Reactome | COQ7:COQ9 octamer hydroxylates DMQ10H2

COQ7:COQ9 octamer hydroxylates DMQ10H2

Stable Identifier

R-HSA-2162194

Type

Reaction [transition]

Species

Homo sapiens

Compartment

mitochondrial inner membrane, mitochondrial matrix

Synonyms

DMQ10H2 is hydroxylated to DeMQ10H2 by COQ7

ReviewStatus

5/5

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5-Demethoxyubiquinone hydroxylase COQ7 catalyzes the hydroxylation of 6-methoxy-3-methyl-2-decaprenyl-1,4-benzoquinol (DMQ10H2, DMQ) to 3-demethylubiquinol-10 (DeMQ10H2, DeMQ), using NADH and oxygen. COQ7 forms a heterooctameric complex with ubiquinone biosynthesis protein COQ9, a lipid-binding protein presenting the substrate to COQ7 activity. In this complex, COQ7 binds two iron ions and forms a heterodimer with COQ9, with four of these dimers forming an octameric cage (Vajo et al., 1999; Lohman et al., 2014; Manicki et al., 2022). This reaction was first studied in yeast (Marbois & Clarke, 1996; Tran et al., 2006). Both COQ8A and COQ8B bind to COQ7, presumably during formation of a hypothetical multienzyme COQ complex. COQ8A,B are required for the assembly of the complex but may not be stably incorporated into it, so only the components identified by Floyd et al. are annotated (Ashraf et al., 2013; Floyd et al., 2016; reviewed in Hojabri et al., 2023; Liang et al., 2023).

Literature References

PubMed ID	Title	Journal	Year
27499296	Mitochondrial Protein Interaction Mapping Identifies Regulators of Respiratory Chain Function Stefely, JA, Taylor, RW, Dolan, BK, Westphall, MS, Wilkerson, EM, Veling, MT, Wrobel, RL, Kim, JP, Jochem, A, Cho, H, Coon, JJ, Xia, C, Ulbrich, A, Gromek, KA, Rensvold, JW, Bohl, SL, Beebe, ET, Pagliarini, DJ, Werner, KM, Alston, CL, Floyd, BJ, Prokisch, H, Kremer, LS, Minogue, CE	Mol Cell	2016
36843884	Clinical features and gene variation analysis of COQ8B nephropathy: Report of seven cases Yang, Q, Zhang, Y, Liang, R, Chen, H, Yang, H, Wu, D, Law, CF, Yu, S, Zhang, G, Wang, A, Wang, M, Jiao, J, Chen, X	Front Pediatr	2022
10501970	Conservation of the Caenorhabditis elegans timing gene clk-1 from yeast to human: a gene required for ubiquinone biosynthesis with potential implications for aging Ho, N, Francomano, CA, Jonassen, T, King, LM, Wilkin, DJ, Munnich, A, Vajo, Z, Clarke, CF	Mamm Genome	1999
24270420	ADCK4 mutations promote steroid-resistant nephrotic syndrome through CoQ10 biosynthesis disruption Salviati, L, Washburn, J, Choi, M, Barua, M, Gee, HY, Han, Z, Saleem, MA, Gok, F, Clarke, CF, Vega-Warner, V, Allen, SJ, Evans, J, Esteve-Rudd, J, Lifton, RP, Nitschké, P, El Desoky, S, Bole-Feysot, C, Levy, S, Airik, R, Ashraf, S, Pei, Y, Haberberger, B, Bierzynska, A, Woerner, S, Paterson, AD, Xie, LX, Bockenhauer, D, Antignac, C, Al-Hamed, MH, Hacihamdioglu, DO, Cochat, P, Kleta, R, Lovric, S, Pollak, M, Wiggins, RC, Avila-Casado, C, Cattran, DC, Zhou, W, Williams, DS, Hildebrandt, F, Prokisch, H, Kari, JA, Otto, EA, Song, X, Fang, H	J Clin Invest	2013
36306796	Structure and functionality of a multimeric human COQ7:COQ9 complex Frost, A, Pagliarini, DJ, Guerra, RM, Dal Peraro, M, Aydin, H, Abriata, LA, Manicki, M, Coon, JJ, Overmyer, KA	Mol Cell	2022
16624818	Complementation of Saccharomyces cerevisiae coq7 mutants by mitochondrial targeting of the Escherichia coli UbiF polypeptide: two functions of yeast Coq7 polypeptide in coenzyme Q biosynthesis Marbois, B, Jonassen, T, Gin, P, Gulmezian, M, Tran, UC, Clarke, CF	J Biol Chem	2006
25339443	Mitochondrial COQ9 is a lipid-binding protein that associates with COQ7 to enable coenzyme Q biosynthesis Sukumar, S, Luna-Sánchez, M, Stefely, JA, Tong, L, Everett, JK, Westphall, MS, Xiao, R, Lew, S, Wrobel, RL, Lohman, DC, Jochem, A, Coon, JJ, Ulbrich, A, Stefely, MS, Beebe, ET, Minogue, CE, Pagliarini, DJ, Mitchell, JC, Wang, H, López, LC, Seetharaman, J, Forouhar, F	Proc. Natl. Acad. Sci. U.S.A.	2014
37476682	Adolescence Onset Primary Coenzyme Q10 Deficiency With Rare CoQ8A Gene Mutation: A Case Report and Review of Literature Nejad Biglari, H, Irilouzadian, R, Sarmadian, R, Hojabri, M, Gilani, A	Clin Med Insights Case Rep	2023
8621692	The COQ7 gene encodes a protein in Saccharomyces cerevisiae necessary for ubiquinone biosynthesis Marbois, BN, Clarke, CF	J Biol Chem	1996

Participants

Input

Output

Participates

as an event of

Ubiquinol biosynthesis (Homo sapiens)

Catalyst Activity

oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen of COQ3:COQ4:COQ5:COQ6:COQ7:COQ9 [mitochondrial inner membrane]

Physical Entity

COQ3:COQ4:COQ5:COQ6:COQ7:COQ9 [mitochondrial inner membrane] (Homo sapiens)

Activity

oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen (GO:0016709)

This event is regulated

Requirements