Literature summary for 1.2.1.11 extracted from

Holland, M.J.; Westhead, E.W.
Chemical reactivity at the catalytic sites of aspartic -semialdehyde dehydrogenase and glyceraldehyde-3-phosphate dehydrogenase (1973), Biochemistry, 12, 2276-2281.

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Inhibitors

Inhibitors	Comment	Organism	Structure
iodoacetamide	at 0.1 mM: 45.4% inactivation in the absence of NADP+, 22% inactivation in the presence of 1 mM NADP+	Saccharomyces cerevisiae
iodoacetate	at 1 mM: completely inhibits in the absence or presence of NADP+, at 0.1 mM: 3% inactivation in the absence of NADP+, 50% inactivation in the presence of 1 mM NADP+	Saccharomyces cerevisiae
N-ethylmaleimide	only 1 mol per subunit causes complete inactivation, at 0.1 mM: 91% inactivation in the absence of NADP+, 12% inactivation in the presence of 1 mM NADP+	Saccharomyces cerevisiae

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-aspartate 4-semialdehyde + phosphate + NADP+	-	Saccharomyces cerevisiae	L-4-aspartyl phosphate + NADPH	-	?

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Release 2023.1 (January 2023)