- Abstract:
-
Biosynthesis of the glycosaminoglycan precursor UDP-α-D-glucuronic acid occurs through a 2-fold oxidation of UDP-α-D-glucose that is catalysed by UGDH (UDP-α-D-glucose 6-dehydrogenase). Structure-function relationships for UGDH and proposals for the enzymatic reaction mechanism are reviewed in the present paper, and structure-based sequence comparison is used for subclassification of UGDH family members. The eukaryotic group of enzymes (UGDH-II) utilize an extended C-terminal domain for the f...
Expand abstract - Publication status:
- Published
- Peer review status:
- Peer reviewed
- Publisher copy:
- 10.1042/BST0381378
-
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- Publisher:
- Portland Press Publisher's website
- Journal:
- Biochemical Society transactions Journal website
- Volume:
- 38
- Issue:
- 5
- Pages:
- 1378-85
- Publication date:
- 2010-01-01
- DOI:
- EISSN:
-
1470-8752
- ISSN:
-
0300-5127
- URN:
-
uuid:0feec673-8b5f-4961-80ad-982d15edd333
- Local pid:
- SGC:20863317
- Copyright holder:
- Austrian Science Fund FWF and Egger et al.
- Copyright date:
- 2010
- Notes:
- Copyright © The Authors Journal compilation © 2010 Biochemical Society.
Journal article
UDP-glucose dehydrogenase: structure and function of a potential drug target
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