PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8848008-0	1995	Mechanism of cytochrome P450 2D6-catalyzed sparteine metabolism in humans.	Sparteine	43-52	cytochrome P450 2D6	Homo sapiens	13-32	
8848008-1	1995	Two different reaction mechanisms for the formation of the two human enamine-structured sparteine metabolites by cytochrome P450 2D6 have been discussed in the literature.	Sparteine	88-97	cytochrome P450 2D6	Homo sapiens	113-132	
8848008-7	1995	However, results of competitive and noncompetitive experiments revealed the presence of a nondissociative enzymatic mechanism for the formation of the two sparteine metabolites, i.e., the sparteine molecule that is bound to the substrate binding site of cytochrome P450 2D6 performs orientational changes without dissociating from the activated enzyme/substrate complex before the product-determining first irreversible reaction step.	Sparteine	155-164	cytochrome P450 2D6	Homo sapiens	254-273	
8848008-7	1995	However, results of competitive and noncompetitive experiments revealed the presence of a nondissociative enzymatic mechanism for the formation of the two sparteine metabolites, i.e., the sparteine molecule that is bound to the substrate binding site of cytochrome P450 2D6 performs orientational changes without dissociating from the activated enzyme/substrate complex before the product-determining first irreversible reaction step.	Sparteine	188-197	cytochrome P450 2D6	Homo sapiens	254-273	
8363993-4	1993	In man, tropisetron metabolism is linked to the cytochrome P-450 2D6 isoenzyme system, which determines the polymorphism of debrisoquine/sparteine metabolism.	Sparteine	137-146	cytochrome P450 2D6	Homo sapiens	48-68