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| Home > Publications database > Effect of pyruvate dehydrogenase complex deficiency on L-lysine production with Corynebacterium glutamicum > print |
| 001 | 59689 | ||
| 005 | 20190625111848.0 | ||
| 024 | 7 | _ | |2 pmid |a pmid:17333167 |
| 024 | 7 | _ | |2 DOI |a 10.1007/s00253-007-0904-1 |
| 024 | 7 | _ | |2 WOS |a WOS:000248893700015 |
| 024 | 7 | _ | |2 ISSN |a 0175-7598 |
| 024 | 7 | _ | |a altmetric:21818157 |2 altmetric |
| 037 | _ | _ | |a PreJuSER-59689 |
| 041 | _ | _ | |a eng |
| 082 | _ | _ | |a 570 |
| 084 | _ | _ | |2 WoS |a Biotechnology & Applied Microbiology |
| 100 | 1 | _ | |a Blombach, B. |b 0 |0 P:(DE-HGF)0 |
| 245 | _ | _ | |a Effect of pyruvate dehydrogenase complex deficiency on L-lysine production with Corynebacterium glutamicum |
| 260 | _ | _ | |c 2007 |a Berlin |b Springer |
| 300 | _ | _ | |a 615 - 623 |
| 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 3 |v 76 |
| 500 | _ | _ | |a Record converted from VDB: 12.11.2012 |
| 520 | _ | _ | |a Intracellular precursor supply is a critical factor for amino acid productivity of Corynebacterium glutamicum. To test for the effect of improved pyruvate availability on L-lysine production, we deleted the aceE gene encoding the E1p enzyme of the pyruvate dehydrogenase complex (PDHC) in the L-lysine-producer C. glutamicum DM1729 and characterised the resulting strain DM1729-BB1 for growth and L-lysine production. Compared to the host strain, C. glutamicum DM1729-BB1 showed no PDHC activity, was acetate auxotrophic and, after complete consumption of the available carbon sources glucose and acetate, showed a more than 50% lower substrate-specific biomass yield (0.14 vs 0.33 mol C/mol C), an about fourfold higher biomass-specific L-lysine yield (5.27 vs 1.23 mmol/g cell dry weight) and a more than 40% higher substrate-specific L-lysine yield (0.13 vs 0.09 mol C/mol C). Overexpression of the pyruvate carboxylase or diaminopimelate dehydrogenase genes in C. glutamicum DM1729-BB1 resulted in a further increase in the biomass-specific L-lysine yield by 6 and 56%, respectively. In addition to L-lysine, significant amounts of pyruvate, L-alanine and L-valine were produced by C. glutamicum DM1729-BB1 and its derivatives, suggesting a surplus of precursor availability and a further potential to improve L-lysine production by engineering the L-lysine biosynthetic pathway. |
| 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 Base Sequence |
| 650 | _ | 2 | |2 MeSH |a Biotechnology |
| 650 | _ | 2 | |2 MeSH |a Corynebacterium glutamicum: genetics |
| 650 | _ | 2 | |2 MeSH |a Corynebacterium glutamicum: growth & development |
| 650 | _ | 2 | |2 MeSH |a Corynebacterium glutamicum: metabolism |
| 650 | _ | 2 | |2 MeSH |a DNA, Bacterial: genetics |
| 650 | _ | 2 | |2 MeSH |a Fermentation |
| 650 | _ | 2 | |2 MeSH |a Gene Deletion |
| 650 | _ | 2 | |2 MeSH |a Gene Expression |
| 650 | _ | 2 | |2 MeSH |a Genes, Bacterial |
| 650 | _ | 2 | |2 MeSH |a Kinetics |
| 650 | _ | 2 | |2 MeSH |a Lysine: biosynthesis |
| 650 | _ | 2 | |2 MeSH |a Pyruvate Dehydrogenase Complex: genetics |
| 650 | _ | 2 | |2 MeSH |a Pyruvate Dehydrogenase Complex: metabolism |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a DNA, Bacterial |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Pyruvate Dehydrogenase Complex |
| 650 | _ | 7 | |0 56-87-1 |2 NLM Chemicals |a Lysine |
| 650 | _ | 7 | |a J |2 WoSType |
| 653 | 2 | 0 | |2 Author |a Corynebacterium glutamicum |
| 653 | 2 | 0 | |2 Author |a L-lysine |
| 653 | 2 | 0 | |2 Author |a pyruvate dehydrogenase complex |
| 653 | 2 | 0 | |2 Author |a L-lysine production |
| 700 | 1 | _ | |a Schreiner, M. E. |b 1 |0 P:(DE-HGF)0 |
| 700 | 1 | _ | |a Moch, M. |b 2 |u FZJ |0 P:(DE-Juel1)VDB23977 |
| 700 | 1 | _ | |a Oldiges, M. |b 3 |u FZJ |0 P:(DE-Juel1)129053 |
| 700 | 1 | _ | |a Eikmanns, B. J. |b 4 |0 P:(DE-HGF)0 |
| 773 | _ | _ | |0 PERI:(DE-600)1464336-4 |a 10.1007/s00253-007-0904-1 |g Vol. 76, p. 615 - 623 |p 615 - 623 |q 76<615 - 623 |t Applied Microbiology and Biotechnology |v 76 |x 0175-7598 |y 2007 |
| 856 | 7 | _ | |u http://dx.doi.org/10.1007/s00253-007-0904-1 |
| 909 | C | O | |o oai:juser.fz-juelich.de:59689 |p VDB |
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| 914 | 1 | _ | |y 2007 |
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| 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 |
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