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

BRENDA support

Literature summary extracted from

  • Johnson, C.M.; Huang, B.; Roderick, S.L.; Cook, P.F.
    Kinetic mechanism of the serine acetyltransferase from Haemophilus influenzae (2004), Arch. Biochem. Biophys., 429, 115-122.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.1.30 glycine competitive versus L-serine, uncompetitive versus acetyl-CoA Haemophilus influenzae
2.3.1.30 L-cysteine dead-end inhibitor, competitive against botn substrates in both reaction directions Haemophilus influenzae
2.3.1.30 L-serine product inhibition is noncompetitive with respect to O-acetyl-L-serine and CoA Haemophilus influenzae
2.3.1.30 O-acetyl-L-serine product inhibition is noncompetitive against acetyl-CoA and uncompetitive against L-serine Haemophilus influenzae
2.3.1.30 S-methyl-L-cysteine competitive versus O-acetyl-L-serine and competitive versus CoA Haemophilus influenzae

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.30 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 L-serine acetylation is an equilibrium ordered mechanism Haemophilus influenzae CoA + O-acetyl-L-serine
-
r