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Literature summary extracted from

  • Hountondji, C.; Beauvallet, C.; Pernollet, J.C.; Blanquet, S.
    Enzyme-induced covalent modification of methionyl-tRNA synthetase from Bacillus stearothermophilus by methionyl-adenylate: identification of the labeled amino acid residues by matrix-assisted laser desorption-ionization mass spectrometry (2000), J. Protein Chem., 19, 563-568.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
6.1.1.10 additional information construction of a truncated enzyme form with 25% reduced activity compared to the wild-type enzyme Geobacillus stearothermophilus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.1.1.10 Mg2+
-
Geobacillus stearothermophilus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
6.1.1.10 62000
-
recombinant truncated mutant, mass spectrometry Geobacillus stearothermophilus
6.1.1.10 149000
-
recombinant wild-type enzyme, mass spectrometry Geobacillus stearothermophilus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.1.1.10 ATP + L-methionine + tRNAMet Geobacillus stearothermophilus
-
AMP + diphosphate + L-methionyl-tRNAMet
-
?

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.10 Geobacillus stearothermophilus
-
MS534, purified recombinant dimeric wild-type and monomeric truncated mutant enzymes expressed in Escherichia coli
-

Reaction

EC Number Reaction Comment Organism Reaction ID
6.1.1.10 ATP + L-methionine + tRNAMet = AMP + diphosphate + L-methionyl-tRNAMet reaction mechanism, Lys261, Lys295, and Lys301 are located in the catalytic crevice of the enzyme Geobacillus stearothermophilus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.10 ATP + L-methionine + tRNAMet
-
Geobacillus stearothermophilus AMP + diphosphate + L-methionyl-tRNAMet
-
?
6.1.1.10 ATP + L-methionine + tRNAMet two-step reaction mechanism, enzyme forms the reaction intermediate L-methionyl-adenylate, which covalently methionylates the enzyme at the epsilon-amino group of a lysine residue, inducing structural modifcation, 4.3 and 2.2 mol of Met are incorporated by 1 mol of wild-type enzyme and truncated mutant enzyme, respectively Geobacillus stearothermophilus AMP + diphosphate + L-methionyl-tRNAMet
-
?
6.1.1.10 additional information enzyme also performs the ATP-diphosphate exchange reaction Geobacillus stearothermophilus ?
-
?

Subunits

EC Number Subunits Comment Organism
6.1.1.10 dimer recombinant wild-type, mass spectrometry Geobacillus stearothermophilus
6.1.1.10 monomer 1 * 62000, recombinant truncated mutant enzyme, mass spectrometry Geobacillus stearothermophilus

Synonyms

EC Number Synonyms Comment Organism
6.1.1.10 Methionine translase
-
Geobacillus stearothermophilus
6.1.1.10 Methionine--tRNA ligase
-
Geobacillus stearothermophilus
6.1.1.10 Methionyl tRNA synthetase
-
Geobacillus stearothermophilus
6.1.1.10 Methionyl-transfer ribonucleate synthetase
-
Geobacillus stearothermophilus
6.1.1.10 Methionyl-transfer ribonucleic acid synthetase
-
Geobacillus stearothermophilus
6.1.1.10 Methionyl-transfer RNA synthetase
-
Geobacillus stearothermophilus
6.1.1.10 MetRS
-
Geobacillus stearothermophilus
6.1.1.10 Synthetase, methionyl-transfer ribonucleate
-
Geobacillus stearothermophilus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.1.1.10 37
-
assay at Geobacillus stearothermophilus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
6.1.1.10 additional information
-
thermostable enzyme Geobacillus stearothermophilus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.1.1.10 8
-
assay at Geobacillus stearothermophilus

Cofactor

EC Number Cofactor Comment Organism Structure
6.1.1.10 ATP
-
Geobacillus stearothermophilus