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Literature summary 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.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.2.1.11 iodoacetamide at 0.1 mM: 45.4% inactivation in the absence of NADP+, 22% inactivation in the presence of 1 mM NADP+ Saccharomyces cerevisiae
1.2.1.11 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
1.2.1.11 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

EC Number Organism UniProt Comment Textmining
1.2.1.11 Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

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