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1971•Agricultural and Biological ChemistryOpen access

Metabolism of Pyridine Coenzymes in Microorganisms

Masaaki Kuwahara, Takashi Tachiki, Tatsurokuro Tochikura, Kôichi Ogata

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Abstract

The NADP analog and NAD diphosphate were tested for the coenzyme or inhibiting activity toward various dehydrogenases. These NAD derivatives showed little or no ac-tivity of as coenzymes for most of dehydrogenases tested. Only glyceraldehyde 3-phosphate dehydrogenase reduced the NADP analog under the high concentration of enzyme system. These NAD derivatives showed no inhibiting effect toward the reduction or oxidation of pyridine coenzymes.

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The NADP analog and NAD diphosphate were tested for the coenzyme or inhibiting activity toward various dehydrogenases. These NAD derivatives showed little or no ac-tivity of as coenzymes for most of dehydrogenases tested. Only glyceraldehyde 3-phosphate dehydrogenase reduced the NADP analog under the high concentration of enzyme system. These NAD derivatives showed no inhibiting effect toward the reduction or oxidation of pyridine coenzymes.

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Available abstract

The NADP analog and NAD diphosphate were tested for the coenzyme or inhibiting activity toward various dehydrogenases. These NAD derivatives showed little or no ac-tivity of as coenzymes for most of dehydrogenases tested. Only glyceraldehyde 3-phosphate dehydrogenase reduced the NADP analog under the high concentration of enzyme system. These NAD derivatives showed no inhibiting effect toward the reduction or oxidation of pyridine coenzymes.

Key concepts: Cofactor, NAD+ kinase, Chemistry, Dehydrogenase, Biochemistry, Enzyme, Pyridine, Metabolism

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