Enzymatic assay of d-glucuronate using uronate dehydrogenase

Authors :: Kristala L. J. Prather
Sang-Hwal Yoon
Amanda M. Lanza
Tae Seok Moon
Mary-Jane Tsang Mui Ching
Massachusetts Institute of Technology. Department of Chemical Engineering
Prather, Kristala L. Jones
Moon, Tae Seok
Yoon, Sang-Hwal
Tsang Mui Ching, Mary-Jane
Lanza, Amanda M.
Source :: Prof. Prather
Publication Year :: 2009
Publisher :: Elsevier BV, 2009.
Abstract: d-Glucuronate is a key metabolite in the process of detoxification of xenobiotics and in a recently constructed synthetic pathway to produce d-glucaric acid, a “top value-added chemical” from biomass. A simple and specific assay of d-glucuronate would be useful for studying these processes, but existing assays are either time-consuming or nonspecific. Using uronate dehydrogenase cloned from Agrobacterium tumefaciens, we developed an assay for d-glucuronate with a detection limit of 5 μM. This method was shown to be more suitable for a system with many interfering compounds than previous methods and was also applied to assays for myo-inositol oxygenase activity.<br />United States. Office of Naval Research. Young Investigator Program (N000140510656)<br />National Science Foundation (U.S.) (EEC-0540879)<br />Merck & Co., Inc. (Undergraduate Research Grant)