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Profiling Thiol Redox Proteome Using Isotope Tagging Mass Spectrometry
Published on: March 24, 2012
The activities of the two thioredoxins from Streptomyces aureofaciens are not interchangeable
Tatiana Horecká1, Dusan Perecko, Eva Kutejová
1Department of Biochemistry, Faculty of Natural Sciences, Comenius University, Mlynská Dolina Ch-1, 842 15 Bratislava, Slovak Republic. horeka@fns.uniba.sk
Abstract:
The physico-chemical features of the NADPH-thioredoxin reductase (TRR) and two thioredoxins from Streptomyces aureofaciens (A14) are reported. The activity of pure S. aureofaciens thioredoxin reductase decreased drastically in the presence of NADPH or NADH while NADP(+), NAD(+), as well as S. aureofaciens thioredoxin-1 (TR1) activated the enzyme activity significantly. TR1 fully protected the enzyme from inactivation and also promoted its complete reactivation. S. aureofaciens thioredoxin-2 (TR2) did not protect thioredoxin reductase from NADPH inactivation. The results indicate that although the two thioredoxins from S. aureofaciens have similar biochemical properties, their essential oxidoreductase activities are not interchangeable.
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