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S-adenosyl-L-methionine + 2-(all-trans-decaprenyl)-5-hydroxy-6-methoxy-3-methylcyclohexa-2,5-diene-1,4-dione
S-adenosyl-L-homocysteine + 2-(all-trans-decaprenyl)-5,6-dimethoxy-3-methylcyclohexa-2,5-diene-1,4-dione
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S-adenosyl-L-methionine + 3-((2E,6E)-farnesyl)benzene-1,2-diol
S-adenosyl-L-homocysteine + 2-methoxy-6-((2E,6E)-farnesyl)phenol
S-adenosyl-L-methionine + 3-((2E,6E)-farnesyl)benzene-1,2-diol
S-adenosyl-L-homocysteine + 2-methoxy-6-(farnesyl)phenol
i.e. 3-[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]benzene-1,2-diol. The substrate is an artificial farnesylated analog of the Escherichia coli substrate 2-octaprenyl-6-hydroxyphenol, an intermediate in the biosynthesis of ubiquinone-8 in Escherichia coli
i.e. 2-methoxy-6-((2E,6E)-3,7,11-trimethyldodeca-2,6,10-trienyl)phenol
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?
S-adenosyl-L-methionine + 3-(all-trans-decaprenyl)-benzene-1,2-diol
S-adenosyl-L-homocysteine + 3-(all-trans-decaprenyl)-1-methoxybenzene-2-ol
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-
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?
S-adenosyl-L-methionine + 3-(all-trans-octaprenyl)benzene-1,2-diol
S-adenosyl-L-homocysteine + 2-methoxy-6-(all-trans-octaprenyl)phenol
S-adenosyl-L-methionine + 3-(all-trans-polyprenyl)benzene-1,2-diol
S-adenosyl-L-homocysteine + 2-methoxy-6-(all-trans-polyprenyl)phenol
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-
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?
additional information
?
-
S-adenosyl-L-methionine + 3-((2E,6E)-farnesyl)benzene-1,2-diol
S-adenosyl-L-homocysteine + 2-methoxy-6-((2E,6E)-farnesyl)phenol
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i.e. 3-[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]benzene-1,2-diol
i.e. 2-methoxy-6-((2E,6E)-3,7,11-trimethyldodeca-2,6,10-trienyl)phenol
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?
S-adenosyl-L-methionine + 3-((2E,6E)-farnesyl)benzene-1,2-diol
S-adenosyl-L-homocysteine + 2-methoxy-6-((2E,6E)-farnesyl)phenol
i.e. 3-[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]benzene-1,2-diol. The substrate is an artificial farnesylated analog of the Escherichia coli substrate 2-all-trans-octaprenyl-6-hydroxyphenol, an intermediate in the biosynthesis of ubiquinone-8 in Escherichia coli
i.e. 2-methoxy-6-((2E,6E)-3,7,11-trimethyldodeca-2,6,10-trienyl)phenol
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?
S-adenosyl-L-methionine + 3-((2E,6E)-farnesyl)benzene-1,2-diol
S-adenosyl-L-homocysteine + 2-methoxy-6-((2E,6E)-farnesyl)phenol
i.e. 3-[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]benzene-1,2-diol. The substrate is an artificial farnesylated analog of the Escherichia coli substrate 2-octaprenyl-6-hydroxyphenol, an intermediate in the biosynthesis of ubiquinone-8 in Escherichia coli
i.e. 2-methoxy-6-((2E,6E)-3,7,11-trimethyldodeca-2,6,10-trienyl)phenol
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?
S-adenosyl-L-methionine + 3-(all-trans-octaprenyl)benzene-1,2-diol
S-adenosyl-L-homocysteine + 2-methoxy-6-(all-trans-octaprenyl)phenol
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?
S-adenosyl-L-methionine + 3-(all-trans-octaprenyl)benzene-1,2-diol
S-adenosyl-L-homocysteine + 2-methoxy-6-(all-trans-octaprenyl)phenol
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the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-8 in Escherichia coli, 1. the methylation of 3-(all-trans-octaprenyl)benzene-1,2-diol and 2. the methylation of 3-demethylubiquinol-8 (this reaction is classified as EC 2.1.1.64)
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additional information
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the enzyme is involved in biosynthesis of ubiquinone-10 in human and catalyzes the methylation of 3-demethylubiquinol-10 to ubiquinol-10 (EC 2.1.1.64) and the methylation of 3,4-dihydroxy-5-decaprenylbenzoate to 3-methoxy-4-hydroxy-5-all-trans-decaprenylbenzoate (EC 2.1.1.114)
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additional information
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wide substrate specificity. The enzyme methylates both eukaryotic substrates demethylubiquinol-3 (this activity is classified as EC 2.1.1.64) and 3,4-dihydroxy-5-farnesylbenzoic acid (this activity is classified as EC 2.1.1.114) and the distinct prokaryotic substrate 3-((2E,6E)-farnesyl)benzene-1,2-diol
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?
additional information
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the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-9 in Rattus norvegicus, 1. the methylation of 3,4-dihydroxy-5-nonaprenylbenzoate (this reaction is classified as EC 2.1.1.114) and 2. the methylation of 3-demethylubiquinol-9 (this reaction is classified as EC 2.1.1.64)
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additional information
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the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-6 in Saccharomyces cerevisiae, 1. the methylation of 3,4-dihydroxy-5-hexaprenylbenzoate (this reaction is classified as EC 2.1.1.114) and 2. the methylation of 3-demethylubiquinol-6 (this reaction is classified as EC 2.1.1.64)
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S-adenosyl-L-methionine + 3-(all-trans-octaprenyl)benzene-1,2-diol
S-adenosyl-L-homocysteine + 2-methoxy-6-(all-trans-octaprenyl)phenol
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the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-8 in Escherichia coli, 1. the methylation of 3-(all-trans-octaprenyl)benzene-1,2-diol and 2. the methylation of 3-demethylubiquinol-8 (this reaction is classified as EC 2.1.1.64)
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?
additional information
?
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additional information
?
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the enzyme is involved in biosynthesis of ubiquinone-10 in human and catalyzes the methylation of 3-demethylubiquinol-10 to ubiquinol-10 (EC 2.1.1.64) and the methylation of 3,4-dihydroxy-5-decaprenylbenzoate to 3-methoxy-4-hydroxy-5-all-trans-decaprenylbenzoate (EC 2.1.1.114)
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?
additional information
?
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the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-9 in Rattus norvegicus, 1. the methylation of 3,4-dihydroxy-5-nonaprenylbenzoate (this reaction is classified as EC 2.1.1.114) and 2. the methylation of 3-demethylubiquinol-9 (this reaction is classified as EC 2.1.1.64)
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?
additional information
?
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the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-6 in Saccharomyces cerevisiae, 1. the methylation of 3,4-dihydroxy-5-hexaprenylbenzoate (this reaction is classified as EC 2.1.1.114) and 2. the methylation of 3-demethylubiquinol-6 (this reaction is classified as EC 2.1.1.64)
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H186A
the mutation completely destroys the interaction of the enzyme with liposomes
I177A
the mutation sharply reduces the interaction of the enzyme with liposomes
K183A
the mutation nearly completely destroys the interaction of the enzyme with liposomes
L132Q
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the mutation results in ubiquinone deficiency in Escherichia coli leading to a high sensitivity to thiols and a failure to grow on succinate
L178A
the mutation nearly completely destroys the interaction of the enzyme with liposomes
L178E
the mutation nearly completely destroys the interaction of the enzyme with liposomes
R179A
the mutation sharply reduces the interaction of the enzyme with liposomes
V181A
the mutation nearly completely destroys the interaction of the enzyme with liposomes
V181A/P182A/K183A/G184A/T185A/H186A
the mutations nearly completely destroy the interaction of the enzyme with liposomes
additional information
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a mutant deleted for ubiG exhibits longer lifespan, as well as enhanced resistance to thermal and oxidative stress (paraquat) compared to wild type at extracellular pH 9.0. The hypoxia-inducible transcription factor ArcA is required for the fully extended lifespan of the mutant
additional information
for mutant UbiGDELTA 165-187 lacking the sequence insertion that covers the methyl donor binding pocket, the binding affinity to SAH is approximately 58fold higher than that of wild-type
additional information
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a mutant deleted for ubiG exhibits longer lifespan, as well as enhanced resistance to thermal and oxidative stress (paraquat) compared to wild type at extracellular pH 9.0. The hypoxia-inducible transcription factor ArcA is required for the fully extended lifespan of the mutant
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Poon, W.W.; Barkovich, R.J.; Hsu, A.Y.; Frankel, A.; Lee, P.T.; Sheperd, J.N.; Myles, D.C.; Clarke, C.F.
Yeast and rat Coq3 and Escherichia coli UbiG polypeptides catalyze both O-methyltransferase steps in coenzyme Q biosynthesis
J. Biol. Chem.
274
21665-21672
1999
Escherichia coli, Saccharomyces cerevisiae (P27680), Rattus norvegicus (Q63159)
brenda
Jonassen, T.; Clarke, C.F.
Isolation and functional expression of human COQ3, a gene encoding a methyltransferase required for ubiquinone biosynthesis
J. Biol. Chem.
275
12381-12387
2000
Homo sapiens (Q9NZJ6)
brenda
Hsu, A.Y.; Poon, W.W.; Shepherd, J.A.; Myles, D.C.; Clarke, C.F.
Complementation of coq3 mutant yeast by mitochondrial targeting of the Escherichia coli UbiG polypeptide: evidence that UbiG catalyzes both O-methylation steps in ubiquinone biosynthesis
Biochemistry
35
9797-9806
1996
Escherichia coli
brenda
Gibert, I.; Llagostera, M.; Barbe, J.
Regulation of ubiG gene expression in Escherichia coli
J. Bacteriol.
170
1346-1349
1988
Escherichia coli
brenda
Joyce, A.R.
Reed, J.L.; White, A.; Edwards, R.; Osterman, A.; Baba, T.; Mori, H.; Lesely, S.A.; Palsson, B.; Agarwalla, S.: Experimental and computational assessment of conditionally essential genes in Escherichia coli
J. Bacteriol.
188
8259-8271
2006
Escherichia coli
brenda
Soballe, B.; Poole, R.K.
Ubiquinone limits oxidative stress in Escherichia coli
Microbiology
146
787-796
2000
Escherichia coli
brenda
Xing, L.; Zhu, Y.; Fang, P.; Wang, J.; Zeng, F.; Li, X.; Teng, M.; Li, X.
Crystallization and preliminary crystallographic studies of UbiG, an O-methyltransferase from Escherichia coli
Acta Crystallogr. Sect. F
67
727-729
2011
Escherichia coli
brenda
Gonidakis, S.; Finkel, S.E.; Longo, V.D.
Lifespan extension and paraquat resistance in a ubiquinone-deficient Escherichia coli mutant depend on transcription factors ArcA and TdcA
Aging
3
291-303
2011
Escherichia coli, Escherichia coli BW25113
brenda
Lu, W.; Shi, Y.; He, S.; Fei, Y.; Yu, K.; Yu, H.
Enhanced production of CoQ10 by constitutive overexpression of 3-demethyl ubiquinone-9 3-methyltransferase under tac promoter in Rhodobacter sphaeroides
Biochem. Eng. J.
72
42-47
2013
Cereibacter sphaeroides (Q3IYM5)
brenda
Zhu, Y.; Wu, B.; Zhang, X.; Fan, X.; Niu, L.; Li, X.; Wang, J.; Teng, M.
Structural and biochemical studies reveal UbiG/Coq3 as a class of novel membrane-binding proteins
Biochem. J.
470
105-114
2015
Escherichia coli (P17993)
brenda
Lu, W.; Ye, L.; Lv, X.; Xie, W.; Gu, J.; Chen, Z.; Zhu, Y.; Li, A.; Yu, H.
Identification and elimination of metabolic bottlenecks in the quinone modification pathway for enhanced coenzyme Q10 production in Rhodobacter sphaeroides
Metab. Eng.
29
208-216
2015
Cereibacter sphaeroides
brenda
Zhu, Y.; Jiang, X.; Wang, C.; Liu, Y.; Fan, X.; Zhang, L.; Niu, L.; Teng, M.; Li, X.
Structural insights into the methyl donor recognition model of a novel membrane-binding protein UbiG
Sci. Rep.
6
23147
2016
Escherichia coli (C3T302)
brenda