Coenzyme specificity of enzymes in the oxidative pentose phosphate pathway of Gluconobacter oxydans.
The coenzyme specificity of enzymes in the oxidative pentose phosphate pathway of Gluconobacter oxydans was investigated. By investigation of the activities of glucose-6-phosphate dehydrogenase (G6PDH) and 6-phosphogluconate dehydrogenase (6PGDH) in the soluble fraction of G. oxydans, and cloning and expression of genes in Escherichia coli, it was found that both G6PDH and 6PGDH have NAD/NADP dual coenzyme specificities. It was suggested that the pentose phosphate pathway is responsible for NADH regeneration in G. oxydans.
Tonouchi
Naoto
N
AminoScience Laboratories, Ajinomoto Co., Inc., Kawasaki-shi, Japan.
Sugiyama
Masakazu
M
Yokozeki
Kenzo
K
D003001:Cloning, Molecular; D003067:Coenzymes / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics; D020600:Gluconobacter oxydans / Q000201:enzymology* / Q000235:genetics; D005954:Glucosephosphate Dehydrogenase / Q000235:genetics / Q000378:metabolism*; D009243:NAD / Q000378:metabolism; D009249:NADP / Q000378:metabolism; D010084:Oxidation-Reduction; D010427:Pentose Phosphate Pathway / Q000502:physiology*; D010734:Phosphogluconate Dehydrogenase / Q000235:genetics / Q000378:metabolism*; D013379:Substrate Specificity
D003067:Coenzymes; D009243:NAD; D009249:NADP; D010734:Phosphogluconate Dehydrogenase; D005954:Glucosephosphate Dehydrogenase