| EC |
1.14.15.45 |
| Accepted name: |
4-hydroxy-3-polyprenylbenzoate 5-hydroxylase |
| Reaction: |
4-hydroxy-3-all-trans-polyprenylbenzoate + 2 reduced [2Fe-2S]-[ferredoxin] + O2 + 2 H+ = 3,4-dihydroxy-5-all-trans-polyprenylbenzoate + 2 oxidized [2Fe-2S]-[ferredoxin] + H2O |
| Other name(s): |
COQ6 (ambiguous) |
| Systematic name: |
4-hydroxy-3-all-trans-polyprenylbenzoate,ferredoxin:oxygen oxidoreductase (5-hydroxylating) |
| Comments: |
The enzyme, found in eukaryotes, is involved in the biosynthesis of ubiquinone. The vertebrate enzyme catalyses two hydroxylations in the pathway at the positions meta to the prenyl side chain (the other hydroxylation is classified as EC 1.14.15.46, 2-methoxy-6-polyprenylphenol 4-hydroxylase). The number of isoprenoid subunits in the side chain varies in different species. The enzyme does not have any specificity concerning the length of the polyprenyl tail, and accepts tails of various lengths with similar efficiency. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Nicoll, C.R., Alvigini, L., Gottinger, A., Cecchini, D., Mannucci, B., Corana, F., Mascotti, M.L. and Mattevi, A. In vitro construction of the COQ metabolon unveils the molecular determinants of coenzyme Q biosynthesis. Nat. Catal. 7 (2024) 148–160. [DOI] [PMID: 38425362] |
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| [EC 1.14.15.45 created 2024] |
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