UDP-glucose 6-dehydrogenase

[1]. Sigrid Egger, et al. Structure and mechanism of human UDP-glucose 6-dehydrogenase. J Biol Chem. 2011 Jul 8;286(27):23877-87. [Content Brief]

[2]. Nathaniel R Beattie, et al. Allostery and Hysteresis Are Coupled in Human UDP-Glucose Dehydrogenase. Biochemistry. 2017 Jan 10;56(1):202-211. [Content Brief]

[3]. Nicholas D Keul, et al. The entropic force generated by intrinsically disordered segments tunes protein function. Nature. 2018 Nov;563(7732):584-588. [Content Brief]

[4]. Nathaniel R Beattie, et al. Hysteresis and Allostery in Human UDP-Glucose Dehydrogenase Require a Flexible Protein Core. Biochemistry. 2018 Dec 18;57(50):6848-6859. [Content Brief]

[5]. Nicholas C Sennett, et al. Conformational flexibility in the allosteric regulation of human UDP-α-D-glucose 6-dehydrogenase. Biochemistry. 2011 Nov 8;50(44):9651-63. [Content Brief]

[6]. Holger Hengel, et al. Loss-of-function mutations in UDP-Glucose 6-Dehydrogenase cause recessive developmental epileptic encephalopathy. Nat Commun. 2020 Jan 30;11(1):595. [Content Brief]

[7]. Nicholas C Sennett, et al. Cofactor binding triggers a molecular switch to allosterically activate human UDP-α-D-glucose 6-dehydrogenase. Biochemistry. 2012 Nov 20;51(46):9364-74. [Content Brief]

[8]. Renuka Kadirvelraj, et al. Hysteresis in human UDP-glucose dehydrogenase is due to a restrained hexameric structure that favors feedback inhibition. Biochemistry. 2014 Dec 30;53(51):8043-51. [Content Brief]

[9]. Sigrid Egger, et al. Structural and kinetic evidence that catalytic reaction of human UDP-glucose 6-dehydrogenase involves covalent thiohemiacetal and thioester enzyme intermediates. J Biol Chem. 2012 Jan 13;287(3):2119-29. [Content Brief]