Malonate-semialdehyde dehydrogenase (acetylating)

Last updated
malonate-semialdehyde dehydrogenase (acetylating)
Identifiers
EC no. 1.2.1.18
CAS no. 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 / QuickGO
Search
PMC articles
PubMed articles
NCBI proteins

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

+ CoA + NAD+
 
 
 
CO2 + H+
Malonate-semialdehyde dehydrogenase (acetylating)
 
CO2 + H+
 
+ NADH
 

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