Biology:Malonate-semialdehyde dehydrogenase (acetylating)

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malonate-semialdehyde dehydrogenase (acetylating)
Identifiers
EC number1.2.1.18
CAS number9028-97-1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

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)+ [math]\displaystyle{ \rightleftharpoons }[/math] 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

  • "Enzymatic studies on the metabolism of beta-alanine". The Journal of Biological Chemistry 236: 781–90. March 1961. PMID 13712439. 
  • "Aldehyde oxidation. V. Direct conversion of malonic semialdehyde to acetyl-coenzyme A". The Journal of Biological Chemistry 235: 589–94. March 1960. PMID 13846369. 
  • "Aldehyde dehydrogenase". The Enzymes. 7 (2nd ed.). New York: Academic Press. 1963. pp. 203–221.