Coenzyme Specificity of Enzymes in the Oxidative Pentose Phosphate Pathway ofGluconobacter oxydans
Naoto Tonouchi, Masakazu Sugiyama, Kenzo Yokozeki
Abstract
Naoto Tonouchi, Masakazu Sugiyama, Kenzo Yokozeki
Abstract
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.
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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.
Key concepts: Pentose phosphate pathway, Biochemistry, Dehydrogenase, Pentose, Cofactor, NAD+ kinase, Phosphogluconate dehydrogenase, Enzyme