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for improving understanding of the biochemical basis for substrate selectivity and other aspects of enzyme activity. This in turn will inform on drug design to overcome UGT-related drug resistance. The human UDP ...
UDP -glucuronosyltransferases are the principal enzymes involved in the glucuronidation of metabolites and xenobiotics for physiological clearance in humans . Though glucuronidation is an indispensable ...
of glucuronidation activities allowed the ontogeny of UGT1A1, UGT1A4, UGT2B7, UGT2B10, and UGT2B15 to be established using multiple selective UGT substrates and matched human liver microsome samples. The postnatal ...
, all such mutases show preferential recognition of a single substrate (e.g., UDP ‐Gal). We report here the detailed structural characterization of the first bifunctional pyranose–furanose mutase, which ...
formation in hrUGT1A6 and pooled human liver microsomes were best described by the Hill equation and in hrUGT1A9 and pooled human kidney microsomes by substrate inhibition. Using inhibitory and selective UGT ...
substrates containing the central -YAVTPGP- acceptor sequence. Eleven human and one bird GalNAc-T were initially characterized revealing a range of preferences for net positive, net negative, or unique ...
. 63 : 409 – 419 . Google Scholar Crossref Search ADS PubMed WorldCat Court , M. H. ( 2005 ) Isoform- selective probe substrates for in vitro studies of human UDP -glucuronosyltransferases . Methods ...
binding affinity between selected putative substrates or ligands and UGT2B10. Finally, we performed molecular dynamics simulations using GROMACS Version 5.1.4 to confirm the potential UGT2B10 ligands ...
provide a molecular explanation for the enzyme's preference for UDP -containing donor substrates , as well as for its glucose versus mannose discrimination, and uncover the structural determinants ...
, have interesting biomedical applications. To predict functional peptide regions important for substrate binding and activity of human β4GalT7, we conducted a phylogenetic analysis of the β1,4 ...
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