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pro vyhledávání: '"Nicholas C. Sennett"'
Autor:
Nicholas C. Sennett, Nicholas D. Keul, Gregory S. Custer, Richard M. Walsh, Zachary A. Wood, Andrew M. Sidlo, Renuka Kadirvelraj
Publikováno v:
Biochemistry. 53:8043-8051
Human UDP-α-d-glucose-6-dehydrogenase (hUGDH) displays hysteresis because of a slow isomerization from an inactive state (E*) to an active state (E). Here we show that the structure of E* constrains hUGDH in a conformation that favors feedback inhib
Autor:
Robert S. Phillips, Gregory S. Custer, Renuka Kadirvelraj, Zachary A. Wood, Nicholas C. Sennett
Publikováno v:
Biochemistry. 52:1456-1465
Human UDP-α-d-glucose 6-dehydrogenase (hUGDH) forms a hexamer that catalyzes the NAD(+)-dependent oxidation of UDP-α-d-glucose (UDG) to produce UDP-α-d-glucuronic acid. Mammalian UGDH displays hysteresis (observed as a lag in progress curves), ind
Publikováno v:
Biochemistry. 50:9651-9663
UDP-α-D-xylose (UDX) acts as a feedback inhibitor of human UDP-α-D-glucose 6-dehydrogenase (hUGDH) by activating an unusual allosteric switch, the Thr131 loop. UDX binding induces the Thr131 loop to translate ~5 Å through the protein core, changin
Publikováno v:
Biochemistry. 51(46)
Human UDP-α-D-glucose dehydrogenase (hUGDH) catalyzes the NAD(+)-dependent oxidation of UDP-α-D-glucose (UDG) to produce UDP-α-D-glucuronic acid. The oligomeric structure of hUGDH is dynamic and can form two distinct hexameric complexes in solutio
Autor:
Stephen E. Weitzel, Samuel J. Polizzi, Renuka Kadirvelraj, Nicholas C. Sennett, Zachary A. Wood
Publikováno v:
Biochemistry. 50(25)
Allosteric feedback inhibition is the mechanism by which metabolic end products regulate their own biosynthesis by binding to an upstream enzyme. Despite its importance in controlling metabolism, there are relatively few allosteric mechanisms underst
Autor:
Nicholas C. Sennett, Renuka Kadirvelraj, Zachary A. Wood, Gregory S. Custer, Robert S. Phillips
Publikováno v:
Biochemistry. 54:629-629