Mammalian choline dehydrogenase is a quinoprotein.
نویسندگان
چکیده
منابع مشابه
5-keto-D-gluconate production is catalyzed by a quinoprotein glycerol dehydrogenase, major polyol dehydrogenase, in gluconobacter species.
Acetic acid bacteria, especially Gluconobacter species, have been known to catalyze the extensive oxidation of sugar alcohols (polyols) such as D-mannitol, glycerol, D-sorbitol, and so on. Gluconobacter species also oxidize sugars and sugar acids and uniquely accumulate two different keto-D-gluconates, 2-keto-D-gluconate and 5-keto-D-gluconate, in the culture medium by the oxidation of D-glucon...
متن کاملGenetic Variation of Choline Dehydrogenase Gene in Idiopathic Male Infertility
Infertility can be caused by an unexplained reduction in semen quality in males who present asnormal on physical examination and endocrine testing. There is some evidence that aberrantmetabolism of micronutrients such as choline may play a causative role in male factorinfertility. Choline is a crucial factor in the regulation of sperm membrane structure andmotility, and this nutrient plays an i...
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The soluble quinoprotein glucose dehydrogenase oxidizes glucose, maltose and a variety of other monosaccharides and disaccharides to the corresponding lactones. An efficient microseeding protocol is reported to produce crystals of three variants that display reduced activity towards maltose. Similar cross-seeding protocols to grow crystals of homologues from Escherichia coli and Streptomyces co...
متن کاملStructure and mechanism of soluble quinoprotein glucose dehydrogenase.
Soluble glucose dehydrogenase (s-GDH; EC 1.1.99.17) is a classical quinoprotein which requires the cofactor pyrroloquinoline quinone (PQQ) to oxidize glucose to gluconolactone. The reaction mechanism of PQQ-dependent enzymes has remained controversial due to the absence of comprehensive structural data. We have determined the X-ray structure of s-GDH with the cofactor at 2.2 A resolution, and o...
متن کاملQuinoprotein alcohol dehydrogenase from ethanol-grown Pseudomonas aeruginosa.
Cell-free extracts of Pseudomonas aeruginosa strains, grown on ethanol, showed dye-linked alcohol dehydrogenase activities. The enzyme responsible for this activity was purified to homogeneity. It appeared to contain two molecules of pyrroloquinoline quinone per enzyme molecule. In many respects, it resembled other quinoprotein alcohol dehydrogenases (EC 1.1.99.8), having a substrate specificit...
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ژورنال
عنوان ژورنال: Agricultural and Biological Chemistry
سال: 1985
ISSN: 0002-1369,1881-1280
DOI: 10.1271/bbb1961.49.3623