The Enzyme Database

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EC 1.14.13.253     
Accepted name: 3-demethoxyubiquinone 3-hydroxylase (NADH)
Reaction: 5-methoxy-2-methyl-3-(all-trans-polyprenyl)benzoquinone + NADH + O2 = 3-demethylubiquinone-n + NAD+ + H2O
Other name(s): COQ7
Systematic name: 5-methoxy-2-methyl-3-(all-trans-polyprenyl)benzoquinone,NADH:oxygen oxidoreductase (5-hydroxylating)
Comments: The enzyme, found in eukaryotes, is involved in the biosynthesis of ubiquinone. The vertebrate enzyme has no activity with 5-methoxy-2-methyl-3-(all-trans-polyprenyl)benzene-1,4-diol (cf. EC 1.14.99.60, 3-demethoxyubiquinol 3-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.  Lu, T.T., Lee, S.J., Apfel, U.P. and Lippard, S.J. Aging-associated enzyme human clock-1: substrate-mediated reduction of the diiron center for 5-demethoxyubiquinone hydroxylation. Biochemistry 52 (2013) 2236–2244. [DOI] [PMID: 23445365]
2.  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]
[EC 1.14.13.253 created 2024]
 
 


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