Abstract
In cell extracts of Micrococcus flavus and Arthrobacter sp. KM, inorganic polyphosphate [poly (P)]- and ATP-dependent NADH kinase activities were detected, and both activities were confirmed to be catalyzed by poly (P)/ATP-NAD kinase, but not by NADH-specific kinase. Poly (P)/ATP-NAD kinas from Mycobacterium tuberculosis also exhibited NADH kinase activity. On the other hand, ATP-NAD kinase from Saccharomyces cerevisiae catalyzed the NADH kinase reaction, although that of Escherichia coli showed no NADH kinase activity, nor did a cell extract of E. coli. Thus, it is indicated that poly (P)/ATP-NAD kinase possesses NADH kinase activity in addition to NAD kinase one, while the ability of ATP-NAD kinase to catalyze the NADH kinase reaction differs in microbes that contain the enzyme.
