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Literature summary for 6.1.1.10 extracted from

  • Kim, S.; Jo, Y.J.; Lee, S.H.; Motegi, H.; Shiba, K.; Sassanfar, M.; Martinis, S.A.
    Biochemical and phylogenetic analyses of methionyl-tRNA synthetase isolated from a pathogenic microorganism, Mycobacterium tuberculosis (1998), FEBS Lett., 427, 259-262.
    View publication on PubMed
Search for more literature for 6.1.1.10

Cloned(Commentary)

Cloned (Comment) Organism
DNA sequence determination and analysis, overexpression in Escherichia coli Mycobacterium tuberculosis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0032
-
 tRNAMet substrate from Escherichia coli, 37°C Mycobacterium tuberculosis
1
-
 tRNAMet recombinant C-terminally truncated enzyme, 37°C Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
additional information enzyme lacks Zn2+ binding motif and contains no Zn2+ Mycobacterium tuberculosis

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
-
 ?
ATP + L-methionine + tRNAMet Mycobacterium tuberculosis
-
 AMP + diphosphate + L-methionyl-tRNAMet
-
 ?
additional information Escherichia coli phylogenetic analysis ?
-
 ?
additional information Mycobacterium tuberculosis phylogenetic analysis ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 purified recombinant C-terminally truncated enzyme
-
Mycobacterium tuberculosis
-
 non-typical class I enzyme lacking the Zn2+ binding motif and the C-terminal dimerization appendix which is found in enzymes from other organisms
-

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
-
 Mycobacterium tuberculosis AMP + diphosphate + L-methionyl-tRNAMet
-
 ?
ATP + L-methionine + tRNAMet also utilizes tRNAMet from Escherichia coli Mycobacterium tuberculosis AMP + diphosphate + L-methionyl-tRNAMet
-
 ?
additional information phylogenetic analysis Escherichia coli ?
-
 ?
additional information phylogenetic analysis Mycobacterium tuberculosis ?
-
 ?

Synonyms

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

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Escherichia coli
37
-
 assay at Mycobacterium tuberculosis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.83
-
 tRNAMet substrate from Escherichia coli, 37°C Mycobacterium tuberculosis
3 6 tRNAMet substrate from Escherichia coli, 37°C Mycobacterium tuberculosis
6.85
-
 tRNAMet recombinant C-terminally truncated enzyme, 37°C Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Escherichia coli
ATP
-
 Mycobacterium tuberculosis