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Information on EC 6.1.1.10 - methionine-tRNA ligase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P00958
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6.1.1.10 methionine-tRNA ligaseIUBMB 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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Word Map
- 6.1.1.10
- synthetases
- aminoacyl-trna
- aminoacylation
-
anticodons
- homocysteine
- trnafmet
-
thiolactone
-
aarss
-
isoleucyl-trna
-
trypsin-modified
-
isoleucylation
-
noncognate
- tyrosyl-trna
- arc1p
-
atp-ppi
- formylmethionine
- medicine
- leucyl-trna
-
kmsks
-
misacylation
-
hcy-thiolactone
- ilers
- lysyl-trna
-
trna-binding
- valrs
- valyl-trna
-
cysteinyl-trna
- drug development
- pharmacology
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Methionine translase
Methionine--tRNA ligase
Methionyl tRNA synthetase
Methionyl-transfer ribonucleate synthetase
Methionyl-transfer ribonucleic acid synthetase
Methionyl-transfer RNA synthetase
MetRS
Synthetase, methionyl-transfer ribonucleate
Methionine translase
-
-
-
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Methionine--tRNA ligase
-
-
-
-
Methionyl tRNA synthetase
-
-
-
-
Methionyl-transfer ribonucleate synthetase
-
-
-
-
Methionyl-transfer ribonucleic acid synthetase
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-
-
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Methionyl-transfer RNA synthetase
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-
-
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MetRS
-
-
-
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Synthetase, methionyl-transfer ribonucleate
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-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + L-methionine + tRNAMet = AMP + diphosphate + L-methionyl-tRNAMet
amino acid residues D138, R139, and F135 are important for activity
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
esterification
Aminoacylation
esterification
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-
-
-
Aminoacylation
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-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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-
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
9033-22-1
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
-
-
-
?
ATP + L-homocysteine + tRNAMet
?
-
edition and aminoacylation by cytoplasmic and mitochondrial isozyme
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
-
-
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
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initiator and elongation tRNAMet, cytoplasmic and mitochondrial isozyme
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?
additional information
?
-
MetRS interacts with the accessory protein Arc1p, interaction mode and structure, overview
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-
?
additional information
?
-
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MetRS interacts with the accessory protein Arc1p, interaction mode and structure, overview
-
-
?
additional information
?
-
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homocysteine thiolactone is formed as a product of an error-editing reaction, which prevents incorporation of homocysteine into tRNA and protein (not enzyme from temperature-sensitive mutant of CHO-cells, at non-permissive temperature)
-
-
?
additional information
?
-
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the isozymes also perform the ATP-diphosphate exchange reaction
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
-
-
-
?
ATP + L-homocysteine + tRNAMet
?
-
edition and aminoacylation by cytoplasmic and mitochondrial isozyme
-
?
ATP + L-methionine + tRNAMet
AMP + diphosphate + L-methionyl-tRNAMet
-
initiator and elongation tRNAMet, cytoplasmic and mitochondrial isozyme
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
-
2 binding sites, 0.14 mM tightly bound zinc is present in 1 mol of cytoplasmic isozyme, but not in the mitochondrial one, required for stability and activity of the cytoplasmic isozyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
complete inhibition of the cytoplasmic isozyme at 1 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Arc1p-N
residues 1-122 of Arc1p, recombinantly expressed, crystal structure analysis, three interacting domains, MetRS-NArc1p-N hetero-dimer resembles a classical GST homo-dimer, overview
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Arc1p-N
residues 1-122 of Arc1p, recombinantly expressed, crystal structure analysis, three interacting domains, MetRS-N-Arc1p-N hetero-dimer resembles a classical GST homo-dimer, overview
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.2
CoA
-
methionylation reaction, cytoplasmic isozyme, pH 7.8, 25°C
6.3
CoA
-
methionylation reaction, mitochondrial isozyme, pH 7.8, 25°C
1.8
L-homocysteine
-
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
0.0004
tRNAMet
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recombinant mitochondrial isozyme as GST-fusion protein, pH 7.8, 25°C
0.015
tRNAMet
-
recombinant cytoplasmic isozyme as GST-fusion protein, pH 7.8, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.7
CoA
-
methionylation reaction, cytoplasmic isozyme, pH 7.8, 25°C
1.6
CoA
-
methionylation reaction, mitochondrial isozyme, pH 7.8, 25°C
0.5
L-homocysteine
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editing reaction, mitochondrial isozyme, pH 7.8, 25°C
0.69
L-homocysteine
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editing reaction, cytoplasmic isozyme, pH 7.8, 25°C
6.08
L-homocysteine
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editing reaction, cytoplasmic isozyme, pH 7.8, 25°C
0.2
tRNAMet
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recombinant mitochondrial isozyme as GST-fusion protein, pH 7.8, 25°C
1
tRNAMet
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recombinant cytoplasmic isozyme as GST-fusion protein, pH 7.8, 25°C
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
mitochondrial isozyme contains no zinc-finger motif and no insertion domain in the nucleotide-binding fold
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cytoplasmic isozyme has a zinc-finger motif and an insertion domain that divides the nucleotide-binding fold into 2 halves
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant MetRS-N-Arc1p-N complex, hanging drop vapour diffusion method, 0.002 ml protein solution containing 15 mg/ml protein in in 20 mM HEPES, 150 mM NaCl, 5 mM MgCl2, 1 mM DTT, pH 7.2 with NaOH, is mixed with 0.002 ml reservoir solution containing 8-14% PEG 20000, 1-3% dioxane, 100 mM bicine, pH 9.0, X-ray diffraction structure determination and analysis at 2.2-2.5 A resolution
purified recombinant MetRS-NArc1p-N complex, hanging drop vapour diffusion method, 0.002 ml protein solution containing 15 mg/ml protein in in 20 mM HEPES, 150 mM NaCl, 5 mM MgCl2, 1 mM DTT, pH 7.2 with NaOH, is mixed with 0.002 ml reservoir solution containing 814% PEG 20000, 13% dioxane, 100 mM bicine, pH 9.0, X-ray diffraction structure determination and analysis at 2.2-2.5 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A355C
-
site-directed mutagenesis, 115% activity compared to the wild-type enzyme, in vivo complementation of a deficient yeast strain
C350A
-
site-directed mutagenesis, 1.5% activity compared to the wild-type enzyme, no in vivo complementation of a deficient yeast strain
C353A
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site-directed mutagenesis, catalytically inactive, no in vivo complementation of a deficient yeast strain
C367A
-
site-directed mutagenesis, catalytically inactive, no in vivo complementation of a deficient yeast strain, mutant shows a second zinc-binding knuckle structure
D348G
-
site-directed mutagenesis, 4.7% activity compared to the wild-type enzyme, in vivo complementation of a deficient yeast strain
D370A
-
site-directed mutagenesis, 8.7% activity compared to the wild-type enzyme, in vivo complementation of a deficient yeast strain
G347R
-
site-directed mutagenesis, catalytically inactive, no in vivo complementation of a deficient yeast strain
I363N
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site-directed mutagenesis, 84% activity compared to the wild-type enzyme, in vivo complementation of a deficient yeast strain
P338I
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site-directed mutagenesis, 74% activity compared to the wild-type enzyme, in vivo complementation of a deficient yeast strain
additional information
additional information
-
a strain carrying the MES1 structure gene on a high copy number plasmid, pFL1
additional information
-
construction of an inactive strain by gene disruption
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged MetRS from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type and mutant His-tagged MetRSs in Escherichia coli strain BL21(DE3)
expression of cytoplasmic and mitochondrial isozymes as GST-fusion proteins in the yeast strain RS453, functional complementation of an inactive gene disruption yeast strain by the mitochondrial isozyme located in the cytoplasm
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Fasiolo,F.; Gibson, B.W.; Walter, P.; Chatton, B.; Biemann, K.; Boulanger, Y.
Cytoplasmic methionyl-tRNA synthetase from bakers' yeast. A monomer with a post-translationally modified N-terminus
J. Biol. Chem.
260
15571-15576
1985
Saccharomyces cerevisiae
Senger, B.; Despons, L.; Walter, P.; Jakubowski, H.; Fasiolo, F.
Yeast cytoplasmic and mitochondrial methionyl-tRNA synthetases: two structural frameworks for identical functions
J. Mol. Biol.
311
205-216
2001
Saccharomyces cerevisiae
Simader, H.; Hothorn, M.; Koehler, C.; Basquin, J.; Simos, G.; Suck, D.
Structural basis of yeast aminoacyl-tRNA synthetase complex formation revealed by crystal structures of two binary sub-complexes
Nucleic Acids Res.
34
3968-3979
2006
Saccharomyces cerevisiae (P00958), Saccharomyces cerevisiae
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