https://transhumanist.ru/index.php?action=history&feed=atom&title=COQ3 2026-10-28T15:13:02Z История изменений этой страницы в вики MediaWiki 1.43.6 https://transhumanist.ru/index.php?title=COQ3&diff=5597&oldid=prev 2021-05-12T13:51:29Z

<p>Новая страница: «Ubiquinone biosynthesis O-methyltransferase, mitochondrial precursor (3-demethylubiquinol 3-O-methyltransferase) (EC 2.1.1.64) (Polyprenyldihydroxybenzoate methyl...»</p> <p><b>Новая страница</b></p><div>Ubiquinone biosynthesis O-methyltransferase, mitochondrial precursor (3-demethylubiquinol 3-O-methyltransferase) (EC 2.1.1.64) (Polyprenyldihydroxybenzoate methyltransferase) (EC 2.1.1.114) [UG0215E05]<br /> <br /> ==Publications==<br /> <br /> {{medline-entry<br /> |title=Isolation and functional expression of human [[COQ3]], a gene encoding a methyltransferase required for ubiquinone biosynthesis.<br /> |pubmed-url=https://pubmed.ncbi.nlm.nih.gov/10777520<br /> |abstract=The [[COQ3]] gene in Saccharomyces cerevisiae encodes an O-methyltransferase required for two steps in the biosynthetic pathway of ubiquinone (coenzyme Q, or Q). This enzyme methylates an early Q intermediate, 3,4-dihydroxy-5-polyprenylbenzoic acid, as well as the final intermediate in the pathway, converting demethyl-Q to Q. This enzyme is also capable of methylating the distinct prokaryotic early intermediate 2-hydroxy-6-polyprenyl phenol. A full-length cDNA encoding the human homologue of [[COQ3]] was isolated from a human heart cDNA library by sequence homology to rat Coq3. The clone contained a 933-base pair open reading frame that encoded a polypeptide with a great deal of sequence identity to a variety of eukaryotic and prokaryotic Coq3 homologues. In the region between amino acids 89 and 255 in the human sequence, the rat and human homologues are 87% identical, whereas human and yeast are 35% identical. When expressed in multicopy, the human construct rescued the growth of a yeast coq3 null mutant on a nonfermentable carbon source and restored coenzyme Q biosynthesis, although at lower levels than that of wild type yeast. In vitro methyltransferase assays using farnesylated analogues of intermediates in the coenzyme Q biosynthetic pathway as substrates showed that the human enzyme is active with all three substrates tested.<br /> |mesh-terms=* Aging<br /> * Amino Acid Sequence<br /> * Animals<br /> * Base Sequence<br /> * Catechol O-Methyltransferase<br /> * Chromatography, High Pressure Liquid<br /> * DNA, Complementary<br /> * Gene Library<br /> * Humans<br /> * Methyltransferases<br /> * Models, Chemical<br /> * Molecular Sequence Data<br /> * Mutation<br /> * Myocardium<br /> * Rats<br /> * Saccharomyces cerevisiae<br /> * Sequence Homology, Amino Acid<br /> * Time Factors<br /> * Ubiquinone<br /> <br /> |full-text-url=https://sci-hub.do/10.1074/jbc.275.17.12381<br /> }}</div>

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