EC Number |
General Information |
Reference |
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1.1.1.22 | more |
dysregulated expression of UGDH can promote the development of androgen independent tumor cell growth by increasing available levels of intracellular androgen. UGDH activity is the rate limiting factor in solubilization of excess androgen from prostate tumor cells, overview |
711665 |
1.1.1.22 | physiological function |
enzyme AglM can be functionally replaced by another UDP-glucose dehydrogenase, VNG1048G, in vivo |
-, 740935 |
1.1.1.22 | metabolism |
enzyme displays a NAD+-dependent SN2 mechanism. The first oxidation involves the nucleophilic addition of the essential Cys residue. The acceptor of C6-OH of UDP-glucose is an ordered H2O molecule. The second NADH is released after hydrolysis of the thioester intermediate |
761284 |
1.1.1.22 | physiological function |
enzyme displays hysteresis, observed as a lag in progress curves, and is sensitive to product inhibition during the lag. The inhibition results in a systematic decrease in steady-state velocity and makes the lag appear to have a second-order dependence on enzyme concentration.The lag is in fact due to a substrate and cofactor-induced isomerization of the enzyme. The cofactor binds to the enzyme:substrate complex with negative cooperativity, suggesting that the isomerization may be related to the formation of an asymmetric enzyme complex. The hysteresis may be the consequence of a functional adaptation, by slowing the response of the enzyme to sudden increases in the flux of substrate, the other biochemical pathways that use this important metabolite will have a competitive edge |
724370 |
1.1.1.22 | physiological function |
enzyme is involved in capsular polysaccharide biosynthesis |
-, 760612 |
1.1.1.22 | more |
enzyme Ugd from Escherichia coli K-12 can functionally replace enzyme Ugd from Escherichia coli serotype K30 in biosynthesis of K30 capsular polysaccharide |
740710 |
1.1.1.22 | physiological function |
enzyme VNG1048G can functionally replace another UDP-glucose dehydrogenase AglM in vivo. In Halobacterium salinarum, where glycoproteins are modified by an N-linked glycan of similar composition, gene VNG1048G is not only found within a cluster of N-glycosylation-related genes reminiscent of the genomic region surrounding its Haloferax volcanii counterpart AglM but can also functionally replace gene aglM in a Haloferax volcanii strain lacking the gene |
-, 740935 |
1.1.1.22 | physiological function |
epirubicin accumulation increases and apoptosis decreases during UGDH knockdown. Hyaluronan-coated matrix increases and a positive modulation of autophagy is detected. Higher levels of UGDH are correlated with worse prognosis in triple-negative breast cancer patients that receive chemotherapy. High expression of UGDH is found in tumoral tissue from HER2--patients. UGDH knockdown contributes to epirubicin resistance |
760676 |
1.1.1.22 | malfunction |
Haloferax volcanii cells deleted of HVO_1531 present a modified S-layer |
-, 728319 |
1.1.1.22 | physiological function |
in breast cancer cells, depletion of the hyaluronic acid precursor UDP-glucuronic acid is sufficient to inhibit several mesenchymal-like properties including cellular invasion and colony formation in vitro, as well as tumor growth and metastasis in vivo. Depletion of UDP-glucuronic acid alters the expression of PPAR-gamma target genes and increases PPAR-gamma DNA binding activity |
762065 |