Metabolism of Pyridine Coenzymes in Microorganisms
Masaaki Kuwahara, Takashi Tachiki, Tatsurokuro Tochikura, Kôichi Ogata
Abstract
Masaaki Kuwahara, Takashi Tachiki, Tatsurokuro Tochikura, Kôichi Ogata
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 activity 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 activity 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: NAD+ kinase, Cofactor, Chemistry, Dehydrogenase, Biochemistry, Enzyme, Pyridine, Metabolism