4-hydroxybenzoate polyprenyltransferase
| 4-hydroxybenzoate polyprenyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.5.1.39 | ||||||||
| CAS no. | 9030-77-7 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a 4-hydroxybenzoate polyprenyltransferase (EC 2.5.1.39) is an enzyme that catalyzes the chemical reaction
- a polyprenyl diphosphate + 4-hydroxybenzoate diphosphate + a 4-hydroxy-3-polyprenylbenzoate
Thus, the two substrates of this enzyme are a polyprenyl diphosphate and 4-hydroxybenzoate, whereas its two products are diphosphate and 4-hydroxy-3-polyprenylbenzoate.
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. This enzyme participates in ubiquinone biosynthesis.[1]
Nomenclature
[edit]The systematic name of this enzyme class is polyprenyl-diphosphate:4-hydroxybenzoate polyprenyltransferase. Other names in common use include:
- nonaprenyl-4-hydroxybenzoate transferase,
- 4-hydroxybenzoate transferase,
- p-hydroxybenzoate dimethylallyltransferase,
- p-hydroxybenzoate polyprenyltransferase,
- p-hydroxybenzoic acid-polyprenyl transferase,
- p-hydroxybenzoic-polyprenyl transferase, and
- 4-hydroxybenzoate nonaprenyltransferase
References
[edit]- ^ Melzer M, Heide L (1994-04-14). "Characterization of polyprenyldiphosphate: 4-hydroxybenzoate polyprenyltransferase from Escherichia coli". Biochim Biophys Acta. 1212 (1): 93–102. doi:10.1016/0005-2760(94)90193-7. PMID 8155731.
- Kalen A, Appelkvist EL, Chojnacki T, Dallner G (1990). "Nonaprenyl-4-hydroxybenzoate transferase, an enzyme involved in ubiquinone biosynthesis, in the endoplasmic reticulum-Golgi system of rat liver". J. Biol. Chem. 265 (2): 1158–64. PMID 2295606.
