Methylmalonyl-CoA decarboxylase

In enzymology, a methylmalonyl-CoA decarboxylase (EC 4.1.1.41) is an enzyme that catalyzes the chemical reaction

(S)-methylmalonyl-CoA propanoyl-CoA + CO₂

Hence, this enzyme has one substrate, (S)-methylmalonyl-CoA, and two products, propanoyl-CoA and CO₂.

This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is (S)-methylmalonyl-CoA carboxy-lyase (propanoyl-CoA-forming). Other names in common use include propionyl-CoA carboxylase, propionyl coenzyme A carboxylase, methylmalonyl-coenzyme A decarboxylase, (S)-2-methyl-3-oxopropanoyl-CoA carboxy-lyase [incorrect], and (S)-methylmalonyl-CoA carboxy-lyase. This enzyme participates in propanoate metabolism.

Structural studies

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1EF8 and 1EF9.

References

• Galivan JH, Allen SH (1968). "Methylmalonyl coenzyme A decarboxylase. Its role in succinate decarboxylation by Micrococcus lactilyticus". J. Biol. Chem. 243 (6): 1253–61. PMID 5646172. 
• Hilpert W, Dimroth P (1982). "Conversion of the chemical energy of methylmalonyl-CoA decarboxylation into a Na+ gradient". Nature. 296 (5857): 584–5. doi:10.1038/296584a0. PMID 7070502. 
• Hoffmann A, Hilpert W, Dimroth P (1989). "The carboxyltransferase activity of the sodium-ion-translocating methylmalonyl-CoA decarboxylase of Veillonella alcalescens". Eur. J. Biochem. 179 (3): 645–50. doi:10.1111/j.1432-1033.1989.tb14596.x. PMID 2920730.