ArticleApplied and environmental microbiology2008
Metabolic function of Corynebacterium glutamicum aminotransferases AlaT and AvtA and impact on L-valine production.
Article in Applied and environmental microbiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 61 citations in OpenAlex.
- Article
- Metabolic capabilities are highly conserved among human nasal-associatedbioRxiv : the preprint server for biology · 2024Article
- Quorum sensing-mediated dynamic regulation of 4-hydroxyisoleucine biosynthesis in Corynebacterium glutamicum.World journal of microbiology & biotechnology · 2023Article
- Metabolic engineering of Corynebacterium glutamicum for producing branched chain amino acids.Microbial cell factories · 2021Review
- Enhanced production of γ-amino acid 3-amino-4-hydroxybenzoic acid by recombinant Corynebacterium glutamicum under oxygen limitation.Microbial cell factories · 2021Article
- Effect of fed-batch and chemostat cultivation processes ofBioengineered · 2021Article
- Enhancing β-alanine production from glucose in genetically modified Corynebacterium glutamicum by metabolic pathway engineering.Applied microbiology and biotechnology · 2021Article
- Engineering of microbial cells for L-valine production: challenges and opportunities.Microbial cell factories · 2021Review
- Rational modification of the carbon metabolism of Corynebacterium glutamicum to enhance L-leucine production.Journal of industrial microbiology & biotechnology · 2020Article
- Improvement of l-Leucine Production inInternational journal of molecular sciences · 2019Article
- Physiological Response ofFrontiers in microbiology · 2018Article
- A method for simultaneous gene overexpression and inactivation in the Corynebacterium glutamicum genome.Journal of industrial microbiology & biotechnology · 2016Article
- A novel aceE mutation leading to a better growth profile and a higher L-serine production in a high-yield L-serine-producing Corynebacterium glutamicum strain.Journal of industrial microbiology & biotechnology · 2016Article
- Anaerobic growth of Corynebacterium glutamicum via mixed-acid fermentation.Applied and environmental microbiology · 2015Article
- Metabolic engineering of Escherichia coli for the synthesis of the plant polyphenol pinosylvin.Applied and environmental microbiology · 2015Article
- Engineering of Corynebacterium glutamicum for high-yield L-valine production under oxygen deprivation conditions.Applied and environmental microbiology · 2013Article
- Horizontal gene transfer is a significant driver of gene innovation in dinoflagellates.Genome biology and evolution · 2013Article
- Improvement of the redox balance increases L-valine production by Corynebacterium glutamicum under oxygen deprivation conditions.Applied and environmental microbiology · 2012Article
- Metabolic engineering of Corynebacterium glutamicum for 2-ketoisovalerate production.Applied and environmental microbiology · 2010Article
- The comprehensive microbial resource.Nucleic acids research · 2010Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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%.
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