Identification of a coenzyme A – glutathione disulfide (DSI), a modified coenzyme A disulfide (DSII), and a NADPH-dependent coenzyme A – glutathione disulfide reductase in E. coli
- 1 October 1977
- journal article
- research article
- Published by Canadian Science Publishing in Canadian Journal of Biochemistry
- Vol. 55 (10), 1019-1027
- https://doi.org/10.1139/o77-152
Abstract
The nucleotides DSI [CoA-glutathione disulfide] and DSII [modified CoA disulfide] induced during a slowdown in growth of Escherichia coli were characterized using chemical and biochemical analysis and by enzymic and alkaline fragmentation. DSI consists of CoA and glutathione joined by a disulfide linkage. DSI could be isolated containing Fe(III) with an A250:260 ratio of 1.05 or not containing Fe with an A250:260 of 0.87. DSII (isolated in 10% the yield of DSI) is a CoA disulfide dimer that also contains 2 molecules of glutamic acid. DSI was a substrate for NADPH-dependent CoAS-SG reductase (EC 1.6.4.6) which was present in crude extracts of E. coli. The specific activity of CoAS-SG reductase increased during growth from early log phase into stationary phase and during a shift from aerobic to anaerobic growth.This publication has 11 references indexed in Scilit:
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