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Literature summary 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

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.5.1.47 serine acetyltransferase serine acetyltransferase (EC 2.3.1.30) 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

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.30 Haemophilus influenzae
-
-
-
2.5.1.47 Haemophilus influenzae
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.30 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
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.5.1.47 HiOASS
-
 Haemophilus influenzae
2.5.1.47 O-acetylserine sulfhydrylase
-
 Haemophilus influenzae

Cofactor

EC Number Cofactor Comment Organism Structure
2.5.1.47 pyridoxal 5'-phosphate
-
 Haemophilus influenzae