PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
19487251-7	2009	Incubation of lithocholic acid with a of human recombinant P450 enzymes revealed that all five metabolites were formed by recombinant CYP3A4.	Lithocholic Acid	14-30	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	59-63	
19487251-8	2009	Chemical inhibition studies with human liver microsomes and recombinant P450 enzymes confirmed that CYP3A4 was the predominant enzyme involved in hepatic microsomal biotransformation of lithocholic acid.	Lithocholic Acid	186-202	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	72-76	
19487251-9	2009	In summary, the results indicate that oxidation of the third carbon of the cholestane ring is the preferred position of oxidation by P450 enzymes for lithocholic acid biotransformation in humans and suggest that formation of lithocholic acid metabolites leads to enhanced hepatic detoxification and elimination.	Lithocholic Acid	150-166	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	133-137	
19487251-9	2009	In summary, the results indicate that oxidation of the third carbon of the cholestane ring is the preferred position of oxidation by P450 enzymes for lithocholic acid biotransformation in humans and suggest that formation of lithocholic acid metabolites leads to enhanced hepatic detoxification and elimination.	Lithocholic Acid	225-241	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	133-137