Multiple Functions of Thioredoxins
Open Access
- 1 August 1978
- journal article
- research article
- Published by Walter de Gruyter GmbH in Zeitschrift für Naturforschung C
- Vol. 33 (7-8), 517-520
- https://doi.org/10.1515/znc-1978-7-811
Abstract
Reduced thioredoxins from microbial and plant cells, both of cytoplasmic or chloroplast origin, are interchangeable in stimulating such diverse enzyme activities as ribonucleoside diphosphate reductase (Escherichia coli), 3''-phosphoadenosine 5''-phosphosulfate sulfotransferase (Synechococcus) and fructose-1,6-bis-phosphatase (spinach) in vitro. Reduced thioredoxins may be unspecific, multifunctional cellular proteins while in contrast the oxidized forms require specific enzymes for their reduction.Keywords
This publication has 8 references indexed in Scilit:
- A factor-dependent sulfotransferase specific for 3?-phosphoadenosine-5?-phosphosulfate (PAPS) in the Cyanobacterium Synechococcus 6301Planta, 1978
- A thioredoxin from green algaeBiochemical and Biophysical Research Communications, 1977
- NADPH activation of deoxycytidylate kinase in rat liver extract: Involvement of an endogenous disulfide reductase systemBiochemical and Biophysical Research Communications, 1977
- Adenosine-5?-phosphosulfate (APS) as sulfate donor for assimilatory sulfate reduction in Rhodospirillum rubrumArchiv für Mikrobiologie, 1977
- Enzymic Reduction of Disulfide Bonds by ThioredoxinEuropean Journal of Biochemistry, 1976
- Ribonucleotide reductase activity in green algaeBiochemical and Biophysical Research Communications, 1976
- Sulfate-reducing pathway in Escherichia coli involving bound intermediatesJournal of Bacteriology, 1976
- ENZYMATIC SYNTHESIS OF DEOXYRIBONUCLEOTIDES .6. CYTIDINE DIPHOSPHATE REDUCTASE SYSTEM FROM NOVIKOFF HEPATOMA1964