycles of freezing and thawing, cause no loss of activity of wild-type enzyme in crude extract
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, about 35% loss of activity after 6 months, wild-type enzyme in crude extract
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
affinity column chromatography
recombinant His-tagged mutants from Escherichia coli strain XL-1 Blue by nickel affinity chromatography
recombinnat His-tagged mutants from Escherichia coli strain XL-1 Blue by nickel affinity chromatography
the SLL-mutant is purified on columns containing Talon affinity resin and Q-Hiload resin, respectively
affinity chromatograph
-
recombinant His-tagged mutant enzymes from strain DH10B by nickel affinity chromatography
-
recombinant N-terminally His6-tagged MetRS monomer from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expression in an auxotroph Escherichia coli strain
expression of His-tagged mutants in Escherichia coli strain XL-1 Blue
the unmutated monomeric versions of MetRS, truncated at residue 548, M547, is produced from the plasmid pBSM547, the pMTY21-sll plasmid codes for an N-terminally 6xHis-tagged M547 MetRS, leading to expression of the MetRS-SLL mutant
expressed in HEK-293 cells
-
expressed in HEK-293T cells
-
expression of an N-terminally His6-tagged MetRS monomer in Escherichia coli strain BL21(DE3)
-
expression of mutant enzymes
-
gene metE, genetic library construction and expression, expression of His-tagged mutant enzymes in strains DH10B and in DH10B Met-
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
facile, after unfolding with 5 M guanidine under conditions where zinc is not sequestred
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schmitt, E.; Panvert, M.; Blanquet, S.; Mechulam, Y.
Transition state stabilization by the `high' motif of class I aminoacyl-tRNA synthetases. The case of Escherichia coli methionyl-tRNA synthetase
Nucleic Acids Res.
23
4793-4798
1995
Escherichia coli
Manually annotated by BRENDA team
Meinnel, T.; Mechulam, Y.; Dardel, F.; Schmitter, J.M.; Hountondji, C.; Brunie, S.; Dessen, P.; Fayat, G.; Blanquet, S.
Methionyl-tRNA synthetase from E. coli - A review
Biochimie
72
625-632
1990
Escherichia coli
Manually annotated by BRENDA team
Fourmy, D.; Dardel, F.; Blanquet, S.
Methionyl-tRNA synthetase zinc binding domain
J. Mol. Biol.
231
1078-1089
1993
Escherichia coli
Manually annotated by BRENDA team
Brunie, S.; Zelwer, C.; Risler, J.L.
Crystallographic study at 2.5 A resolution of the interaction of methionyl-tRNA synthetase from Escherichia coli with ATP
J. Mol. Biol.
216
411-424
1990
Escherichia coli
Manually annotated by BRENDA team
Jakubowski, H.; Goldman, E.
Synthesis of homocysteine thiolactone by methionyl-tRNA synthetase in cultured mammalian cells
FEBS Lett.
317
237-240
1993
Saccharomyces cerevisiae, Cricetulus griseus, Escherichia coli, Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Robert-Gero, M.; Waller, J.P.
Purification of methionyl-tRNA synthetase from Escherichia coli K12 by affinity chromatography
Eur. J. Biochem.
31
315-319
1972
Escherichia coli
Manually annotated by BRENDA team
Lawrence, F.
Effect of adenosine on methionyl-tRNA synthetase
Eur. J. Biochem.
40
493-500
1973
Escherichia coli
Manually annotated by BRENDA team
Koch, G.L.E.; Bruton, C.J.
The subunit structure of methionyl-tRNA synthetase from Escherichia coli
FEBS Lett.
40
180-182
1974
Escherichia coli, Escherichia coli EM
Manually annotated by BRENDA team
Posorske, L.H.; Cohn, M.; Yanagisawa, N.; Auld, D.S.
Methionyl-tRNA synthetase of Escherichia coli. A zinc metalloprotein
Biochim. Biophys. Acta
576
128-133
1979
Escherichia coli
Manually annotated by BRENDA team
Armstrong, J.B.; Fairfield, J.A.
A new method for the isolation of methionyl transfer synthetase mutants from Escherichia coli
Can. J. Microbiol.
21
754-758
1975
Escherichia coli
Manually annotated by BRENDA team
Zelwer, C.; Risler, J.L.; Monteilhet, C.
A low-resolution model of crystalline methionyl-transfer RNA synthetase from Escherichia coli
J. Mol. Biol.
102
93-101
1976
Escherichia coli
Manually annotated by BRENDA team
Zelwer, C.; Risler, J.L.; Brunie, S.
Crystal structure of Escherichia coli methionyl-tRNA synthetase at 2.5 A resolution
J. Mol. Biol.
155
63-81
1982
Escherichia coli
Manually annotated by BRENDA team
Dardel, F.; Fayat, G.; Blanqauet, S.
Molecular cloning and primary structure of the Escherichia coli methionyl-tRNA synthetase gene
J. Bacteriol.
160
1115-1122
1984
Escherichia coli
Manually annotated by BRENDA team
Deniziak, M.A.; Barciszewski, J.
Methionyl-tRNA synthetase
Acta Biochim. Pol.
48
337-350
2001
Escherichia coli, Thermus thermophilus
Manually annotated by BRENDA team
Crepin, T.; Schmitt, E.; Blanquet, S.; Mechulam, Y.
Structure and function of the C-terminal domain of methionyl-tRNA synthetase
Biochemistry
41
13003-13011
2002
Escherichia coli, Pyrococcus abyssi (Q9V011), Pyrococcus abyssi
Manually annotated by BRENDA team
Lee, J.; Kang, S.U.; Kim, S.Y.; Kim, S.E.; Kang, M.K.; Jo, Y.J.; Kim, S.
Ester and hydroxamate analogues of methionyl and isoleucyl adenylates as inhibitors of methionyl-tRNA and isoleucyl-tRNA synthetases
Bioorg. Med. Chem. Lett.
11
961-964
2001
Escherichia coli
Manually annotated by BRENDA team
Lee, J.; Kang, S.U.; Kim, S.Y.; Kim, S.E.; Job, Y.J.; Kim, S.
Vanilloid and isovanilloid analogues as inhibitors of methionyl-tRNA and isoleucyl-tRNA synthetases
Bioorg. Med. Chem. Lett.
11
965-968
2001
Escherichia coli
Manually annotated by BRENDA team
Kim, S.; Jo, Y.J.; Lee, S.H.; Motegi, H.; Shiba, K.; Sassanfar, M.; Martinis, S.A.
Biochemical and phylogenetic analyses of methionyl-tRNA synthetase isolated from a pathogenic microorganism, Mycobacterium tuberculosis
FEBS Lett.
427
259-262
1998
Escherichia coli, Mycobacterium tuberculosis
Manually annotated by BRENDA team
Jo, Y.J.; Lee, S.W.; Jo, M.K.; Lee, J.W.; Kang, M.K.; Yoon, J.H.; Kim, S.
Methionine analogue probes functionally important residues in active site of methionyl-tRNA synthetase
J. Biochem. Mol. Biol.
32
547-553
1999
Escherichia coli
-
Manually annotated by BRENDA team
Mechulam, Y.; Schmitt, E.; Maveyraud, L.; Zelwer, C.; Nureki, O.; Yokoyama, S.; Konno, M.; Blanquet, S.
Crystal structure of Escherichia coli methionyl-tRNA synthetase highlights species-specific features
J. Mol. Biol.
294
1287-1297
1999
Escherichia coli
Manually annotated by BRENDA team
Serre, L.; Verdon, G.; Choinowski, T.; Hervouet, N.; Risler, J.L.; Zelwer, C.
How methionyl-tRNA synthetase creates its amino acid recognition pocket upon L-methionine binding
J. Mol. Biol.
306
863-876
2001
Escherichia coli
Manually annotated by BRENDA team
Crepin, T.; Schmitt, E.; Mechulam, Y.; Sampson, P.B.; Vaughan, M.D.; Honek, J.F.; Blanquet, S.
Use of analogues of methionine and methionyl adenylate to sample conformational changes during catalysis in Escherichia coli methionyl-tRNA synthetase
J. Mol. Biol.
332
59-72
2003
Escherichia coli (P00959), Escherichia coli
Manually annotated by BRENDA team
Kiick, K.L.; Tirrell, D.A.
Protein Engineering by In Vivo Incorporation of Non-Natural Amino Acids: Control of Incorporation of Methionine Analogues by Methionyl-tRNA Synthetase
Tetrahedron
56
9487-9493
2000
Escherichia coli (P00959)
-
Manually annotated by BRENDA team
Yoo, T.H.; Tirrell, D.A.
High-throughput screening for methionyl-tRNA synthetases that enable residue-specific incorporation of noncanonical amino acids into recombinant proteins in bacterial cells
Angew. Chem.
46
5340-5343
2007
Escherichia coli
Manually annotated by BRENDA team
Kim, S.Y.; Lee, Y.S.; Kang, T.; Kim, S.; Lee, J.
Pharmacophore-based virtual screening: the discovery of novel methionyl-tRNA synthetase inhibitors
Bioorg. Med. Chem. Lett.
16
4898-4907
2006
Escherichia coli
Manually annotated by BRENDA team
Link, A.J.; Vink, M.K.; Agard, N.J.; Prescher, J.A.; Bertozzi, C.R.; Tirrell, D.A.
Discovery of aminoacyl-tRNA synthetase activity through cell-surface display of noncanonical amino acids
Proc. Natl. Acad. Sci. USA
103
10180-10185
2006
Escherichia coli (P00959), Escherichia coli
Manually annotated by BRENDA team
Ghosh, A.; Vishveshwara, S.
A study of communication pathways in methionyl-tRNA synthetase by molecular dynamics simulations and structure network analysis
Proc. Natl. Acad. Sci. USA
104
15711-15716
2007
Escherichia coli
Manually annotated by BRENDA team
Green, L.; Bullard, J.; Ribble, W.; Dean, F.; Ayers, D.; Ochsner, U.; Janjic, N.; Jarvis, T.
Inhibition of methionyl-tRNA synthetase by REP8839 and effects of resistance mutations on enzyme activity
Antimicrob. Agents Chemother.
53
86-94
2009
Streptococcus pneumoniae, Escherichia coli, Haemophilus influenzae, Homo sapiens, Staphylococcus aureus
Manually annotated by BRENDA team
Critchley, I.A.; Green, L.S.; Young, C.L.; Bullard, J.M.; Evans, R.J.; Price, M.; Jarvis, T.C.; Guiles, J.W.; Janjic, N.; Ochsner, U.A.
Spectrum of activity and mode of action of REP3123, a new antibiotic to treat Clostridium difficile infections
J. Antimicrob. Chemother.
63
954-963
2009
Clostridioides difficile, Streptococcus pneumoniae, Escherichia coli, Haemophilus influenzae, Homo sapiens, Staphylococcus aureus
Manually annotated by BRENDA team
Schmitt, E.; Tanrikulu, I.C.; Yoo, T.H.; Panvert, M.; Tirrell, D.A.; Mechulam, Y.
Switching from an induced-fit to a lock-and-key mechanism in an aminoacyl-tRNA synthetase with modified specificity
J. Mol. Biol.
394
843-851
2009
Escherichia coli (P00959)
Manually annotated by BRENDA team
Casina, V.C.; Lobashevsky, A.A.; McKinney, W.E.; Brown, C.L.; Alexander, R.W.
Role for a conserved structural motif in assembly of a class I aminoacyl-tRNA synthetase active site
Biochemistry
50
763-769
2011
Escherichia coli
Manually annotated by BRENDA team
Jones, T.E.; Alexander, R.W.; Pan, T.
Misacylation of specific nonmethionyl tRNAs by a bacterial methionyl-tRNA synthetase
Proc. Natl. Acad. Sci. USA
108
6933-6938
2011
Escherichia coli (P00959), Escherichia coli
Manually annotated by BRENDA team
Ngo, J.T.; Schuman, E.M.; Tirrell, D.A.
Mutant methionyl-tRNA synthetase from bacteria enables site-selective N-terminal labeling of proteins expressed in mammalian cells
Proc. Natl. Acad. Sci. USA
110
4992-4997
2013
Escherichia coli
Manually annotated by BRENDA team
Lee, J.Y.; Kim, D.G.; Kim, B.G.; Yang, W.S.; Hong, J.; Kang, T.; Oh, Y.S.; Kim, K.R.; Han, B.W.; Hwang, B.J.; Kang, B.S.; Kang, M.S.; Kim, M.H.; Kwon, N.H.; Kim, S.
Promiscuous methionyl-tRNA synthetase mediates adaptive mistranslation to protect cells against oxidative stress
J. Cell Sci.
127
4234-4245
2014
Escherichia coli
Manually annotated by BRENDA team