ArticleJournal of industrial microbiology & biotechnology2016
Characterization of aspartate kinase and homoserine dehydrogenase from Corynebacterium glutamicum IWJ001 and systematic investigation of L-isoleucine biosynthesis.
Article in Journal of industrial microbiology & biotechnology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 40 citations in OpenAlex.
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- Metabolic engineering strategies of Corynebacterium glutamicum for sulfur-containing amino acid production: current progress and future directions.World journal of microbiology & biotechnology · 2026Review
- Regulatory mechanism of ferrous ion in enhancing the biosynthesis of L-homoserine, L-threonine, and L-isoleucine in Corynebacterium glutamicum.World journal of microbiology & biotechnology · 2025Article
- Engineering a Lactobacillus Lysine Riboswitch to Dynamically Control Metabolic Pathways for Lysine Production inMicroorganisms · 2024Article
- Strategies to Enhance l-Isoleucine Synthesis by Modifying the Threonine Metabolism Pathway inACS omega · 2024Article
- Insight into de-regulation of amino acid feedback inhibition: a focus on structure analysis method.Microbial cell factories · 2023Review
- Engineering allosteric inhibition of homoserine dehydrogenase by semi-rational saturation mutagenesis screening.Frontiers in bioengineering and biotechnology · 2023Article
- High-Level Production of Isoleucine and Fusel Alcohol by Expression of the Feedback Inhibition-Insensitive Threonine Deaminase inApplied and environmental microbiology · 2022Article
- Metabolic engineering of Corynebacterium glutamicum for producing branched chain amino acids.Microbial cell factories · 2021Review
- New Therapeutic Candidates for the Treatment of Malassezia pachydermatis -Associated Infections.Scientific reports · 2020Article
- Increasing L-threonine production in Escherichia coli by overexpressing the gene cluster phaCAB.Journal of industrial microbiology & biotechnology · 2019Article
- Enzymatic characterization and molecular mechanism of a novel aspartokinase mutant M372I/T379W fromRSC advances · 2019Article
- Construction of Novel Aspartokinase Mutant A380I and Its Characterization by Molecular Dynamics Simulation.Molecules (Basel, Switzerland) · 2018Article
- Bicistronic expression strategy for high-level expression of recombinant proteins inEngineering in life sciences · 2017Article
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4 authors at 2 institutions in 1 country.
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Abstract
Previously we have characterized a threonine dehydratase mutant TD(F383V) (encoded by ilvA1) and an acetohydroxy acid synthase mutant AHAS(P176S, D426E, L575W) (encoded by ilvBN1) in Corynebacterium glutamicum IWJ001, one of the best L-isoleucine producing strains. Here, we further characterized an aspartate kinase mutant AK(A279T) (encoded by lysC1) and a homoserine dehydrogenase mutant HD(G378S) (encoded by hom1) in IWJ001, and analyzed the consequences of all these mutant enzymes on amino acids production in the wild type background. In vitro enzyme tests confirmed that AK(A279T) is completely resistant to feed-back inhibition by L-threonine and L-lysine, and that HD(G378S) is partially resistant to L-threonine with the half maximal inhibitory concentration between 12 and 14 mM. In C. glutamicum ATCC13869, expressing lysC1 alone led to exclusive L-lysine accumulation, co-expressing hom1 and thrB1 with lysC1 shifted partial carbon flux from L-lysine (decreased by 50.1 %) to L-threonine (4.85 g/L) with minor L-isoleucine and no L-homoserine accumulation, further co-expressing ilvA1 completely depleted L-threonine and strongly shifted carbon flux from L-lysine (decreased by 83.0 %) to L-isoleucine (3.53 g/L). The results demonstrated the strongly feed-back resistant TD(F383V) might be the main driving force for L-isoleucine over-synthesis in this case, and the partially feed-back resistant HD(G378S) might prevent the accumulation of toxic intermediates. Information exploited from such mutation-bred production strain would be useful for metabolic engineering.
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