Malonate-semialdehyde dehydrogenase (acetylating)

malonate-semialdehyde dehydrogenase (acetylating)
Identifiers
EC number	1.2.1.18
CAS number	9028-97-1
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / EGO
Search PMC articles PubMed articles NCBI proteins

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)+ $\rightleftharpoons$ 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

• Hayaishi, O; Nishizuka, Y; Tatibana, M; Takeshita, M; Kuno, S (1961). "Enzymatic studies on the metabolism of beta-alanine". The Journal of Biological Chemistry 236: 781–90. PMID 13712439.
• Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, p. 203-221.
• Yamada, E. W.; Jakoby, W. B. (1960). "Aldehyde oxidation. V. Direct conversion of malonic semialdehyde to acetyl-coenzyme A". The Journal of Biological Chemistry 235: 589–594. PMID 13846369.