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- W40890157 abstract "UDP Glucuronosyltransferase isozyme super family metabolizes a vast class of lipophilic endobiotics and xenobiotics, to water soluble excretable glucuronides. The homolog of these genes and their protein products are present in all organisms. The most important biologically active 1A family of proteins uses 4 common exons preceding with a unique amino-terminal encoding exon. These 4 common exons are thought to be responsible for encoding the binding donor substrate, UDP-glucuronic acid (UDPGA), whereas the unique exon specifies acceptor substrate by a UGT. A method to predict the binding site for the donor substrate (UDPGA) for one of the isozymes, UGT1A10, was carried out by homology modeling with UDP-galactose 4-Epimerase (PDB ID 1XEL) and its binding sites for UDP-glucose. The derived sites in UGT1A10 were verified by site- directed mutagenesis. Competitive inhibition studies with different UDP sugars and UDP sugar analog revealed that these binding sites are UDP-specific. Scatchard analysis revealed that this enzyme has bi-phasic binding kinetics with a high and a low affinity binding site. The results represent the first tentative UDPGA binding sites in a UGT molecule." @default.
- W40890157 created "2016-06-24" @default.
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- W40890157 date "2007-01-01" @default.
- W40890157 modified "2023-09-26" @default.
- W40890157 title "Determination of possible UDP binding sites in UGT1A10" @default.
- W40890157 doi "https://doi.org/10.1096/fasebj.21.6.a1002-b" @default.
- W40890157 hasPublicationYear "2007" @default.
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