NAD kinase from Bacillus licheniformis: inhibition by NADP and other properties.

Abstract:

:NAD kinase was purified 180-fold from Bacillus licheniformis to determine the role it plays in NADP turnover in this organism. The enzyme was found to have a pH optimum of 6.8 and an apparent Km for NAD of 2.7 mM. The ATP saturation curve was not hyperbolic; 5.5 mM ATP was required to reach half maximal activity. Both Mn2+ and Ca2+ could be substituted for Mg2+. Several compounds including nicotinic acid, nicotinamide, nicotinamide mononucleotide, quinolinic acid, NADPH, ADP, AMP and cyclic AMP did not affect NAD kinase activity. In contrast, the enzyme was inhibited by NADP at concentrations typically found in logarithmic cells of B. licheniformis. This inhibition was competitive with NAD and had a Ki of 0.13 mM. It is suggested that in vivo NAD kinase activity is highly dependent on the concentrations of NAD and ATP and the proportion of oxidized and reduced NADP.

journal_name

Arch Microbiol

journal_title

Archives of microbiology

authors

Zerez CR,Moul DE,Andreoli AJ

doi

10.1007/BF00409878

subject

Has Abstract

pub_date

1986-05-01 00:00:00

pages

313-6

issue

4

eissn

0302-8933

issn

1432-072X

journal_volume

144

pub_type

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