Fructose-6-phosphate is not a substrate for glucose-6-phosphate dehydrogenase
β Scribed by Jeffery, Jonathan ;Wood, Irene
- Publisher
- John Wiley and Sons
- Year
- 1986
- Tongue
- English
- Weight
- 188 KB
- Volume
- 239
- Category
- Article
- ISSN
- 0022-104X
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β¦ Synopsis
D-Fructose-6-phosphate was shown not to be a substrate for glucose-6-phosphate dehydrogenases (EC. 1.1.1.49) from human erythrocytes, bovine adrenal, rat liver, three yeasts (brewer's yeast, baker's yeast, and Candida utilis), and Leuconostoc mesenteroides. These findings contrast with those of G.M. Kidder (J. Exp. Zool., 226:385-390, '83).
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The electrophoretic distribution and substrate specificities of isozymes of glucose-6-phosphate dehydrogenase (E.C. 1.1.1.49) were studied in seven species of teleost fish. The fish examined included two species of bonefish, Albula neoguinaica and A. glossodonta (Albulidae, Anquilliformes) (Shaklee
Glutamine:fructose-6-phosphate amidotransferase (GFAT) catalyzes the first step in the biosynthesis of amino sugars by transferring the amino group from L-glutamine to the acceptor substrate, fructose 6-phosphate, generating the products glucosamine 6-phosphate and glutamic acid. We describe a metho