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
Search PMC articles PubMed articles NCBI proteins

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

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1T90.

References

• 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.