Biology:2-Polyprenyl-6-hydroxyphenol methylase
From HandWiki
Short description: Class of enzymes
| 2-polyprenyl-6-hydroxyphenol methylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.1.1.222 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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2-polyprenyl-6-hydroxyphenol methylase (EC 2.1.1.222, ubiG (gene), ubiG methyltransferase, 2-octaprenyl-6-hydroxyphenol methylase) is an enzyme with systematic name S-adenosyl-L-methionine:3-(all-trans-polyprenyl)benzene-1,2-diol 2-O-methyltransferase.[1][2] This enzyme catalyses the following chemical reaction
- S-adenosyl-L-methionine + 3-(all-trans-polyprenyl)benzene-1,2-diol [math]\displaystyle{ \rightleftharpoons }[/math] S-adenosyl-L-homocysteine + 2-methoxy-6-(all-trans-polyprenyl)phenol
UbiG catalyses both methylation steps in ubiquinone biosynthesis in Escherichia coli.
References
- ↑ "Yeast and rat Coq3 and Escherichia coli UbiG polypeptides catalyze both O-methyltransferase steps in coenzyme Q biosynthesis". The Journal of Biological Chemistry 274 (31): 21665–72. July 1999. doi:10.1074/jbc.274.31.21665. PMID 10419476.
- ↑ "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 (30): 9797–806. July 1996. doi:10.1021/bi9602932. PMID 8703953.
External links
- 2-polyprenyl-6-hydroxyphenyl+methylase at the US National Library of Medicine Medical Subject Headings (MeSH)
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