EC Number   |
General Information |
Reference |
|---|
    2.1.1.201 | malfunction |
deletion of the chromosomal COQ5 gene results in a respiration deficiency and reduced levels of respiratory protein components |
704387 |
| 2.1.1.201 | malfunction |
in humans, mutations in several COQ genes cause primary Q deficiency, and a decrease in coenzyme Q biosynthesis is associated with mitochondrial, cardiovascular, kidney and neurodegenerative diseases |
735704 |
| 2.1.1.201 | malfunction |
strains of Escherichia coli with mutations in the ubiE gene are not able to catalyze the carbon methylation reaction in the biosynthesis of ubiquinone (coenzyme Q) and menaquinone (vitamin K2), essential isoprenoid quinone components of the respiratory electron transport chain |
698549 |
| 2.1.1.201 | malfunction |
ubiE mutant accumulate 2-methoxy-6-octaprenyl-1,4-benzoquinol |
704239 |
| 2.1.1.201 | metabolism |
Coq5 is an S-adenosyl methionine-dependent methyltransferase (SAM-MTase) that catalyzes the only C-methylation step in the coenzyme Q (CoQ) biosynthesis pathway, in which 2-methoxy-6-polyprenyl-1,4-benzoquinone (DDMQH2) is converted to 2-methoxy-5-methyl-6-polyprenyl-1,4-benzoquinone |
735364 |
| 2.1.1.201 | metabolism |
the broccoli BoCOQ5-2 methyltransferase gene is involved in the ubiquinone biosynthetic pathway |
720768 |
| 2.1.1.201 | more |
Coq5 displays a typical class I SAM-MTase structure with two minor variations beyond the core domain, both of which are considered to participate in dimerization and/or substrate recognition. Slight conformational changes at the active-site pocket are observed upon binding of SAM. Remodelling of the substrate-binding site, structure-based computational simulation, overview |
735364 |
| 2.1.1.201 | more |
expression of BoCOQ5-2 stimulates Se volatilization in bacteria and plants |
720768 |
| 2.1.1.201 | physiological function |
BoCOQ5-2 methyltransferase is a facilitator of selenium volatilization |
720768 |
| 2.1.1.201 | physiological function |
chemical uncoupler carbonyl cyanide-p-trifluoromethoxyphenylhydrazone suppresses the COQ5 in mitochondrion and in cybrids with MERRF mutation, associated with decreased mitochondrial membrane potential and mitochondrial ATP production. Total CoQ10 levels are decreased under both conditions, but the ubiquinol-10:ubiquinone-10 ratio is increased in mutant cybrids. The expression of COQ5 is increased but COQ5 protein maturation is suppressed in the mutant cybrids |
756080 |
