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| Hauptseite > Publikationsdatenbank > Metabolic Function of Corynebacterium glutamicum Aminotransferases AlaT and AvtA and Impact on L-Valine Production > print |
| Hauptseite > Publikationsdatenbank > Metabolic Function of Corynebacterium glutamicum Aminotransferases AlaT and AvtA and Impact on L-Valine Production > print |
| 001 | 950 | ||
| 005 | 20180208231723.0 | ||
| 024 | 7 | _ | |2 pmid |a pmid:18931286 |
| 024 | 7 | _ | |2 pmc |a pmc:PMC2607172 |
| 024 | 7 | _ | |2 DOI |a 10.1128/AEM.01025-08 |
| 024 | 7 | _ | |2 WOS |a WOS:000261513700001 |
| 037 | _ | _ | |a PreJuSER-950 |
| 041 | _ | _ | |a eng |
| 082 | _ | _ | |a 570 |
| 084 | _ | _ | |2 WoS |a Biotechnology & Applied Microbiology |
| 084 | _ | _ | |2 WoS |a Microbiology |
| 100 | 1 | _ | |0 P:(DE-Juel1)144031 |a Marienhagen, J. |b 0 |u FZJ |
| 245 | _ | _ | |a Metabolic Function of Corynebacterium glutamicum Aminotransferases AlaT and AvtA and Impact on L-Valine Production |
| 260 | _ | _ | |a Washington, DC [u.a.] |b Soc. |c 2008 |
| 300 | _ | _ | |a 7457 - 7462 |
| 336 | 7 | _ | |0 PUB:(DE-HGF)16 |2 PUB:(DE-HGF) |a Journal Article |
| 336 | 7 | _ | |2 DataCite |a Output Types/Journal article |
| 336 | 7 | _ | |0 0 |2 EndNote |a Journal Article |
| 336 | 7 | _ | |2 BibTeX |a ARTICLE |
| 336 | 7 | _ | |2 ORCID |a JOURNAL_ARTICLE |
| 336 | 7 | _ | |2 DRIVER |a article |
| 440 | _ | 0 | |0 8561 |a Applied and Environmental Microbiology |v 74 |x 0099-2240 |y 24 |
| 500 | _ | _ | |a We thank H. Sahm and M. Bott for continuous support, K. Krumbach for strain construction, and T. Bartek and C. Rudolf (IBT 2, Forschungszentrum Julich, Germany) for assistance with the SIXFORS fermentations.This work was supported by Deutsche Bundestiftung Umwelt Projekt 13158. |
| 520 | _ | _ | |a Aminotransferases (ATs) interacting with L-alanine are the least studied bacterial ATs. Whereas AlaT converts pyruvate to L-alanine in a glutamate-dependent reaction, AvtA is able to convert pyruvate to L-alanine in an L-valine-dependent manner. We show here that the wild type of Corynebacterium glutamicum with a deletion of either of the corresponding genes does not exhibit an explicit growth deficiency. However, a double mutant was auxotrophic for L-alanine, showing that both ATs can provide L-alanine and that they are the only ATs involved. Kinetic studies with isolated enzymes demonstrate that the catalytic efficiency, k(cat)/K(m), of AlaT is higher than 1 order of magnitude in the direction of L-alanine formation (3.5 x 10(4) M(-1) s(-1)), but no preference was apparent for AvtA, suggesting that AlaT is the principal L-alanine-supplying enzyme. This is in line with the cytosolic L-alanine concentration, which is reduced in the exponential growth phase from 95 mM to 18 mM by a deletion of alaT, whereas avtA deletion decreases the L-alanine concentration only to 76 mM. The combined data show that the presence of both ATs has subtle but obvious consequences on balancing intracellular amino acid pools in the wild type. The consequences are more obvious in an L-valine production strain where a high intracellular drain-off of the L-alanine precursor pyruvate prevails. We therefore used deletion of alaT to successfully reduce the contaminating L-alanine in extracellular accumulated L-valine by 80%. |
| 536 | _ | _ | |0 G:(DE-Juel1)FUEK410 |2 G:(DE-HGF) |a Biotechnologie |c PBT |x 0 |
| 588 | _ | _ | |a Dataset connected to Web of Science, Pubmed |
| 650 | _ | 2 | |2 MeSH |a Alanine: metabolism |
| 650 | _ | 2 | |2 MeSH |a Corynebacterium glutamicum: enzymology |
| 650 | _ | 2 | |2 MeSH |a Corynebacterium glutamicum: genetics |
| 650 | _ | 2 | |2 MeSH |a Corynebacterium glutamicum: growth & development |
| 650 | _ | 2 | |2 MeSH |a Cytosol: chemistry |
| 650 | _ | 2 | |2 MeSH |a Gene Deletion |
| 650 | _ | 2 | |2 MeSH |a Kinetics |
| 650 | _ | 2 | |2 MeSH |a Pyruvic Acid: metabolism |
| 650 | _ | 2 | |2 MeSH |a Substrate Specificity |
| 650 | _ | 2 | |2 MeSH |a Transaminases: genetics |
| 650 | _ | 2 | |2 MeSH |a Transaminases: isolation & purification |
| 650 | _ | 2 | |2 MeSH |a Transaminases: metabolism |
| 650 | _ | 2 | |2 MeSH |a Valine: biosynthesis |
| 650 | _ | 7 | |0 127-17-3 |2 NLM Chemicals |a Pyruvic Acid |
| 650 | _ | 7 | |0 56-41-7 |2 NLM Chemicals |a Alanine |
| 650 | _ | 7 | |0 7004-03-7 |2 NLM Chemicals |a Valine |
| 650 | _ | 7 | |0 EC 2.6.1.- |2 NLM Chemicals |a Transaminases |
| 650 | _ | 7 | |2 WoSType |a J |
| 700 | 1 | _ | |0 P:(DE-Juel1)VDB57928 |a Eggeling, L. |b 1 |u FZJ |
| 773 | _ | _ | |0 PERI:(DE-600)1478346-0 |a 10.1128/AEM.01025-08 |g Vol. 74, p. 7457 - 7462 |p 7457 - 7462 |q 74<7457 - 7462 |t Applied and environmental microbiology |v 74 |x 0099-2240 |y 2008 |
| 856 | 7 | _ | |2 Pubmed Central |u http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2607172 |
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| 914 | 1 | _ | |y 2008 |
| 915 | _ | _ | |0 StatID:(DE-HGF)0010 |a JCR/ISI refereed |
| 920 | 1 | _ | |0 I:(DE-Juel1)VDB55 |g IBT |k IBT-1 |l Biotechnologie 1 |x 0 |z ab 31.10.10 weitergeführt als IBG-1 |
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| 980 | _ | _ | |a journal |
| 980 | _ | _ | |a I:(DE-Juel1)IBG-1-20101118 |
| 980 | _ | _ | |a UNRESTRICTED |
| 981 | _ | _ | |a I:(DE-Juel1)IBG-1-20101118 |
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