MinireviewSpecificity of human UDP-Glucuronosyltransferases and xenobiotic glucuronidation
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Steviol glucuronidation and its potential interaction with UDP-glucuronosyltransferase 2B7 substrates
2014, Food and Chemical ToxicologyThe UDP-glucuronosyltransferases: Their role in drug metabolism and detoxification
2013, International Journal of Biochemistry and Cell BiologyCitation Excerpt :Consistent with the ability of UGT to metabolise such commonly occurring functional groups, glucuronidation serves as an elimination pathway for numerous structurally diverse endogenous and exogenous compounds (Miners and Mackenzie, 1991). Indeed, this reaction is involved in the metabolism of key endogenous compounds including bilirubin, bile acids, fatty acids, steroid hormones, thyroid hormones and fat soluble vitamins (Burchell et al., 1995; Radominska-Pandya et al., 1999; Tukey and Strassburg, 2000; Miners et al., 2004; Kiang et al., 2005) and serves as an essential clearance mechanism for drugs from many therapeutic classes, including but not limited to: analgesics, non-steroidal anti-inflammatory agents, anticonvulsants, antipsychotics, antivirals and benzodiazepines (Miners and Mackenzie, 1991; Kiang et al., 2005; Sorich et al., 2006; Miners et al., 2010a). Glucuronidation occurs to some extent in all mammalian species, however significant variation in enzyme substrate selectivity and rates of glucuronidation between species is common and well documented (Miners and Mackenzie, 1991).
Mechanistic role of acyl glucuronides
2013, Drug-Induced Liver DiseaseMechanisms underlying food-drug interactions: Inhibition of intestinal metabolism and transport
2012, Pharmacology and TherapeuticsCitation Excerpt :The study was projected to be completed in January 2012; results await publication. Human glucuronosyl transferases (UGTs) facilitate elimination of endogenous substrates and xenobiotics by increasing hydrophilicity via formation of glucuronide conjugates (Burchell et al., 1995). In general, the UGTs are bound to the endoplasmic reticulum, and substrate binding sites are exposed to the lumen (Meech & Mackenzie, 1997; Radominska-Pandya et al., 1999).
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Professor B Burchell, Department of Biochemical Medicine, Ninewells Medical School, The University, Dundee, DDI 9SY.