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Literature summary for 6.1.1.10 extracted from

  • 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 (2001), J. Mol. Biol., 306, 863-876.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-methionine + tRNAMet Escherichia coli
-
AMP + diphosphate + L-methionyl-tRNAMet
-
?
additional information Escherichia coli L-homocysteine is a natural competitor to L-methionine, its activation by the enzyme is prevented by a proof-reading mechanism, structural requirements are determined form the crystal structure ?
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Reaction

Reaction Comment Organism Reaction ID
ATP + L-methionine + tRNAMet = AMP + diphosphate + L-methionyl-tRNAMet substrate recognition, editing, binding and reaction mechanism Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-methionine + tRNAMet
-
Escherichia coli AMP + diphosphate + L-methionyl-tRNAMet
-
?
ATP + L-methionine + tRNAMet substrate editing mechanism, L-methionine is bound to a hydrophobic pocket formed by amino acid residues W253, Y15, A256, P257, L13, A12, I297, Y260, H301, and W305 around the side-chain Escherichia coli AMP + diphosphate + L-methionyl-tRNAMet
-
?
additional information L-homocysteine is a natural competitor to L-methionine, its activation by the enzyme is prevented by a proof-reading mechanism, structural requirements are determined form the crystal structure Escherichia coli ?
-
?

Synonyms

Synonyms Comment Organism
Methionine translase
-
Escherichia coli
Methionine--tRNA ligase
-
Escherichia coli
Methionyl tRNA synthetase
-
Escherichia coli
Methionyl-transfer ribonucleate synthetase
-
Escherichia coli
Methionyl-transfer ribonucleic acid synthetase
-
Escherichia coli
Methionyl-transfer RNA synthetase
-
Escherichia coli
MetRS
-
Escherichia coli
Synthetase, methionyl-transfer ribonucleate
-
Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP
-
Escherichia coli