PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
11695850-0	2001	Roles of cytochrome P450 3A enzymes in the 2-hydroxylation of 1,4-cineole, a monoterpene cyclic ether, by rat and human liver microsomes.	1,4-cineole	62-73	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	20-24	
11695850-3	2001	On analysis with gas chromatography/mass spectrometry, 2-exo-hydroxy-1,4-cineole was identified as a principal oxidation product of 1,4-cineole catalysed by rat and human P450 enzymes.	1,4-cineole	69-80	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	171-175	
11695850-8	2001	Finally, of 10 recombinant human P450 enzymes examined, CYP3A4 had the highest activity for 1,4-cineole 2-hydroxylation.	1,4-cineole	92-103	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	33-37