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

BRENDA support

Literature summary for 2.3.1.30 extracted from

  • Campanini, B.; Speroni, F.; Salsi, E.; Cook, P.F.; Roderick, S.L.; Huang, B.; Bettati, S.; Mozzarelli, A.
    Interaction of serine acetyltransferase with O-acetylserine sulfhydrylase active site: evidence from fluorescence spectroscopy (2005), Protein Sci., 14, 2115-2124.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.3.1.30

Organism

Organism UniProt Comment Textmining
Haemophilus influenzae
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + L-serine serine acetyltransferase is a key enzyme in the sulfur assimilation pathway and forms a bienzyme complex with O-acetylserine sulfhydrylase, the last enzyme in the cysteine biosynthetic pathway. Serine acetyltransferase can inhibit O-acetylserine sulfhydrylase catalytic activity with a double mechanism, the competition with O-acetylserine for binding to the enzyme active site and the stabilization of a closed conformation that is less accessible to the natural substrate Haemophilus influenzae CoA + O-acetyl-L-serine
-
 ?