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Literature summary for 6.1.1.18 extracted from

  • Ludmerer, S.W.; Wright, D.J.; Schimmel, P.
    Purification of glutamine tRNA synthetase from Saccharomyces cerevisiae (1993), J. Biol. Chem., 268, 5519-5523.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information truncated enzyme form lacking the NH2-terminal domain, with modest increase in Km value for glutamine and ATP and no difference in kcat for aminoacylation or Km for tRNA Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0017
-
tRNAGln full-length enzyme and truncated enzyme Saccharomyces cerevisiae
0.028
-
Gln full-length enzyme Saccharomyces cerevisiae
0.038
-
ATP full-length enzyme Saccharomyces cerevisiae
0.11
-
Gln truncated enzyme Saccharomyces cerevisiae
0.26
-
ATP truncated enzyme Saccharomyces cerevisiae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
91000
-
1 * 91000, SDS-PAGE Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
full-length and truncated enzyme form lacking the NH2-terminal domain
-

Purification (Commentary)

Purification (Comment) Organism
-
Saccharomyces cerevisiae

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-glutamine + tRNAGln
-
Saccharomyces cerevisiae AMP + diphosphate + L-glutaminyl-tRNAGln
-
?

Subunits

Subunits Comment Organism
monomer 1 * 91000, SDS-PAGE Saccharomyces cerevisiae

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information
-
Saccharomyces cerevisiae