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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 (show RHOC Proteins), DLG5 (show DLG5 Proteins), UGDH, TMOD3 (show TMOD3 Proteins) 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 (show STMN1 Proteins) 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 (show STMN1 Proteins).
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.
Six proteins were regulated at both basal and inducible levels exhibiting the largest dynamic range of Nrf2 (show NFE2L2 Proteins) regulation: cytochrome CYP2A5, GSTM3 (show GSTM3 Proteins), GSTM1 (show GSTM1 Proteins), ENTPD5 (show ENTPD5 Proteins),UDPGDH, and EPHX1 (show EPHX1 Proteins).
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