Title : Characterization of UDP-glucuronosyltransferase 2A1 (UGT2A1) variants and their potential role in tobacco carcinogenesis.

Pub. Date : 2011 Feb

PMID : 21164388






4 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 A significant (P<0.05) decrease (approximately 25%) in glucuronidation activity (Vmax/KM) was observed against all polycyclic aromatic hydrocarbons substrates for the UGT2A1(75Lys308Gly) variant compared with homogenates from wildtype UGT2A1(75Lys308Gly); no activity was observed for cell homogenates overexpressing the UGT2A1 variant for all substrates tested. 75lys308gly UDP glucuronosyltransferase 2 family, polypeptide A1 Mus musculus
2 A significant (P<0.05) decrease (approximately 25%) in glucuronidation activity (Vmax/KM) was observed against all polycyclic aromatic hydrocarbons substrates for the UGT2A1(75Lys308Gly) variant compared with homogenates from wildtype UGT2A1(75Lys308Gly); no activity was observed for cell homogenates overexpressing the UGT2A1 variant for all substrates tested. 75lys308gly UDP glucuronosyltransferase 2 family, polypeptide A1 Mus musculus
3 A significant (P<0.05) decrease (approximately 25%) in glucuronidation activity (Vmax/KM) was observed against all polycyclic aromatic hydrocarbons substrates for the UGT2A1(75Lys308Gly) variant compared with homogenates from wildtype UGT2A1(75Lys308Gly); no activity was observed for cell homogenates overexpressing the UGT2A1 variant for all substrates tested. 75lys308gly UDP glucuronosyltransferase 2 family, polypeptide A1 Mus musculus
4 A significant (P<0.05) decrease (approximately 25%) in glucuronidation activity (Vmax/KM) was observed against all polycyclic aromatic hydrocarbons substrates for the UGT2A1(75Lys308Gly) variant compared with homogenates from wildtype UGT2A1(75Lys308Gly); no activity was observed for cell homogenates overexpressing the UGT2A1 variant for all substrates tested. 75lys308gly UDP glucuronosyltransferase 2 family, polypeptide A1 Mus musculus