Methylmalonyl-CoA decarboxylase

From Wikipedia, the free encyclopedia

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

(S)-methylmalonyl-CoA $\rightleftharpoons$ 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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

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

[edit] References

IUBMB entry for 4.1.1.41
BRENDA references for 4.1.1.41 (Recommended.)
PubMed references for 4.1.1.41
PubMed Central references for 4.1.1.41
Google Scholar references for 4.1.1.41
Galivan JH, Allen SH (1968). "Methylmalonyl coenzyme A decarboxylase. Its role in succinate decarboxylation by Micrococcus lactilyticus". J. Biol. Chem. 243: 1253–61. PMID 5646172.
Hilpert W, Dimroth P (1982). "Conversion of the chemical energy of methylmalonyl-CoA decarboxylation into a Na+ gradient". Nature. 296: 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: 645–50. doi:10.1111/j.1432-1033.1989.tb14596.x. PMID 2920730.