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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. 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.