Abstract
A mutant of Escherichia coli defective in thioredoxin reductase has been isolated and partially characterized. This mutant has no detectable thioredoxin reductase activity in vitro and yet it exhibits no in vivo defect in reduction of ribonucleotides. Evidence is presented that indicates that, in cells permeabilized via ether treatment, ribonucleoside diphosphate reduction can utilize glutathione as an alternate reducing system.
MeSH Terms
Escherichia coli/enzymology,metabolism
Glutathione/metabolism
Methionine/metabolism
Methionine Sulfoximine/metabolism
Mutation
NADH, NADPH Oxidoreductases/biosynthesis
NADP/metabolism
Ribonucleoside Diphosphate Reductase/metabolism
Temperature
Thioredoxin-Disulfide Reductase/biosynthesis,metabolism
Thioredoxins/metabolism
Uracil Nucleotides/metabolism
Chemicals
Uracil Nucleotides
Methionine Sulfoximine
Thioredoxins
NADP
Methionine
Ribonucleoside Diphosphate Reductase
NADH, NADPH Oxidoreductases
Thioredoxin-Disulfide Reductase
Glutathione
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Fuchs J
References (22)
22 references, click to expand
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