Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 6.1.1.12 extracted from

  • Lorber, B.; Mejdoub, H.; Reinbolt, J.; Boulanger, Y.; Giege, R.
    Properties of N-terminal truncated yeast aspartyl synthetase and structural characteristics of the cleaved domain (1988), Eur. J. Biochem., 174, 155-161.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information truncated form that has lost the first 50-64 residues, with full retention of both the activity and the dimeric structure Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
native form and truncated form that has lost the first 50-64 residues
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-aspartate + tRNAAsp
-
Saccharomyces cerevisiae AMP + diphosphate + L-aspartyl-tRNAAsp
-
?