Home > Publications database > Polyphosphate/ATP-dependent NAD kinase of Corynebacterium glutamicum: biochemical properties and impact of ppnK overexpression on lysine production > print

001     10968
005     20190625111107.0
024 7 _ |2 pmid
|a pmid:20180116
024 7 _ |2 DOI
|a 10.1007/s00253-010-2481-y
024 7 _ |2 WOS
|a WOS:000277959500020
024 7 _ |2 ISSN
|a 0175-7598
024 7 _ |a altmetric:21804578
|2 altmetric
037 _ _ |a PreJuSER-10968
041 _ _ |a eng
082 _ _ |a 570
084 _ _ |2 WoS
|a Biotechnology & Applied Microbiology
100 1 _ |a Lindner, S.N.
|b 0
|0 P:(DE-HGF)0
245 _ _ |a Polyphosphate/ATP-dependent NAD kinase of Corynebacterium glutamicum: biochemical properties and impact of ppnK overexpression on lysine production
260 _ _ |c 2010
|a Berlin
|b Springer
300 _ _ |a 583 - 593
336 7 _ |a Journal Article
|0 PUB:(DE-HGF)16
|2 PUB:(DE-HGF)
336 7 _ |a Output Types/Journal article
|2 DataCite
336 7 _ |a Journal Article
|0 0
|2 EndNote
336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a JOURNAL_ARTICLE
|2 ORCID
336 7 _ |a article
|2 DRIVER
440 _ 0 |a Applied Microbiology and Biotechnology
|x 0175-7598
|0 555
|y 2
|v 87
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a 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.
536 _ _ |a Biotechnologie
|c PBT
|2 G:(DE-HGF)
|0 G:(DE-Juel1)FUEK410
|x 0
588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Adenosine Triphosphate: metabolism
650 _ 2 |2 MeSH
|a Amino Acid Sequence
650 _ 2 |2 MeSH
|a Bacterial Proteins: chemistry
650 _ 2 |2 MeSH
|a Bacterial Proteins: genetics
650 _ 2 |2 MeSH
|a Bacterial Proteins: metabolism
650 _ 2 |2 MeSH
|a Corynebacterium glutamicum: chemistry
650 _ 2 |2 MeSH
|a Corynebacterium glutamicum: enzymology
650 _ 2 |2 MeSH
|a Corynebacterium glutamicum: genetics
650 _ 2 |2 MeSH
|a Corynebacterium glutamicum: metabolism
650 _ 2 |2 MeSH
|a Gene Expression
650 _ 2 |2 MeSH
|a Lysine: biosynthesis
650 _ 2 |2 MeSH
|a Molecular Sequence Data
650 _ 2 |2 MeSH
|a Phosphotransferases: chemistry
650 _ 2 |2 MeSH
|a Phosphotransferases: genetics
650 _ 2 |2 MeSH
|a Phosphotransferases: metabolism
650 _ 2 |2 MeSH
|a Polyphosphates: chemistry
650 _ 2 |2 MeSH
|a Polyphosphates: metabolism
650 _ 2 |2 MeSH
|a Protein Multimerization
650 _ 2 |2 MeSH
|a Sequence Homology, Amino Acid
650 _ 2 |2 MeSH
|a Substrate Specificity
650 _ 7 |0 0
|2 NLM Chemicals
|a Bacterial Proteins
650 _ 7 |0 0
|2 NLM Chemicals
|a Polyphosphates
650 _ 7 |0 56-65-5
|2 NLM Chemicals
|a Adenosine Triphosphate
650 _ 7 |0 56-87-1
|2 NLM Chemicals
|a Lysine
650 _ 7 |0 EC 2.7.-
|2 NLM Chemicals
|a Phosphotransferases
650 _ 7 |0 EC 2.7.1.-
|2 NLM Chemicals
|a polyphosphate NAD-kinase
650 _ 7 |a J
|2 WoSType
653 2 0 |2 Author
|a Polyphosphate
653 2 0 |2 Author
|a NAD kinase
653 2 0 |2 Author
|a Corynebacterium
653 2 0 |2 Author
|a Lysine production
700 1 _ |a Niederholtmeyer, H.
|b 1
|0 P:(DE-HGF)0
700 1 _ |a Schmitz, K.
|b 2
|0 P:(DE-HGF)0
700 1 _ |a Schobert, S.
|b 3
|u FZJ
|0 P:(DE-Juel1)VDB93979
700 1 _ |a Wendisch, V. F.
|b 4
|u FZJ
|0 P:(DE-Juel1)VDB1764
773 _ _ |0 PERI:(DE-600)1464336-4
|a 10.1007/s00253-010-2481-y
|g Vol. 87, p. 583 - 593
|p 583 - 593
|q 87<583 - 593
|t Applied Microbiology and Biotechnology
|v 87
|x 0175-7598
|y 2010
856 7 _ |u http://dx.doi.org/10.1007/s00253-010-2481-y
909 C O |o oai:juser.fz-juelich.de:10968
|p VDB
913 1 _ |k PBT
|v Biotechnologie
|l ohne FE
|b außerhalb PoF
|0 G:(DE-Juel1)FUEK410
|x 0
913 2 _ |a DE-HGF
|b Key Technologies
|l Key Technologies for the Bioeconomy
|1 G:(DE-HGF)POF3-580
|0 G:(DE-HGF)POF3-581
|2 G:(DE-HGF)POF3-500
|v Biotechnology
|x 0
914 1 _ |y 2010
915 _ _ |a JCR/ISI refereed
|0 StatID:(DE-HGF)0010
|2 StatID
915 _ _ |a JCR
|0 StatID:(DE-HGF)0100
|2 StatID
915 _ _ |a WoS
|0 StatID:(DE-HGF)0111
|2 StatID
|b Science Citation Index Expanded
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0150
|2 StatID
|b Web of Science Core Collection
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0199
|2 StatID
|b Thomson Reuters Master Journal List
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0300
|2 StatID
|b Medline
920 1 _ |k IBT-1
|l Biotechnologie 1
|g IBT
|z ab 31.10.10 weitergeführt als IBG-1
|0 I:(DE-Juel1)VDB55
|x 0
970 _ _ |a VDB:(DE-Juel1)121691
980 _ _ |a VDB
980 _ _ |a ConvertedRecord
980 _ _ |a journal
980 _ _ |a I:(DE-Juel1)IBG-1-20101118
980 _ _ |a UNRESTRICTED
981 _ _ |a I:(DE-Juel1)IBG-1-20101118

LibraryCollectionCLSMajorCLSMinorLanguageAuthor
Marc 21