Methylmalonate-semialdehyde dehydrogenase (acylating)
| methylmalonate-semialdehyde dehydrogenase (acylating) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Methylmalonate semialdehyde dehydrogenase tetramer, Bacillus subtilis | |||||||||
| Identifiers | |||||||||
| EC no. | 1.2.1.27 | ||||||||
| CAS no. | 37205-49-5 | ||||||||
| 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 | ||||||||
| |||||||||
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.
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): 2500–6. doi:10.1016/S0021-9258(18)93403-4. 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" (PDF). Acta Crystallogr. D. 60 (Pt 8): 1435–7. 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): 107–15. doi:10.1042/BJ20051525. PMC 1409689. PMID 16332250.
