ArticleJournal of biotechnology2013
Reductive amination by recombinant Escherichia coli: whole cell biotransformation of 2-keto-3-methylvalerate to L-isoleucine.
Article in Journal of biotechnology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed, 11 citations in OpenAlex.
- The branched-chain amino acid-related isoleucic acid: recent research advances.Plant biology (Stuttgart, Germany) · 2025Review
- In vivo plug-and-play: a modular multi-enzyme single-cell catalyst for the asymmetric amination of ketoacids and ketones.Microbial cell factories · 2017Article
- Whole-cell biocatalysts by design.Microbial cell factories · 2017Review
- Role of L-alanine for redox self-sufficient amination of alcohols.Microbial cell factories · 2015Article
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3 authors at 1 institution in 1 country.
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Abstract
A whole cell biotransformation system for reductive amination has been studied in recombinant Escherichia coli cells. Reductive amination of 2-keto-3-methylvalerate to L-isoleucine by a two-enzyme-cascade was achieved by overproduction of endogenous L-alanine dependent transaminase AvtA and heterologous L-alanine dehydrogenase from Bacillus subtilis in recombinant E. coli. Up to 100 mM L-isoleucine were produced from 100 mM 2-keto-3-methylvalerate and 100 mM ammonium sulfate. Regeneration of NADH as cofactor in the whole cell system was driven by glucose catabolism. The effects of defined gene deletions in the central carbon metabolism on biotransformation were tested. Strains lacking the NuoG subunit of NADH:ubiquinone oxidoreductase (complex I) or aceA encoding the glyoxylate cycle enzyme isocitrate lyase exhibited increased biotransformation rates.
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