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Literature summary for 6.1.1.12 extracted from

  • Gangloff, J; Dirheimer, G.
    Studies on aspartyl-tRNA synthetase from baker's yeast. I. Purification and properties of the enzyme (1973), Biochim. Biophys. Acta, 294, 263-272.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00027
-
tRNAAsp
-
Saccharomyces cerevisiae
0.023
-
ATP
-
Saccharomyces cerevisiae
2.2
-
Asp
-
Saccharomyces cerevisiae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
83000 100000 sucrose density gradient centrifugation Saccharomyces cerevisiae
260000
-
gel filtration Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-
Saccharomyces cerevisiae C836
-
-
-

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-aspartate + tRNAAsp
-
Saccharomyces cerevisiae AMP + diphosphate + L-aspartyl-tRNAAsp
-
?
ATP + L-aspartate + tRNAAsp
-
Saccharomyces cerevisiae C836 AMP + diphosphate + L-aspartyl-tRNAAsp
-
?

Subunits

Subunits Comment Organism
monomer 1 * 106000-114000, SDS-PAGE Saccharomyces cerevisiae

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
16.9
-
aspartyl-tRNA
-
Saccharomyces cerevisiae