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000010968 0247_ $$2DOI$$a10.1007/s00253-010-2481-y
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000010968 084__ $$2WoS$$aBiotechnology & Applied Microbiology
000010968 1001_ $$0P:(DE-HGF)0$$aLindner, S.N.$$b0
000010968 245__ $$aPolyphosphate/ATP-dependent NAD kinase of Corynebacterium glutamicum: biochemical properties and impact of ppnK overexpression on lysine production
000010968 260__ $$aBerlin$$bSpringer$$c2010
000010968 300__ $$a583 - 593
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000010968 440_0 $$0555$$aApplied Microbiology and Biotechnology$$v87$$x0175-7598$$y2
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000010968 520__ $$aNicotinamide adenine dinucleotide phosphate (NADP) is synthesized by phosphorylation of either oxidized or reduced nicotinamide adenine dinucleotide (NAD/NADH). Here, the cg1601/ppnK gene product from Corynebacterium glutamicum genome was purified from recombinant Escherichia coli and enzymatic characterization revealed its activity as a polyphosphate (PolyP)/ATP-dependent NAD kinase (PPNK). PPNK from C. glutamicum was shown to be active as homotetramer accepting PolyP, ATP, and even ADP for phosphorylation of NAD. The catalytic efficiency with ATP as phosphate donor for phosphorylation of NAD was higher than with PolyP. With respect to the chain length of PolyP, PPNK was active with short-chain PolyPs. PPNK activity was independent of bivalent cations when using ATP, but was enhanced by manganese and in particular by magnesium ions. When using PolyP, PPNK required bivalent cations, preferably manganese ions, for activity. PPNK was inhibited by NADP and NADH at concentrations below millimolar. Overexpression of ppnK in C. glutamicum wild type slightly reduced growth and ppnK overexpression in the lysine producing strain DM1729 resulted in a lysine product yield on glucose of 0.136 +/- 0.006 mol lysine (mol glucose)(-1), which was 12% higher than that of the empty vector control strain.
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000010968 650_2 $$2MeSH$$aAdenosine Triphosphate: metabolism
000010968 650_2 $$2MeSH$$aAmino Acid Sequence
000010968 650_2 $$2MeSH$$aBacterial Proteins: chemistry
000010968 650_2 $$2MeSH$$aBacterial Proteins: genetics
000010968 650_2 $$2MeSH$$aBacterial Proteins: metabolism
000010968 650_2 $$2MeSH$$aCorynebacterium glutamicum: chemistry
000010968 650_2 $$2MeSH$$aCorynebacterium glutamicum: enzymology
000010968 650_2 $$2MeSH$$aCorynebacterium glutamicum: genetics
000010968 650_2 $$2MeSH$$aCorynebacterium glutamicum: metabolism
000010968 650_2 $$2MeSH$$aGene Expression
000010968 650_2 $$2MeSH$$aLysine: biosynthesis
000010968 650_2 $$2MeSH$$aMolecular Sequence Data
000010968 650_2 $$2MeSH$$aPhosphotransferases: chemistry
000010968 650_2 $$2MeSH$$aPhosphotransferases: genetics
000010968 650_2 $$2MeSH$$aPhosphotransferases: metabolism
000010968 650_2 $$2MeSH$$aPolyphosphates: chemistry
000010968 650_2 $$2MeSH$$aPolyphosphates: metabolism
000010968 650_2 $$2MeSH$$aProtein Multimerization
000010968 650_2 $$2MeSH$$aSequence Homology, Amino Acid
000010968 650_2 $$2MeSH$$aSubstrate Specificity
000010968 650_7 $$00$$2NLM Chemicals$$aBacterial Proteins
000010968 650_7 $$00$$2NLM Chemicals$$aPolyphosphates
000010968 650_7 $$056-65-5$$2NLM Chemicals$$aAdenosine Triphosphate
000010968 650_7 $$056-87-1$$2NLM Chemicals$$aLysine
000010968 650_7 $$0EC 2.7.-$$2NLM Chemicals$$aPhosphotransferases
000010968 650_7 $$0EC 2.7.1.-$$2NLM Chemicals$$apolyphosphate NAD-kinase
000010968 650_7 $$2WoSType$$aJ
000010968 65320 $$2Author$$aPolyphosphate
000010968 65320 $$2Author$$aNAD kinase
000010968 65320 $$2Author$$aCorynebacterium
000010968 65320 $$2Author$$aLysine production
000010968 7001_ $$0P:(DE-HGF)0$$aNiederholtmeyer, H.$$b1
000010968 7001_ $$0P:(DE-HGF)0$$aSchmitz, K.$$b2
000010968 7001_ $$0P:(DE-Juel1)VDB93979$$aSchobert, S.$$b3$$uFZJ
000010968 7001_ $$0P:(DE-Juel1)VDB1764$$aWendisch, V. F.$$b4$$uFZJ
000010968 773__ $$0PERI:(DE-600)1464336-4$$a10.1007/s00253-010-2481-y$$gVol. 87, p. 583 - 593$$p583 - 593$$q87<583 - 593$$tApplied Microbiology and Biotechnology$$v87$$x0175-7598$$y2010
000010968 8567_ $$uhttp://dx.doi.org/10.1007/s00253-010-2481-y
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