Discovery and Biochemical Characterization of UDP-Glucose Dehydrogenase from Granulibacter bethesdensis

Title:Discovery and Biochemical Characterization of UDP-Glucose Dehydrogenase from Granulibacter bethesdensis

Volume: 22 Issue: 7

Author(s): Shuang Wei, Anna Kulinich, Xu C. Duan, Li Liu and Josef Voglmeir

Affiliation:

Keywords: Granulibacter bethesdensis, UDP-glucuronic acid, UDP-glucose dehydrogenase.

Abstract: UDP-glucose dehydrogenases (EC 1.1.1.22) are responsible for the conversion of UDP-glucose to UDP-glucuronic acid, a key precursor in the biosynthesis of glycoconjugates. Herein we report the discovery and characterization of a UDPglucose dehydrogenase (GbUGD) from Granulibacter bethesdensis, a bacterium originally isolated from the lymph nodes of patients with chronic granulomatous disease (CGD). The recombinant form of the protein was expressed in high yield and the purified enzyme showed highest activity at 37°C/pH 9.0 and was strongly inhibited by Zn²⁺ ions, sodium dodecyl sulfate (SDS) and urea. UDP-xylose, an allosteric feedback inhibitor, reduced significantly the activity of the enzyme. High activities were observed using the co-substrates UDP-glucose and NAD⁺, whereas no activity could be detected using other nucleotide sugars or NADP⁺ as potential alternative substrates. The high activity combined with the simple purification procedure used make GbUGD a valuable new alternative biocatalyst for the synthesis of UDP-glucuronic acid or the development of NAD⁺ regeneration systems.

Cite this article as:

Wei Shuang, Kulinich Anna, C. Duan Xu, Liu Li and Voglmeir Josef, Discovery and Biochemical Characterization of UDP-Glucose Dehydrogenase from Granulibacter bethesdensis, Protein & Peptide Letters 2015; 22 (7) . https://dx.doi.org/10.2174/0929866522666150526092818