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000000950 0247_ $$2DOI$$a10.1128/AEM.01025-08
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000000950 084__ $$2WoS$$aBiotechnology & Applied Microbiology
000000950 084__ $$2WoS$$aMicrobiology
000000950 1001_ $$0P:(DE-Juel1)144031$$aMarienhagen, J.$$b0$$uFZJ
000000950 245__ $$aMetabolic Function of Corynebacterium glutamicum Aminotransferases AlaT and AvtA and Impact on L-Valine Production
000000950 260__ $$aWashington, DC [u.a.]$$bSoc.$$c2008
000000950 300__ $$a7457 - 7462
000000950 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000000950 3367_ $$2BibTeX$$aARTICLE
000000950 3367_ $$2ORCID$$aJOURNAL_ARTICLE
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000000950 440_0 $$08561$$aApplied and Environmental Microbiology$$v74$$x0099-2240$$y24
000000950 500__ $$aWe 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.
000000950 520__ $$aAminotransferases (ATs) interacting with L-alanine are the least studied bacterial ATs. Whereas AlaT converts pyruvate to L-alanine in a glutamate-dependent reaction, AvtA is able to convert pyruvate to L-alanine in an L-valine-dependent manner. We show here that the wild type of Corynebacterium glutamicum with a deletion of either of the corresponding genes does not exhibit an explicit growth deficiency. However, a double mutant was auxotrophic for L-alanine, showing that both ATs can provide L-alanine and that they are the only ATs involved. Kinetic studies with isolated enzymes demonstrate that the catalytic efficiency, k(cat)/K(m), of AlaT is higher than 1 order of magnitude in the direction of L-alanine formation (3.5 x 10(4) M(-1) s(-1)), but no preference was apparent for AvtA, suggesting that AlaT is the principal L-alanine-supplying enzyme. This is in line with the cytosolic L-alanine concentration, which is reduced in the exponential growth phase from 95 mM to 18 mM by a deletion of alaT, whereas avtA deletion decreases the L-alanine concentration only to 76 mM. The combined data show that the presence of both ATs has subtle but obvious consequences on balancing intracellular amino acid pools in the wild type. The consequences are more obvious in an L-valine production strain where a high intracellular drain-off of the L-alanine precursor pyruvate prevails. We therefore used deletion of alaT to successfully reduce the contaminating L-alanine in extracellular accumulated L-valine by 80%.
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000000950 650_2 $$2MeSH$$aAlanine: metabolism
000000950 650_2 $$2MeSH$$aCorynebacterium glutamicum: enzymology
000000950 650_2 $$2MeSH$$aCorynebacterium glutamicum: genetics
000000950 650_2 $$2MeSH$$aCorynebacterium glutamicum: growth & development
000000950 650_2 $$2MeSH$$aCytosol: chemistry
000000950 650_2 $$2MeSH$$aGene Deletion
000000950 650_2 $$2MeSH$$aKinetics
000000950 650_2 $$2MeSH$$aPyruvic Acid: metabolism
000000950 650_2 $$2MeSH$$aSubstrate Specificity
000000950 650_2 $$2MeSH$$aTransaminases: genetics
000000950 650_2 $$2MeSH$$aTransaminases: isolation & purification
000000950 650_2 $$2MeSH$$aTransaminases: metabolism
000000950 650_2 $$2MeSH$$aValine: biosynthesis
000000950 650_7 $$0127-17-3$$2NLM Chemicals$$aPyruvic Acid
000000950 650_7 $$056-41-7$$2NLM Chemicals$$aAlanine
000000950 650_7 $$07004-03-7$$2NLM Chemicals$$aValine
000000950 650_7 $$0EC 2.6.1.-$$2NLM Chemicals$$aTransaminases
000000950 650_7 $$2WoSType$$aJ
000000950 7001_ $$0P:(DE-Juel1)VDB57928$$aEggeling, L.$$b1$$uFZJ
000000950 773__ $$0PERI:(DE-600)1478346-0$$a10.1128/AEM.01025-08$$gVol. 74, p. 7457 - 7462$$p7457 - 7462$$q74<7457 - 7462$$tApplied and environmental microbiology$$v74$$x0099-2240$$y2008
000000950 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC2607172
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