Enzymatic assay of d-glucuronate using uronate dehydrogenase
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Prather_Enzymatic assay.pdf
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Author(s)
Moon, Tae Seok
Yoon, Sang-Hwal
Tsang Mui Ching, Mary-Jane
Lanza, Amanda M.
Prather, Kristala L. Jones
Date Issued
May 2009
Journal
Analytical Biochemistry
Publisher
Elsevier
Citation
Moon, Tae Seok, Sang-Hwal Yoon, Mary-Jane Tsang Mui Ching, Amanda M. Lanza, and Kristala L. Jones Prather. “Enzymatic Assay of d-Glucuronate Using Uronate Dehydrogenase.” Analytical Biochemistry 392, no. 2 (September 2009): 183–185.
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Author's final manuscript
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.
MIT Department
Massachusetts Institute of Technology. Department of Chemical Engineering
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Creative Commons Attribution-NonCommercial-NoDerivs License
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DOI of Published Version
https://doi.org/10.1016/j.ab.2009.05.032
