Decylcitrate synthase
| decylcitrate synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.3.3.2 | ||||||||
| CAS no. | 9068-72-8 | ||||||||
| 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 | ||||||||
| |||||||||
Decylcitrate synthase (EC 2.3.3.2) is an enzyme that catalyzes the chemical reaction in enzymology.
- lauroyl-CoA + H2O + oxaloacetate (2S,3S)-2-hydroxytridecane-1,2,3-tricarboxylate + CoA
The 3 substrates of this enzyme are , H2O, and oxaloacetate, whereas its two products are and CoA.
This enzyme belongs to the family of transferases, specifically those acyltransferases that convert acyl groups into alkyl groups on transfer. The systematic name of this enzyme class is dodecanoyl-CoA:oxaloacetate C-dodecanoyltransferase (thioester-hydrolysing, 1-carboxyundecyl-forming). Other names in common use include 2-decylcitrate synthase, (2S,3S)-2-hydroxytridecane-1,2,3-tricarboxylate oxaloacetate-lyase, and (CoA-acylating).
References[]
- Mahlen A, Gatenbeck S (1968). "A metabolic variation in Penicillium spiculisporum Lehman. II Purification and some properties of the enzyme synthesizing (--)-decylcitric acid". Acta Chem. Scand. 22 (8): 2617–2623. doi:10.3891/acta.chem.scand.22-2617. PMID 5719165.
- Mahlen A (1971). "Properties of 2-decylcitrate synthase from Penicillium spiculisporum Lehman". Eur. J. Biochem. 22 (1): 104–114. doi:10.1111/j.1432-1033.1971.tb01520.x. PMID 5099208.
Categories:
- EC 2.3.3
- Enzymes of unknown structure
- EC 2.3 stubs