Title : N-glucuronidation catalyzed by UGT1A4 and UGT2B10 in human liver microsomes: Assay optimization and substrate identification.

Pub. Date : 2017 Oct 25

PMID : 28803208






5 Functional Relationships(s)
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1 N-glucuronidation catalyzed by UGT1A4 and UGT2B10 in human liver microsomes: Assay optimization and substrate identification. Nitrogen UDP glucuronosyltransferase family 2 member B10 Homo sapiens
2 However, the metabolic patterns of UGT1A4- and UGT2B10-mediated N-glucuronidation are not fully clear. Nitrogen UDP glucuronosyltransferase family 2 member B10 Homo sapiens
3 In this study, we first optimized in vitro reaction conditions for N-glucuronidation by using specific substrates (i.e., trifluoperazine for UGT1A4, cotinine and amitriptyline for UGT2B10). Nitrogen UDP glucuronosyltransferase family 2 member B10 Homo sapiens
4 In addition, UGT1A4 and UGT2B10 were primarily responsible for N-glucuronidation of many tertiary amines, including asenapine, loxapine, clozapine, chlorpromazine, dothiepin, doxepin, mirtazapine, mianserin, chlorcyclizine, cyclizine, promethazine, cyclobenzaprine, imatinib, retrorsine, strychnine and brucine. Nitrogen UDP glucuronosyltransferase family 2 member B10 Homo sapiens
5 Also, UGT1A4- and UGT2B10-mediated N-glucuronidation might play significant roles in metabolism and detoxification of tertiary amines in humans. Nitrogen UDP glucuronosyltransferase family 2 member B10 Homo sapiens