PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
17010942-3	2006	The P450 M-2C enzyme expressed in yeast cells catalyzed p-methylhydroxylation of only tolbutamide among four substrates tested, paclitaxel as a CYP2C8 substrate, diclofenac and tolbutamide as CYP2C9 substrates and S-mephenytoin as a CYP2C19 substrate.	Tolbutamide	86-97	cytochrome P450 family 2 subfamily C member 9	Homo sapiens	192-198	
17010942-5	2006	Although all of the recombinant human CYP2C8, CYP2C9 and CYP2C19 expressed in yeast cells catalyzed tolbutamide p-methylhydroxylation, the kinetic profile of CYP2C8 was most similar to that of P450 M-2C.	Tolbutamide	100-111	cytochrome P450 family 2 subfamily C member 9	Homo sapiens	46-52	
17010942-6	2006	Tolbutamide oxidation by the marmoset liver microsomes and the recombinant P450 M-2C was inhibited most effectively by quercetin, a CYP2C8 inhibitor, followed by omeprazole, a CYP2C19 inhibitor, whereas sulfaphenazole, a CYP2C9 inhibitor, was less potent under the conditions used.	Tolbutamide	0-11	cytochrome P450 family 2 subfamily C member 9	Homo sapiens	221-227