Enzymatic assay of d-glucuronate using uronate dehydrogenase
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 exis...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | en_US |
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Elsevier
2016
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| Online Access: | http://hdl.handle.net/1721.1/101228 https://orcid.org/0000-0003-0437-3157 |
| _version_ | 1826207982030946304 |
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| author | Moon, Tae Seok Yoon, Sang-Hwal Tsang Mui Ching, Mary-Jane Lanza, Amanda M. Prather, Kristala L. Jones |
| author2 | Massachusetts Institute of Technology. Department of Chemical Engineering |
| author_facet | Massachusetts Institute of Technology. Department of Chemical Engineering Moon, Tae Seok Yoon, Sang-Hwal Tsang Mui Ching, Mary-Jane Lanza, Amanda M. Prather, Kristala L. Jones |
| author_sort | Moon, Tae Seok |
| collection | MIT |
| description | 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. |
| first_indexed | 2024-09-23T13:58:00Z |
| format | Article |
| id | mit-1721.1/101228 |
| institution | Massachusetts Institute of Technology |
| language | en_US |
| last_indexed | 2024-09-23T13:58:00Z |
| publishDate | 2016 |
| publisher | Elsevier |
| record_format | dspace |
| spelling | mit-1721.1/1012282022-09-28T17:28:24Z Enzymatic assay of d-glucuronate using uronate dehydrogenase Moon, Tae Seok Yoon, Sang-Hwal Tsang Mui Ching, Mary-Jane Lanza, Amanda M. Prather, Kristala L. Jones 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. Prather, Kristala L. Jones 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. United States. Office of Naval Research. Young Investigator Program (N000140510656) National Science Foundation (U.S.) (EEC-0540879) Merck & Co., Inc. (Undergraduate Research Grant) 2016-02-22T15:14:24Z 2016-02-22T15:14:24Z 2009-05 2009-04 Article http://purl.org/eprint/type/JournalArticle 00032697 1096-0309 http://hdl.handle.net/1721.1/101228 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. https://orcid.org/0000-0003-0437-3157 en_US http://dx.doi.org/10.1016/j.ab.2009.05.032 Analytical Biochemistry Creative Commons Attribution-NonCommercial-NoDerivs License http://creativecommons.org/licenses/by-nc-nd/4.0/ application/pdf Elsevier Prof. Prather |
| spellingShingle | Moon, Tae Seok Yoon, Sang-Hwal Tsang Mui Ching, Mary-Jane Lanza, Amanda M. Prather, Kristala L. Jones Enzymatic assay of d-glucuronate using uronate dehydrogenase |
| title | Enzymatic assay of d-glucuronate using uronate dehydrogenase |
| title_full | Enzymatic assay of d-glucuronate using uronate dehydrogenase |
| title_fullStr | Enzymatic assay of d-glucuronate using uronate dehydrogenase |
| title_full_unstemmed | Enzymatic assay of d-glucuronate using uronate dehydrogenase |
| title_short | Enzymatic assay of d-glucuronate using uronate dehydrogenase |
| title_sort | enzymatic assay of d glucuronate using uronate dehydrogenase |
| url | http://hdl.handle.net/1721.1/101228 https://orcid.org/0000-0003-0437-3157 |
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