Malonate-semialdehyde dehydrogenase (acetylating)
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)+ 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.
|
---|
| Activity | |
---|
| Regulation | |
---|
| Classification | |
---|
| Types | |
---|
|