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@ARTICLE{Lindner:10968,
author = {Lindner, S.N. and Niederholtmeyer, H. and Schmitz, K. and
Schobert, S. and Wendisch, V. F.},
title = {{P}olyphosphate/{ATP}-dependent {NAD} kinase of
{C}orynebacterium glutamicum: biochemical properties and
impact of ppn{K} overexpression on lysine production},
journal = {Applied Microbiology and Biotechnology},
volume = {87},
issn = {0175-7598},
address = {Berlin},
publisher = {Springer},
reportid = {PreJuSER-10968},
pages = {583 - 593},
year = {2010},
note = {Record converted from VDB: 12.11.2012},
abstract = {Nicotinamide 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.},
keywords = {Adenosine Triphosphate: metabolism / Amino Acid Sequence /
Bacterial Proteins: chemistry / Bacterial Proteins: genetics
/ Bacterial Proteins: metabolism / Corynebacterium
glutamicum: chemistry / Corynebacterium glutamicum:
enzymology / Corynebacterium glutamicum: genetics /
Corynebacterium glutamicum: metabolism / Gene Expression /
Lysine: biosynthesis / Molecular Sequence Data /
Phosphotransferases: chemistry / Phosphotransferases:
genetics / Phosphotransferases: metabolism / Polyphosphates:
chemistry / Polyphosphates: metabolism / Protein
Multimerization / Sequence Homology, Amino Acid / Substrate
Specificity / Bacterial Proteins (NLM Chemicals) /
Polyphosphates (NLM Chemicals) / Adenosine Triphosphate (NLM
Chemicals) / Lysine (NLM Chemicals) / Phosphotransferases
(NLM Chemicals) / polyphosphate NAD-kinase (NLM Chemicals) /
J (WoSType)},
cin = {IBT-1},
ddc = {570},
cid = {I:(DE-Juel1)VDB55},
pnm = {Biotechnologie},
pid = {G:(DE-Juel1)FUEK410},
shelfmark = {Biotechnology $\&$ Applied Microbiology},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:20180116},
UT = {WOS:000277959500020},
doi = {10.1007/s00253-010-2481-y},
url = {https://juser.fz-juelich.de/record/10968},
}