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Evidence for an additional disulfide reduction pathway in Escherichia coli

Paper ID Volume ID Publish Year Pages File Format Full-Text
22285 43265 2007 4 PDF Available
Title
Evidence for an additional disulfide reduction pathway in Escherichia coli
Abstract

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.

Keywords
glutathione; disulfide reductase; Escherichia coli
First Page Preview
Evidence for an additional disulfide reduction pathway in Escherichia coli
Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Bioscience and Bioengineering - Volume 103, Issue 4, April 2007, Pages 373–376
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering