Abstract
UDP-glucose dehydrogenase catalyzes the incorporation of tritium into UDP-glucose (UDPG) in the presence of UDP-α-D-gluco-hexodialdose (UDP-Glc-6-CHO) and [B- 3H]-NADH. The 3H is located exclusively at C-6 of the glucose moiety of UDPG and at least 79% of it is in the pro-R position. It is concluded that UDPG dehydrogenase catalyzes the abstraction of the pro-R hydrogen at C-6 of the glucose moiety of the substrate as the first step in the conversion of UDPG to UDP-glucuronic acid. The apparent lack of complete stereospecificity has been shown to result from a hitherto undetected reversible redox reaction prior to the release of UDP-glucuronic acid by the enzyme.
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 callMore From: Biochemical and Biophysical Research Communications
Disclaimer: 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.
