EC 2.1.1.222 - 2-polyprenyl-6-hydroxyphenol methylase

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IntEnz Enzyme Nomenclature
EC 2.1.1.222

Names

Accepted name:
2-polyprenyl-6-hydroxyphenol methylase
Other names:
ubiG (gene name) [ambiguous]
ubiG methyltransferase [ambiguous]
2-octaprenyl-6-hydroxyphenol methylase
Systematic name:
S-adenosyl-L-methionine:3-(all-trans-polyprenyl)benzene-1,2-diol 2-O-methyltransferase

Reactions

Comments:

UbiG catalyses both methylation steps in ubiquinone biosynthesis in Escherichia coli. The second methylation is classified as EC 2.1.1.64 (3-demethylubiquinol 3-O-methyltransferase) [2]. 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 2.1.1.114 (polyprenyldihydroxybenzoate methyltransferase). The substrate of the eukaryotic enzyme (3,4-dihydroxy-5-all-trans-polyprenylbenzoate) differs by an additional carboxylate moiety.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot: (244) [show] [UniProt]

References

  1. Poon, W. W., Barkovich, R. J., Hsu, A. Y., Frankel, A., Lee, P. T., Shepherd, 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). [PMID: 10419476]
  2. 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). [PMID: 8703953]

[EC 2.1.1.222 created 2011, modified 2013]