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UDP-glucose dehydrogenase has a role in hyaluronan synthesis
Data indicate that the A136M substitution in UDP-glucose dehydrogenase (hUGDH) stabilizes the hexamer.
study has identified several new proteins like RHOC, DLG5, UGDH, TMOD3 in addition to known chemoresistance associated proteins in non-small cell lung carcinoma.
UGDH protein level in osteoarthritis cartilage was much lower than in control cartilage.
UGDH displays hysteresis because of a slow isomerization from an inactive state (E*) to an active state (E). We show that the structure of E* constrains UGDH in a conformation that favors feedback inhibition at physiological pH.
Kinetic analysis of wild-type UGDH and hexamer T325A showed that upon increasing enzyme concentration, which favors the hexameric species, activity was decreased and exhibited cooperativity. Cooperative kinetics was not observed in obligate dimer T325D.
Mammalian UGDH displays hysteresis (observed as a lag in progress curves), indicating that the enzyme undergoes a slow transition from an inactive to an active state. Human UGDH is sensitive to product inhibition during the lag.
both missense mutations significantly reducing the ability of UGDH to provide precursors for cardiac cushion formation, which is essential to subsequent valve formation.
Structural and kinetic evidence that catalytic reaction of human UDP-glucose 6-dehydrogenase involves covalent thiohemiacetal and thioester enzyme intermediates.
An alternate crystal structure of human UGDH (hUGDH) in complex with UDP-glucose at 2.8 A resolution, is reported.
A structurally detailed model of UDP-alpha-D-glucose 6-dehydrogenase (UGDH) demonstrates hinge-bending motion that represents allosteric feedback inhibition and substrate-product exchange during the catalytic cycle.
high UGDH levels may underlie susceptibility of the orbit to localized overproduction of hyaluronan in Graves disease.
Structure and mechanism of human UDP-glucose 6-dehydrogenase.
An atypical allosteric mechanism in human UDP-alpha-D-glucose 6-dehydrogenase (UGDH) based on an easily acquired and identifiable structural attribute: packing defects in the protein core.
UGDH can regulate cell motility through the production of glycosaminoglycans
Results support the UGDH content in prostatic acini as a novel candidate biomarker that may complement the development of a multi-biomarker panel for detecting PC within the tumor adjacent field on a histologically normal biopsy specimen.
UGDH core promoter has a role in up- and down-regulation of UGDH after TGF-beta stimulation and in hypoxic conditions
role of Cys-276 as a catalytic residue; Lys-279 is likely to have a role in positioning active site residues and in maintaining the hexameric quaternary structure
Gly-13 plays an important role for efficient binding of NAD(+) to human UDP-glucose dehydrogenase
C276 plays an important role for efficient binding of UDP-glucose to hUGDH
Our results indicate that the region from nucleotide position -486 to -632 relative to the start of the small transcript contains positive regulatory elements that contribute to gene expression.
The protein encoded by this gene converts UDP-glucose to UDP-glucuronate and thereby participates in the biosynthesis of glycosaminoglycans such as hyaluronan, chondroitin sulfate, and heparan sulfate. These glycosylated compounds are common components of the extracellular matrix and likely play roles in signal transduction, cell migration, and cancer growth and metastasis. The expression of this gene is up-regulated by transforming growth factor beta and down-regulated by hypoxia. Alternative splicing results in multiple transcript variants.
, UDP-glucose 6-dehydrogenase
, UDP-glucose dehydrogenase
, distal W5.4 group XIII
, UDP-glucose dehydrogenase b
, UDP-glucose dehydrogenase a
, UDP-Glc dehydrogenase
, uridine diphospho-glucose dehydrogenase
, UDP-glucose dehydrogeanse