2020 review
Integration of Sugar Metabolism and Proteoglycan Synthesis by UDP-glucose Dehydrogenase
[Review of ]. JOURNAL OF HISTOCHEMISTRY & CYTOCHEMISTRY, 69(1), 13–23.
author keywords: developmental disorders; extracellular matrix; glucuronidation; glycosaminoglycan; hyaluronan; nucleotide sugars; post-translational modifications; proteoglycan; UDP-glucuronate
MeSH headings : Allosteric Regulation; Animals; Biosynthetic Pathways; Humans; Models, Molecular; Neoplasms / metabolism; Protein Processing, Post-Translational; Proteoglycans / metabolism; Sugars / metabolism; Uridine Diphosphate Glucose Dehydrogenase / chemistry; Uridine Diphosphate Glucose Dehydrogenase / metabolism
TL;DR:
The cellular mechanisms that regulate UG DH expression are reviewed, the structural features of the enzyme are discussed, and the structures are used to provide a context for recent studies that link post-translational modifications and allosteric modulators of UGDH to its function in downstream pathways.
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open access via journals.sagepub.com (publisher PDF)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
Source: Web Of Science
Added: August 24, 2020
Regulation of proteoglycan and glycosaminoglycan synthesis is critical throughout development, and to maintain normal adult functions in wound healing and the immune system, among others. It has become increasingly clear that these processes are also under tight metabolic control and that availability of carbohydrate and amino acid metabolite precursors has a role in the control of proteoglycan and glycosaminoglycan turnover. The enzyme uridine diphosphate (UDP)-glucose dehydrogenase (UGDH) produces UDP-glucuronate, an essential precursor for new glycosaminoglycan synthesis that is tightly controlled at multiple levels. Here, we review the cellular mechanisms that regulate UGDH expression, discuss the structural features of the enzyme, and use the structures to provide a context for recent studies that link post-translational modifications and allosteric modulators of UGDH to its function in downstream pathways: