Evidence for an Additional Disulfide Reduction Pathway in Escherichia coli(GENETICS, MOLECULAR BIOLOGY, AND GENE ENGINEERING)
スポンサーリンク
概要
- 論文の詳細を見る
An Escherichia coli cell-free protein synthesis cell extract has been created that lacks all known cytoplasmic disulfide reduction pathways but still retains significant reductase activity. Oxidized glutathione was partially stabilized by deleting the gene for glutathione reductase. To avoid previously reported AhpC mutations, thioredoxin reductase was only removed after extract preparation. The trxB gene was extended to encode a hemagglutinin tag so that TrxB could be removed by affinity adsorption. However, significant glutathione reductase activity remained. The unknown glutathione reductase pathway is disabled by iodoacetamide, is inhibited by NADH, and appears to use NADPH as an electron source.
- 公益社団法人日本生物工学会の論文
- 2007-04-25
著者
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Knapp Kurtis
Department Of Chemical Engineering Stanford University
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Swartz James
Department of BioEngineering, Stanford University
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Swartz James
Department Of Bioengineering Stanford University