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
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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
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results (Engineering
Engineering on EC 6.1.1.10 - methionine-tRNA ligase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
F316S
the mutant exhibits a significantly reduced growth rate compared with the wild type
F501L
the mutant exhibits a significantly reduced growth rate compared with the wild type
L216P
the mutant exhibits a significantly reduced growth rate compared with the wild type
P27S
the mutant exhibits a significantly reduced growth rate compared with the wild type
R424P
the mutant exhibits a significantly reduced growth rate compared with the wild type
D229N
A256X
C477S
the mutant shows at least a 2fold increase in mismethionylation percentage compared to the wild type enzyme
D369A
D369K/K295D
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site-directed mutagenesis in the MetRS SCF, the mutant shows reduced transfer RNA aminoacylation compared to the wild-type enzyme
D369N
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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
F277L
the mutant displays at least a 6fold reduction in mismethionylation percentage compared to the wild type enzyme
G23A
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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
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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
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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
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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
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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
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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
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saturation mutagenesis, the mutant shows altered amino acid substrate binding compared to the wild-type enzyme
K295A
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site-directed mutagenesis in the MetRS SCF, the mutant shows reduced transfer RNA aminoacylation compared to the wild-type enzyme
K295V
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site-directed mutagenesis in the MetRS SCF, the mutant shows reduced transfer RNA aminoacylation compared to the wild-type enzyme
K335Q
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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
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
L13N/Y260L/H301L
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the mutant enzyme enables cells to use the methionine surrogate azidonorleucine in protein synthesis
L13S
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saturation mutagenesis, the mutant shows altered amino acid substrate binding compared to the wild-type enzyme
L13S/Y260L/H301L
MetRS SLL-mutant with modified substrate specificity
L22A
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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
M78L
M88F
P257X
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saturation mutagenesis, the mutant shows altered amino acid substrate binding compared to the wild-type enzyme
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
S209A/S825A
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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
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the mutation mimicks dual phosphorylation and leads to reduced activity compared to the wild type enzyme
T10M
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natural mutant, 5% activity compared to the wild-type, complementation of an enzyme-deficient Escherichia coli strain, no inhibition by L-methionine hydroxamate
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
Y15A
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natural mutant, very low residual activity, complementation of an enzyme-deficient Escherichia coli strain
Y260L
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saturation mutagenesis, the mutant shows altered amino acid substrate binding compared to the wild-type enzyme
Y490A
the mutant shows at least a 2fold increase in mismethionylation percentage compared to the wild type enzyme
Y94H
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natural mutant, unstable, no complementation of an enzyme-deficient Escherichia coli strain
S662D
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the mutation induces a conformational change in methionyl-tRNAsynthetase and significantly reduces its interaction with aminoacyl-tRNA synthetase-interacting multifunctional protein-3. This mutant possesses significantly reduced catalytic activity because of loss of tRNAMet binding, resulting in down-regulation of global translation
A355C
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site-directed mutagenesis, 115% activity compared to the wild-type enzyme, in vivo complementation of a deficient yeast strain
C350A
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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
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site-directed mutagenesis, catalytically inactive, no in vivo complementation of a deficient yeast strain, mutant shows a second zinc-binding knuckle structure
D348G
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site-directed mutagenesis, 4.7% activity compared to the wild-type enzyme, in vivo complementation of a deficient yeast strain
D370A
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site-directed mutagenesis, 8.7% activity compared to the wild-type enzyme, in vivo complementation of a deficient yeast strain
G347R
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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
A256X
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random mutagnesis, the mutant shows altered amino acid substrate binding compared to the wild-type enzyme
A256X
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random mutagenesis, the mutant shows altered amino acid substrate binding compared to the wild-type enzyme
D369A
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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
D369A
the mutant displays at least a 6fold reduction in mismethionylation percentage compared to the wild type enzyme
M218A
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random mutagnesis, the mutant shows altered amino acid substrate binding compared to the wild-type enzyme
M218A
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random mutagenesis, the mutant shows altered amino acid substrate binding compared to the wild-type enzyme
M233I
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random mutagnesis, the mutant shows altered amino acid substrate binding compared to the wild-type enzyme
M233I
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random mutagenesis, the mutant shows altered amino acid substrate binding compared to the wild-type enzyme
M78L
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random mutagnesis, the mutant shows altered amino acid substrate binding compared to the wild-type enzyme
M78L
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random mutagenesis, the mutant shows altered amino acid substrate binding compared to the wild-type enzyme
M88F
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random mutagnesis, the mutant shows altered amino acid substrate binding compared to the wild-type enzyme
M88F
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random mutagenesis, the mutant shows altered amino acid substrate binding compared to the wild-type enzyme
additional information
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gene replacement mutagenesis, downregulation of metS1 by its antisense construct, xylose-induced antisense expression, antisense orientation is identified for the metS1 allele, while no such orientation bias is seen for the metS2 allele, attenuation of MetS1 enzyme expression hypersensitizes Bacillus anthracis cells to a MetS-specific antimicrobial compound Rx-000019, but not to other antibiotics that affect cell wall assembly, fatty acid biosynthesis, protein translation, or DNA replication, overview
additional information
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construction of truncated mutants lacking the tRNA-binding domain, deletion of the C-terminal tRBD of MetRS-Ce results in a 10fold increase in the kcat of Met-tRNAMet formation and a 15fold increase in KM for tRNAMe compared to the wild-type enzyme
additional information
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construction of C-terminal truncated mutant, removal of beta10 strand and insertion of a stop codon at position 666, M665
additional information
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high-throughput screening for mutant enzymes that enable residue-specific incorporation of noncanonical amino acids into the recombinant mutant enzymes in the bacterial cells, overview
additional information
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replacement of amino acids of the MetRS SCF with portions of the structurally similar glutaminyl-tRNA synthetase, EC6.1.1.18, motif or with alanine residues. Chimeric variants retain significant tRNA methionylation activity, indicating that structural integrity of the helix-turn-strand-helix motif contributes more to RNA aminoacylation than does amino acid identity. In contrast, chimeras are significantly reduced in methionyl adenylate synthesis, suggesting a role for the SCF in formation of a structured active site domain
additional information
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construction of a truncated enzyme form with 25% reduced activity compared to the wild-type enzyme
additional information
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a strain carrying the MES1 structure gene on a high copy number plasmid, pFL1
additional information
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construction of an inactive strain by gene disruption
