Di-trans,poly-cis-decaprenylcistransferase
Class of enzymes
From Wikipedia, the free encyclopedia
In enzymology, a di-trans,poly-cis-decaprenylcistransferase (EC 2.5.1.31) is an enzyme that catalyzes the chemical reaction
- di-trans,poly-cis-decaprenyl diphosphate + isopentenyl diphosphate diphosphate + di-trans,poly-cis-undecaprenyl diphosphate
| di-trans,poly-cis-decaprenylcistransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.5.1.31 | ||||||||
| CAS no. | 52350-87-5 | ||||||||
| 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 | ||||||||
| |||||||||
Thus, the two substrates of this enzyme are di-trans,poly-cis-decaprenyl diphosphate and isopentenyl diphosphate, whereas its two products are diphosphate and di-trans,poly-cis-undecaprenyl diphosphate.
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is di-trans,poly-cis-decaprenyl-diphosphate:isopentenyl-diphosphate undecaprenylcistransferase. Other names in common use include di-trans,poly-cis-undecaprenyl-diphosphate synthase, undecaprenyl-diphosphate synthase, bactoprenyl-diphosphate synthase, UPP synthetase, undecaprenyl diphosphate synthetase, and undecaprenyl pyrophosphate synthetase. This enzyme participates in terpenoid biosynthesis.
Structural studies
References
- Muth JD, Allen CM (1984). "Undecaprenyl pyrophosphate synthetase from Lactobacillus plantarum: a dimeric protein". Arch. Biochem. Biophys. 230 (1): 49â60. doi:10.1016/0003-9861(84)90085-7. PMID 6712246.
- Takahashi I, Ogura K (November 1982). "Prenyltransferases of Bacillus subtilis: undecaprenyl pyrophosphate synthetase and geranylgeranyl pyrophosphate synthetase". J. Biochem. 92 (5). Tokyo: 1527â37. doi:10.1093/oxfordjournals.jbchem.a134077. PMID 6818223.
 | This EC 2.5 enzyme-related article is a stub. You can help Wikipedia by adding missing information. |