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Integration of Sugar Metabolism and Proteoglycan Synthesis by UDP-glucose Dehydrogenase.
Journal of Histochemistry & Cytochemistry ( IF 1.9 ) Pub Date : 2020-08-04 , DOI: 10.1369/0022155420947500
Brenna M Zimmer 1 , Joseph J Barycki 1 , Melanie A Simpson 1
Affiliation  

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:



中文翻译:

UDP-葡萄糖脱氢酶整合糖代谢和蛋白多糖合成。

蛋白多糖和糖胺聚糖合成的调节在整个发育过程中至关重要,并且在伤口愈合和免疫系统等方面维持正常的成人功能。越来越清楚的是,这些过程也受到严格的代谢控制,碳水化合物和氨基酸代谢物前体的可用性在控制蛋白聚糖和糖胺聚糖周转中发挥作用。尿苷二磷酸 (UDP)-葡萄糖脱氢酶 (UGDH) 产生 UDP-葡萄糖醛酸,这是在多个层面受到严格控制的新糖胺聚糖合成的必要前体。在这里,我们回顾了调节 UGDH 表达的细胞机制,讨论了酶的结构特征,

更新日期:2020-08-04
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