Malonate-semialdehyde dehydrogenase

Malonate-semialdehyde dehydrogenase
Identifiers
EC no.1.2.1.15
CAS no.9028-94-8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
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PMCarticles
PubMedarticles
NCBIproteins

In enzymology, malonate-semialdehyde dehydrogenase (EC 1.2.1.15) is an enzyme that catalyzes the chemical reaction

+ NAD+
 
 
H2O
H+
H2O
H+
 
 

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

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. This enzyme participates in beta-alanine metabolism.

References

  1. ^ Enzyme 1.2.1.15 at KEGG Pathway Database.
  2. ^ Nakamura K, Bernheim F (June 1961). "Studies on malonic semialdehyde dehydrogenase from Pseudomonas aeruginosa". Biochimica et Biophysica Acta. 50: 147–52. doi:10.1016/0006-3002(61)91071-X. PMID 13727610.