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.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
