enzymology, a methylmalonate-semialdehyde dehydrogenase (acylating) ( EC 22.214.171.124) is an enzyme that catalyzes the chemical reaction
2-methyl-3-oxopropanoate + CoA + H 2O + NAD + ⇌ propanoyl-CoA + HCO 3- + NADH
substrates of this enzyme are 2-methyl-3-oxopropanoate, CoA, H, and 2O 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.
Structural studies [ edit ]
As of late 2007, only one
structure has been solved for this class of enzymes, with the PDB accession code 1T90.
References [ edit ]
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 (10): 2500&ndash, 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 60 (Pt 8): 1435&ndash, 7. doi: 10.1107/S0907444904012533. PMID 15272169. Stines-Chaumeil C, Talfournier F, Branlant G (2006). "Mechanistic characterization of the MSDH (methylmalonate semialdehyde dehydrogenase) from Bacillus subtilis". Biochem. J. 395 (1): 107&ndash, 15. doi: 10.1042/BJ20051525. PMC . 1409689 PMID 16332250.