Literature summary for 2.3.1.30 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.

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Inhibitors

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

Organism

Organism	UniProt	Comment	Textmining
Haemophilus influenzae	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
acetyl-CoA + L-serine	L-serine acetylation is an equilibrium ordered mechanism	Haemophilus influenzae	CoA + O-acetyl-L-serine	-	r

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Release 2023.1 (January 2023)