Literature summary for 6.1.1.10 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.

Search for more literature for 6.1.1.10

Protein Variants

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

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	-	Geobacillus stearothermophilus

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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

Organism

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

Reaction

Reaction	Comment	Organism	Reaction ID
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	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + L-methionine + tRNAMet	-	Geobacillus stearothermophilus	AMP + diphosphate + L-methionyl-tRNAMet	-	?
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	-	?
additional information	enzyme also performs the ATP-diphosphate exchange reaction	Geobacillus stearothermophilus	?	-	?

Subunits

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

Synonyms

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

Temperature Optimum [°C]

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

Temperature Stability [°C]

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

pH Optimum

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

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Geobacillus stearothermophilus

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Release 2023.1 (January 2023)