EC Number   |
General Information |
Reference |
|---|
    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 | more |
mutation in either ugd leads to activation of RpoE, an extracytoplasmic function sigma factor that is activated by protein misfolding and alterations in cell surface structure in other bacteria. Activation of RpoE or RpoE overexpression causes inhibition of FlhDC and hemolysin expression |
710889 |
| 1.1.1.22 | more |
Sequence and structure comparison of UDP-glucose dehydrogenase AglM from Haloferax volcanii and VNG1048G from Halobacterium salinarum, homology modelling, overview |
-, 740935 |
| 1.1.1.22 | more |
surface-exposed residues in homology models of the UDP-glucose dehydrogenase reveals the more acidic and less basic VNG1048G surface, explaining the salt-dependence of the Halobacterium salinarum enzyme. Sequence and structure comparison of UDP-glucose dehydrogenase AglM from Haloferax volcanii and VNG1048G from Halobacterium salinarum, homology modelling, overview |
-, 740935 |
| 1.1.1.22 | more |
the active site of UgdG bound to UDP-Glc and coenzyme NADH contains 6 highly conserved residues: Thr122, Glu151, Lys207, Asn211, Cys263 and Asp267. Residue Cys263 is a clear candidate for the catalytic nucleophile of the reaction. Tyr10 plays a catalytic role in the final hydrolysis of UDP-Glc |
-, 739891 |
| 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 | 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 | 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 |
