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Norvaline is accumulated after a down-shift of oxygen in <Emphasis Type="Italic">Escherichia coli W3110</Emphasis> |
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| Authors: | Jaakko Soini Christina Falschlehner Christina Liedert Jörg Bernhardt Jussi Vuoristo Peter Neubauer |
| Institution: | 1.Department of Process and Environmental Engineering and Biocenter Oulu,Bioprocess Engineering Laboratory, University of Oulu,Oulu,Finland;2.Department of Microbial Physiology,Institute of Microbiology, Ernst-Moritz-Arndt-University Greifswald,Greifswald,Germany;3.Biocenter Oulu, University of Oulu,Oulu,Finland;4.Department of Bioprocess Technology,Institute of Biotechnology, Technische Universit?t Berlin,Berlin,Germany |
| Abstract: | BackgroundNorvaline is an unusual non-proteinogenic branched-chain amino acid which has been of interest especially during the early enzymological studies on regulatory mutants of the branched-chain amino acid pathway in Serratia marcescens. Only recently norvaline and other modified amino acids of the branched-chain amino acid synthesis pathway got attention again when they were found to be incorporated in minor amounts in heterologous proteins with a high leucine or methionine content. Earlier experiments have convincingly shown that norvaline and norleucine are formed from pyruvate being an alternative substrate of α-isopropylmalate synthase, however so far norvaline accumulation was not shown to occur in non-recombinant strains of E. coli. |
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