This enzyme is involved in ubiquinone biosynthesis. Ubiquinones from different organisms have a different number of prenyl units (for example, ubiquinone-6 in Saccharomyces, ubiquinone-9 in rat and ubiquinone-10 in human), and thus the natural substrate for the enzymes from different organisms has a different number of prenyl units. However, the enzyme usually shows a low degree of specificity regarding the number of prenyl units. For example, the human COQ3 enzyme can restore biosynthesis of ubiquinone-6 in coq3 deletion mutants of yeast . The enzymes from yeast, Escherichia coli and rat also catalyse the methylation of 3,4-dihydroxy-5-all-trans-polyprenylbenzoate (a reaction that is classified as EC 2.1.1.114, polyprenyldihydroxybenzoate methyltransferase).
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
This enzyme is involved in ubiquinone biosynthesis. Ubiquinones from different organisms have a different number of prenyl units (for example, ubiquinone-6 in Saccharomyces, ubiquinone-9 in rat and ubiquinone-10 in human), and thus the natural substrate for the enzymes from different organisms has a different number of prenyl units. However, the enzyme usually shows a low degree of specificity regarding the number of prenyl units. For example, the human COQ3 enzyme can restore biosynthesis of ubiquinone-6 in coq3 deletion mutants of yeast [3]. The enzymes from yeast, Escherichia coli and rat also catalyse the methylation of 3,4-dihydroxy-5-all-trans-polyprenylbenzoate [3] (a reaction that is classified as EC 2.1.1.114, polyprenyldihydroxybenzoate methyltransferase).
the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-10, 1. the methylation of 3,4-dihydroxy-5-all-trans-decaprenylbenzoate (this reaction is classified as EC 2.1.1.114) and 2. the methylation of 3-demethylubiquinol-10
wide substrate specificity. The enzyme methylates both eukaryotic substrates 3,4-dihydroxy-5-farnesylbenzoic acid (this activity is classified as EC 2.1.1.114) and demethylubiquinol-3 and the distinct prokaryotic substrate 3-((2E,6E)-farnesyl)benzene-1,2-diol
3-demethylubiquinol-6 is an intermediate in biosynthesis of ubiquinone-6 in Saccharomyces cerevisiae (methylated by the yeast enzyme COQ3 to ubiquinol-6). The human construct rescues the growth of a yeast coq3 null mutant on a nonfermentable carbon source and restores coenzyme Q biosynthesis, although at lower levels than that of wild type yeast
the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-6 in Saccharomyces cerevisiae, 1. the methylation of 3,4-dihydroxy-5-all-trans-hexaprenylbenzoate (this reaction is classified as EC 2.1.1.114) and 2. the methylation of 3-demethylubiquinol-6
the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-8 in Escherichia coli, 1. the methylation of 3,4-dihydroxy-5-all-trans-octaprenylbenzoate (this reaction is classified as EC 2.1.1.114) and 2. the methylation of 3-demethylubiquinol-8
the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-8 in Escherichia coli, 1. the methylation of 3,4-dihydroxy-5-octaprenylbenzoate (this reaction is classified as EC 2.1.1.114) and 2. the methylation of 3-demethylubiquinol-8
the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-9 in Rattus norvegicus, 1. the methylation of 3,4-dihydroxy-5-all-trans-octaprenylbenzoate (this reaction is classified as EC 2.1.1.114) and 2. the methylation of 3-demethylubiquinol-9
the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-10, 1. the methylation of 3,4-dihydroxy-5-all-trans-decaprenylbenzoate (this reaction is classified as EC 2.1.1.114) and 2. the methylation of 3-demethylubiquinol-10
the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-6 in Saccharomyces cerevisiae, 1. the methylation of 3,4-dihydroxy-5-all-trans-hexaprenylbenzoate (this reaction is classified as EC 2.1.1.114) and 2. the methylation of 3-demethylubiquinol-6
the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-8 in Escherichia coli, 1. the methylation of 3,4-dihydroxy-5-all-trans-octaprenylbenzoate (this reaction is classified as EC 2.1.1.114) and 2. the methylation of 3-demethylubiquinol-8
the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-8 in Escherichia coli, 1. the methylation of 3,4-dihydroxy-5-octaprenylbenzoate (this reaction is classified as EC 2.1.1.114) and 2. the methylation of 3-demethylubiquinol-8
the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-9 in Rattus norvegicus, 1. the methylation of 3,4-dihydroxy-5-all-trans-octaprenylbenzoate (this reaction is classified as EC 2.1.1.114) and 2. the methylation of 3-demethylubiquinol-9
the optimum ratio of dithiothreitol to divalent metal ion is about 10:1. The maximal methyltransferase activity is achieved at 10 mM dithiothreitol and 1 mM Zn2+
after 1 h of H2O2 treatment, the viability of the strain defective in ubiG is reduced 28fold compared to the corresponding wild-type. When treated with CuSO4, the viability of the the strain defective in ubiG (HW271), is reduced 4.4fold after 30 min compared to its isogenic wild-type
the membrane-binding region of UbiG gates the entrance of methyl donor. When bound with liposome, UbiG displays an enhanced binding ability toward the methyl donor product S-adenosylhomocysteine
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using either 0.1 M HEPES pH 7.5 and 20% polyethylene glycol 10000 or 10% (v/v) 2-methyl-2,4-pentanediol and 0.1 M HEPES pH 7.0
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
when expressed in multicopy, the human construct rescues the growth of a yeast coq3 null mutant on a nonfermentable carbon source and restores coenzyme Q biosynthesis, although at lower levels than that of wild type yeast
Cloning and functional expression of AtCOQ3, the Arabidopsis homologue of the yeast COQ3 gene, encoding a methyltransferase from the plant mitochondria involved in ubiquinone biosynthesis
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
Cloning of a rat cDNA encoding dihydroxypolyprenylbenzoate methyltransferase by functional complementation of a Saccharomyces cerevisiae mutant deficient in ubiquinone biosynthesis
Lee, P.T.; Strahan, J.; Shepherd, J.N., Clarke, C.F.: Coq3 and Coq4 define a polypeptide complex in yeast mitochondria for the biosynthesis of coenzyme Q