PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 8654206-0 1995 Identification of the human liver cytochrome P450 enzymes involved in the metabolism of zileuton (ABT-077) and its N-dehydroxylated metabolite, Abbott-66193. zileuton 88-96 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 34-49 8654206-0 1995 Identification of the human liver cytochrome P450 enzymes involved in the metabolism of zileuton (ABT-077) and its N-dehydroxylated metabolite, Abbott-66193. 2,2'-azino-di-(3-ethylbenzothiazoline)-6-sulfonic acid 98-101 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 34-49 8654206-1 1995 In vitro studies were conducted to identify the hepatic cytochrome P450 (CYP) forms involved in the oxidative metabolism of [14C]zileuton (ABT-077) and its N-dehydroxylated metabolite, [14C]Abbott-66193, by human liver microsomes. Carbon-14 125-128 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 56-71 8654206-1 1995 In vitro studies were conducted to identify the hepatic cytochrome P450 (CYP) forms involved in the oxidative metabolism of [14C]zileuton (ABT-077) and its N-dehydroxylated metabolite, [14C]Abbott-66193, by human liver microsomes. Carbon-14 125-128 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 73-76 8654206-1 1995 In vitro studies were conducted to identify the hepatic cytochrome P450 (CYP) forms involved in the oxidative metabolism of [14C]zileuton (ABT-077) and its N-dehydroxylated metabolite, [14C]Abbott-66193, by human liver microsomes. zileuton 129-137 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 56-71 8654206-1 1995 In vitro studies were conducted to identify the hepatic cytochrome P450 (CYP) forms involved in the oxidative metabolism of [14C]zileuton (ABT-077) and its N-dehydroxylated metabolite, [14C]Abbott-66193, by human liver microsomes. zileuton 129-137 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 73-76 8654206-1 1995 In vitro studies were conducted to identify the hepatic cytochrome P450 (CYP) forms involved in the oxidative metabolism of [14C]zileuton (ABT-077) and its N-dehydroxylated metabolite, [14C]Abbott-66193, by human liver microsomes. 2,2'-azino-di-(3-ethylbenzothiazoline)-6-sulfonic acid 139-142 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 56-71 8654206-1 1995 In vitro studies were conducted to identify the hepatic cytochrome P450 (CYP) forms involved in the oxidative metabolism of [14C]zileuton (ABT-077) and its N-dehydroxylated metabolite, [14C]Abbott-66193, by human liver microsomes. 2,2'-azino-di-(3-ethylbenzothiazoline)-6-sulfonic acid 139-142 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 73-76 8654206-1 1995 In vitro studies were conducted to identify the hepatic cytochrome P450 (CYP) forms involved in the oxidative metabolism of [14C]zileuton (ABT-077) and its N-dehydroxylated metabolite, [14C]Abbott-66193, by human liver microsomes. Carbon-14 186-189 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 56-71 8654206-1 1995 In vitro studies were conducted to identify the hepatic cytochrome P450 (CYP) forms involved in the oxidative metabolism of [14C]zileuton (ABT-077) and its N-dehydroxylated metabolite, [14C]Abbott-66193, by human liver microsomes. Carbon-14 186-189 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 73-76 8654206-3 1995 Results suggested that whereas the metabolism of zileuton and Abbott-66193 were mediated by the same CYP forms, the CYP forms responsible for hydroxylation (CYP1A2 and CYP2C9/10) were distinct from those involved in sulfoxidation (CYP3A > CYP2C9/10). zileuton 49-57 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 101-104 8654206-3 1995 Results suggested that whereas the metabolism of zileuton and Abbott-66193 were mediated by the same CYP forms, the CYP forms responsible for hydroxylation (CYP1A2 and CYP2C9/10) were distinct from those involved in sulfoxidation (CYP3A > CYP2C9/10). zileuton 49-57 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 231-236 8654206-3 1995 Results suggested that whereas the metabolism of zileuton and Abbott-66193 were mediated by the same CYP forms, the CYP forms responsible for hydroxylation (CYP1A2 and CYP2C9/10) were distinct from those involved in sulfoxidation (CYP3A > CYP2C9/10). zileuton 49-57 cytochrome P450 family 2 subfamily C member 9 Homo sapiens 242-248 8654206-4 1995 Sulfoxidation (zileuton, Km = 0.82 +/- 0.40 mM, Vmax = 39.1 +/- 21.8 pmol/min/mg; Abbott-66193, Km = 0.23 +/- 0.06 mM, Vmax = 507 +/- 215 pmol/min/mg; mean +/- SD, N=3) was highly correlated with the CYP3A-specific erythromycin N-demethylase activity (r=0794-0.856; p<0.01, N=11) in human microsomes and was inhibited (32-67%) by ketoconazole and troleandomycin. sulfoxidation 0-13 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 200-205 8654206-5 1995 In addition, purified recombinant human CYP3A4/rat NADPH-P450 reductase fusion protein catalyzed only the sulfoxidation of zileuton and Abbott-66193; no hydroxylated metabolites were detected. zileuton 123-131 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 40-46 8654206-6 1995 On the other hand, hydroxylation of the two compounds (zileuton, Km = 0.34 +/- 0.25 mM, Vmax = 17.8 +/- 5.58 pmol/min/mg; Abbott-66193,Km = 0.39 +/- 0.14 mM, Vmax = 1061 +/- 220 pmol/min/mg) was significantly correlated with 7-ethoxyresorufin O-deethylase (CYP1A2; r=0.652-0.762; p<0.01, N=11) and tolbutamide methyl hydroxylase (CYP2C9/10; r=0.863-0.935; p<0.01, N=10) activity in human liver microsome, and was inhibited (26-51%) by well-known CYP1A2 inhibitors (furafylline and alpha-naphthoflavone). zileuton 55-63 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 257-263 8654206-6 1995 On the other hand, hydroxylation of the two compounds (zileuton, Km = 0.34 +/- 0.25 mM, Vmax = 17.8 +/- 5.58 pmol/min/mg; Abbott-66193,Km = 0.39 +/- 0.14 mM, Vmax = 1061 +/- 220 pmol/min/mg) was significantly correlated with 7-ethoxyresorufin O-deethylase (CYP1A2; r=0.652-0.762; p<0.01, N=11) and tolbutamide methyl hydroxylase (CYP2C9/10; r=0.863-0.935; p<0.01, N=10) activity in human liver microsome, and was inhibited (26-51%) by well-known CYP1A2 inhibitors (furafylline and alpha-naphthoflavone). zileuton 55-63 cytochrome P450 family 2 subfamily C member 9 Homo sapiens 333-339 8654206-6 1995 On the other hand, hydroxylation of the two compounds (zileuton, Km = 0.34 +/- 0.25 mM, Vmax = 17.8 +/- 5.58 pmol/min/mg; Abbott-66193,Km = 0.39 +/- 0.14 mM, Vmax = 1061 +/- 220 pmol/min/mg) was significantly correlated with 7-ethoxyresorufin O-deethylase (CYP1A2; r=0.652-0.762; p<0.01, N=11) and tolbutamide methyl hydroxylase (CYP2C9/10; r=0.863-0.935; p<0.01, N=10) activity in human liver microsome, and was inhibited (26-51%) by well-known CYP1A2 inhibitors (furafylline and alpha-naphthoflavone). zileuton 55-63 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 452-458 8654206-7 1995 Furthermore, microsomes from human B-lymphoblastoid cells expressing CYP1A2 catalyzed only the hydroxylation of zileuton and Abbott-66193; sulfoxide were not formed. zileuton 112-120 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 69-75 8654206-7 1995 Furthermore, microsomes from human B-lymphoblastoid cells expressing CYP1A2 catalyzed only the hydroxylation of zileuton and Abbott-66193; sulfoxide were not formed. sulfoxide 139-148 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 69-75 8654206-8 1995 Abbott-66193 was a better substrate for CYP2C9/10, when compared with zileuton: 1) the effect of sulfaphenazole on hydroxylation in human liver microsomes was more pronounced for Abbott-66193 than zileuton (56% vs. 9% inhibition); and 2) the rate of Abbott-66193 hydroxylation by purified CYP2C9 was almost 30-fold greater than that of zilueton. Sulfaphenazole 97-111 cytochrome P450 family 2 subfamily C member 9 Homo sapiens 40-46