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Malonate-semialdehyde dehydrogenase (acetylating)

From Wikipedia, the free encyclopedia

In enzymology, a malonate-semialdehyde dehydrogenase (acetylating) (EC 1.2.1.18) is an enzyme that catalyzes the chemical reaction

3-oxopropanoate + CoA + NAD(P)+ acetyl-CoA + CO2 + NAD(P)H

The 4 substrates of this enzyme are 3-oxopropanoate, CoA, NAD+, and NADP+, whereas its 4 products are acetyl-CoA, CO2, NADH, and NADPH.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3-oxopropanoate:NAD(P)+ oxidoreductase (decarboxylating, CoA-acetylating). This enzyme is also called malonic semialdehyde oxidative decarboxylase. This enzyme participates in 4 metabolic pathways: inositol metabolism, alanine and aspartate metabolism, beta-alanine metabolism, and propanoate metabolism.

References

Further reading

  • Hayaishi O, Nishizuka Y, Tatibana M, Takeshita M, Kuno S (March 1961). "Enzymatic studies on the metabolism of beta-alanine". The Journal of Biological Chemistry. 236: 781–90. PMID 13712439.
  • Yamada EW, Jakoby WB (March 1960). "Aldehyde oxidation. V. Direct conversion of malonic semialdehyde to acetyl-coenzyme A". The Journal of Biological Chemistry. 235: 589–94. PMID 13846369.
  • Jakoby WB (1963). "Aldehyde dehydrogenase". In Boyer PD, Lardy H, Myrback K (eds.). The Enzymes. Vol. 7 (2nd ed.). New York: Academic Press. pp. 203–221.


This page was last edited on 26 August 2023, at 14:51
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