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 | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, methylmalonate-semialdehyde dehydrogenase (acylating) (EC 1.2.1.27) is an enzyme that catalyzes the chemical reaction
The three substrates of this enzyme are methylmalonic acid semialdehyde, coenzyme A (CoA), and oxidised nicotinamide adenine dinucleotide (NAD+). Its products are propionyl-CoA, carbon dioxide, reduced NADH, and a proton.[1][2][3][4]
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 PDB: 1T90.
References
[edit]- ↑ Enzyme 1.2.1.27 at KEGG Pathway Database.
- ↑ 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.
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