Title : Identification of human UDP-glucuronosyltransferases involved in N-carbamoyl glucuronidation of lorcaserin.

Pub. Date : 2012 Apr

PMID : 22259019






3 Functional Relationships(s)
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1 With recombinant UGT enzymes, lorcaserin N-carbamoyl glucuronidation was predominantly catalyzed by three UGT2Bs (UGT2B7, UGT2B15, and UGT2B17), whereas two UGT1As (UGT1A6 and UGT1A9) played a minor role. lorcaserin UDP glucuronosyltransferase family 2 member B15 Homo sapiens
2 The rank order of catalytic efficiency of human UGT enzymes for lorcaserin N-carbamoyl glucuronidation was UGT2B15 > UGT2B7 > UGT2B17 > UGT1A9 > UGT1A6. lorcaserin UDP glucuronosyltransferase family 2 member B15 Homo sapiens
3 Inhibition of lorcaserin N-carbamoyl glucuronidation activities of UGT2B7, UGT2B15, and UGT2B17 in human liver microsomes by mefenamic acid, bisphenol A, and eugenol further substantiated the involvement of these UGT2B isoforms. lorcaserin UDP glucuronosyltransferase family 2 member B15 Homo sapiens