Methylmalonate-semialdehyde dehydrogenase (acylating)
From Wikipedia, the free encyclopedia
In enzymology, a methylmalonate-semialdehyde dehydrogenase (acylating) (EC 1.2.1.27) is an enzyme that catalyzes the chemical reaction
- 2-methyl-3-oxopropanoate + CoA + H2O + NAD+ propanoyl-CoA + HCO3- + NADH
The 4 substrates of this enzyme are 2-methyl-3-oxopropanoate, CoA, H2O, and NAD+, whereas its 3 products are propanoyl-CoA, HCO3-, and NADH.
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 2-methyl-3-oxopropanoate:NAD+ 3-oxidoreductase (CoA-propanoylating). Other names in common use include MSDH, and MMSA dehydrogenase. This enzyme participates in 3 metabolic pathways: inositol metabolism, valine, leucine and isoleucine degradation, and propanoate metabolism.
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[edit] Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1T90.
[edit] References
- IUBMB entry for 1.2.1.27
- BRENDA references for 1.2.1.27 (Recommended.)
- PubMed references for 1.2.1.27
- PubMed Central references for 1.2.1.27
- Google Scholar references for 1.2.1.27
- Sokatch JR, Sanders LE, Marshall VP (1968). "Oxidation of methylmalonate semialdehyde to propionyl coenzyme A in Pseudomonas aeruginosa grown on valine". J. Biol. Chem. 243: 2500–6. PMID 4297649.
- Rahuel-Clermont S, Branlant G, Aubry A (2004). "Expression, purification, crystallization and preliminary X-ray diffraction data of methylmalonate-semialdehyde dehydrogenase from Bacillus subtilis". Acta. Crystallogr. D. Biol. Crystallogr. 60: 1435–7. doi: . PMID 15272169.
- Stines-Chaumeil C, Talfournier F, Branlant G (2006). "Mechanistic characterization of the MSDH (methylmalonate semialdehyde dehydrogenase) from Bacillus subtilis". Biochem. J. 395: 107–15. doi: . PMID 16332250.
[edit] External links
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- The CAS registry number for this enzyme class is 37205-49-5.