Malonate-semialdehyde dehydrogenase (acetylating)

malonate-semialdehyde dehydrogenase (acetylating)
Identifiers
EC no.1.2.1.18
CAS no.9028-97-1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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In enzymology, malonate-semialdehyde dehydrogenase (acetylating) (EC 1.2.1.18) is an enzyme that catalyzes the chemical reaction

+ CoA + NAD+
 
 
 
CO2 + H+
 
CO2 + H+
 
 

The three substrates of this enzyme are 3-oxopropanoic acid, coenzyme A (CoA), and oxidised nicotinamide adenine dinucleotide (NAD+). Its products are acetyl-CoA, carbon dioxide, reduced NADH, and a proton. This enzyme can use the alternative cofactor, nicotinamide adenine dinucleotide phosphate.[1][2][3]

The 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

  1. ^ Enzyme 1.2.1.18 at KEGG Pathway Database.
  2. ^ 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 (3): 781–90. doi:10.1016/S0021-9258(18)64309-1. PMID 13712439.
  3. ^ Yamada EW, Jakoby WB (March 1960). "Aldehyde oxidation. V. Direct conversion of malonic semialdehyde to acetyl-coenzyme A". The Journal of Biological Chemistry. 235 (3): 589–94. doi:10.1016/S0021-9258(19)67910-X. PMID 13846369.

Further reading

  • 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.