Methylmalonyl-CoA decarboxylase
| methylmalonyl-CoA decarboxylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
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Methylmalonyl CoA decarboxylase trimer, E.Coli | |||||||||
| Identifiers | |||||||||
| EC number | 4.1.1.41 | ||||||||
| CAS number | 37289-44-4 | ||||||||
| 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 / EGO | ||||||||
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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.