|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 188.8.131.52
Enzymes and Genes:
bifunctional 3-demethylubiquinone-8 3-O-methyltransferase and 2-octaprenyl-6-hydroxyphenol methylase : ubiG ( Escherichia coli K-12 substr. MG1655 )
hexaprenyldihydroxybenzoate methyltransferase : COQ3 ( Homo sapiens )
In Pathway: ubiquinol-8 biosynthesis (prokaryotic)
Note that this reaction equation differs from the official Enzyme Commission reaction equation for this EC number, which can be found here .
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.
Mass balance status: Balanced.
Enzyme Commission Primary Name: 2-polyprenyl-6-hydroxyphenol methylase
Enzyme Commission Synonyms: ubiG (gene name, ambiguous), ubiG methyltransferase (ambiguous), 2-octaprenyl-6-hydroxyphenol methylase
Standard Gibbs Free Energy (ΔrG'° in kcal/mol): -4.359993 [Latendresse13]
The enzyme is involved in the pathway of ubiquinone-8 in Escherichia coli. COQ3 from human, yeast and rat also catalyse the reaction although this is not a step in biosynthesis of ubiquinone in these organisms [Poon99]. The enzyme also catalyses the methylation of 3-demethylubiquinone-8 (this activity is classified as EC 184.108.40.206) [Hsu96].
Enzyme Commission Summary:
UbiG catalyses both methylation steps in ubiquinone biosynthesis in Escherichia coli. The second methylation is classified as EC 220.127.116.11 (3-demethylubiquinol 3-O-methyltransferase) [Hsu96]. In eukaryotes Coq3 catalyses the two methylation steps in ubiquinone biosynthesis. However, while the second methylation is common to both enzymes, the first methylation by Coq3 occurs at a different position within the pathway, and thus involves a different substrate and is classified as EC 18.104.22.168 (polyprenyldihydroxybenzoate methyltransferase). The substrate of the eukaryotic enzyme (3,4-dihydroxy-5-all-trans-polyprenylbenzoate) differs by an additional carboxylate moiety.
Instance reactions of [a 3-(all-trans-polyrenyl)benzene-1,2-diol + S-adenosyl-L-methionine → a 2-methoxy-6-(all-trans-polyprenyl)phenol + S-adenosyl-L-homocysteine + H+] (22.214.171.124):
i1: 3-(all-trans-decaprenyl)benzene-1,2-diol + S-adenosyl-L-methionine → 2-methoxy-6-(all-trans-decaprenyl)phenol + S-adenosyl-L-homocysteine + H+ (126.96.36.199)
i2: 3-(all-trans-nonaprenyl)benzene-1,2-diol + S-adenosyl-L-methionine → 2-methoxy-6-(all-trans-nonaprenyl)phenol + S-adenosyl-L-homocysteine + H+ (188.8.131.52)
i3: 3-(all-trans-octaprenyl)benzene-1,2-diol + S-adenosyl-L-methionine → 2-methoxy-6-(all-trans-octaprenyl)phenol + S-adenosyl-L-homocysteine + H+ (184.108.40.206)
i4: 3-(all-trans-heptaprenyl)benzene-1,2-diol + S-adenosyl-L-methionine → 2-methoxy-6-(all-trans-heptaprenyl)phenol + S-adenosyl-L-homocysteine + H+ (220.127.116.11)
Hsu96: Hsu AY, Poon WW, Shepherd JA, Myles DC, Clarke CF (1996). "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 1996;35(30);9797-806. PMID: 8703953
Poon99: Poon WW, Barkovich RJ, Hsu AY, Frankel A, Lee PT, Shepherd JN, Myles DC, Clarke CF (1999). "Yeast and rat Coq3 and Escherichia coli UbiG polypeptides catalyze both O-methyltransferase steps in coenzyme Q biosynthesis." J Biol Chem 274(31);21665-72. PMID: 10419476
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