In enzymology, a methylmalonyl-CoA decarboxylase (EC 7.2.4.3) is an enzyme that catalyzes the chemical reaction
| methylmalonyl-CoA decarboxylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Methylmalonyl CoA decarboxylase trimer, E.Coli | |||||||||
| Identifiers | |||||||||
| EC no. | 7.2.4.3 | ||||||||
| CAS no. | 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 / QuickGO | ||||||||
| |||||||||
- (S)-methylmalonyl-CoA propanoyl-CoA + CO2
Hence, this enzyme has one substrate, (S)-methylmalonyl-CoA, and two products, propanoyl-CoA and CO2. Along with this reaction, this enzyme transports sodium cations across the membrane, creating a gradient which can be used for synthesis of ATP, hence its classification as a translocase.[1]
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 edit
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1EF8 and 1EF9.
References edit
- ^ "ENZYME - 7.2.4.3 (S)-methylmalonyl-CoA decarboxylase (sodium-transporting)". enzyme.expasy.org. Retrieved 2022-11-24.
- 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. Bibcode:1982Natur.296..584H. doi:10.1038/296584a0. PMID 7070502. S2CID 2595001.
- 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.
