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pro vyhledávání: '"Bisesh Shrestha"'
Autor:
Brandall L. Ingle, Bisesh Shrestha, Margarita C. De Jesus, Heather M. Conrad-Webb, Mary E. Anderson, Thomas R. Cundari
Publikováno v:
Computational and Structural Biotechnology Journal, Vol 17, Iss , Pp 31-38 (2019)
The second step in the biosynthesis of the cellular antioxidant glutathione (GSH) is catalyzed by human glutathione synthetase (hGS), a negatively cooperative homodimer. Patients with mutations in hGS have been reported to exhibit a range of symptoms
Externí odkaz:
https://doaj.org/article/9039b4877b0644caa9d1381c92526c36
Autor:
Bisesh Shrestha, Heather Conrad-Webb, Thomas R. Cundari, Mary E. Anderson, Margarita De Jesus, Brandall L. Ingle
Publikováno v:
Computational and Structural Biotechnology Journal, Vol 17, Iss, Pp 31-38 (2019)
Computational and Structural Biotechnology Journal
Computational and Structural Biotechnology Journal
The second step in the biosynthesis of the cellular antioxidant glutathione (GSH) is catalyzed by human glutathione synthetase (hGS), a negatively cooperative homodimer. Patients with mutations in hGS have been reported to exhibit a range of symptoms
The role of strong electrostatic interactions at the dimer interface of human glutathione synthetase
Autor:
Kerri D. Slavens, Thomas R. Cundari, Margarita De Jesus, Bisesh Shrestha, Mary E. Anderson, Brandall L. Ingle, Khaldoon A. Barakat
Publikováno v:
The protein journal. 33(5)
The obligate homodimer human glutathione synthetase (hGS) provides an ideal system for exploring the role of protein–protein interactions in the structural stability, activity and allostery of enzymes. The two active sites of hGS, which are 40 A ap
Publikováno v:
The FASEB Journal. 28
Human glutathione synthetase (hGS) catalyzes the second step in the synthesis of the key antioxidant glutathione. The homodimeric enzyme displays negative cooperativity towards the ɣ-glutamylcysteine substrate. The presented work probes the signific