Carnitine O-octanoyltransferase
| carnitine O-octanoyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.3.1.137 | ||||||||
| CAS number | 39369-19-2 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a carnitine O-octanoyltransferase (EC 2.3.1.137) is an enzyme that catalyzes the chemical reaction
- octanoyl-CoA + L-carnitine
CoA + L-octanoylcarnitine
Thus, the two substrates of this enzyme are octanoyl-CoA and L-carnitine, whereas its two products are CoA and L-octanoylcarnitine.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is octanoyl-CoA:L-carnitine O-octanoyltransferase. Other names in common use include medium-chain/long-chain carnitine acyltransferase, carnitine medium-chain acyltransferase, easily solubilized mitochondrial carnitine palmitoyltransferase, and overt mitochondrial carnitine palmitoyltransferase.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1XL7, 1XL8, 1XMC, and 1XMD.
References
- Farrell SO, Fiol CJ, Reddy JK, Bieber LL (1984). "Properties of purified carnitine acyltransferases of mouse liver peroxisomes". J. Biol. Chem. 259 (21): 13089–95. PMID 6436243.
- Healy MJ, Kerner J, Bieber LL (1988). "Enzymes of carnitine acylation. Is overt carnitine palmitoyltransferase of liver peroxisomal carnitine octanoyltransferase?". Biochem. J. 249 (1): 231–7. PMC 1148689. PMID 3342008.
- Miyazawa S, Ozasa H, Osumi T, Hashimoto T (Tokyo). "Purification and properties of carnitine octanoyltransferase and carnitine palmitoyltransferase from rat liver". J. Biochem. (2): 529–42. PMID 6630173.