ATP- and Polyphosphate-Dependent Bacterial NAD super(+) Kinases

Measurable levels of activity of NAD super(+) kinases of actinomycetes Micrococcus luteus and Corynebacterium ammoniagenes were observed after substituting inorganic tripolyphosphate for ATP, whereas the enzyme from the eubacterium Escherichia coli was not active with this substrate. Gradient PAGE f...

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Veröffentlicht in:Applied biochemistry and microbiology 2000-03, Vol.36 (2), p.97-100
Hauptverfasser: Filippovich, SY, Afanas'eva, T P, Bachurina, G P, Kritskii, MS
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creator Filippovich, SY
Afanas'eva, T P
Bachurina, G P
Kritskii, MS
description Measurable levels of activity of NAD super(+) kinases of actinomycetes Micrococcus luteus and Corynebacterium ammoniagenes were observed after substituting inorganic tripolyphosphate for ATP, whereas the enzyme from the eubacterium Escherichia coli was not active with this substrate. Gradient PAGE found two molecular isoforms of NAD super(+) kinase in C. ammoniagenes and E. coli; four forms were found in M. luteus. All isoforms of this enzyme found in C. ammoniagenes and M. luteus displayed NADP-synthesizing activity in the presence of either ATP or tripolyphosphate. Because of its capability of utilizing inorganic tripolyphosphate, M. luteus is the most promising NADP producer organism.
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subjects ATP
Corynebacterium ammoniagenes
Micrococcus luteus
polyphosphate
tripolyphosphate
title ATP- and Polyphosphate-Dependent Bacterial NAD super(+) Kinases
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