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Literature summary for 6.1.1.17 extracted from

  • Proulx, M.; Duplain, L.; Lacoste, L.; Yaguchi, M.; Lapointe, J.
    The monomeric glutamyl-tRNA synthetase from Bacillus subtilis 168 and its regulatory factor. Their purification, characterization, and the study of their interaction (1983), J. Biol. Chem., 258, 753-759.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
gamma-Globulin
-
Bacillus subtilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information
-
Bacillus subtilis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
65500
-
1 * 65500, enzyme copurifies with a 46000 MW polypeptide which increases the affinity for glutamate and ATP, and stabilizes it against heat inactivation, SDS-PAGE Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
Trp-
-
Bacillus subtilis 168
-
Trp-
-

Purification (Commentary)

Purification (Comment) Organism
-
Bacillus subtilis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-glutamate + tRNAGlu
-
Bacillus subtilis AMP + diphosphate + L-glutamyl-tRNAGlu
-
?
ATP + L-glutamate + tRNAGlu
-
Bacillus subtilis 168 AMP + diphosphate + L-glutamyl-tRNAGlu
-
?

Subunits

Subunits Comment Organism
monomer 1 * 65500, enzyme copurifies with a 46000 MW polypeptide which increases the affinity for glutamate and ATP, and stabilizes it against heat inactivation, SDS-PAGE Bacillus subtilis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
46000 MW polypeptide stabilizes the enzyme against heat inactivation Bacillus subtilis