PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
12416991-4	2002	We report here determination of the kinetic mechanism for 5alpha-DHP reduction catalyzed by human 3alpha-HSD type III by using steady-state kinetics studies and assessment of the ability of fluoxetine and various other small molecules to activate 3alpha-HSD type III catalyzed allopregnanolone formation.	5-alpha-Dihydroprogesterone	58-68	aldo-keto reductase family 1 member C4	Homo sapiens	98-108	
16611167-4	2006	This enzyme inactivates 17beta-estradiol and exhibits a strong oxidative 3alpha-HSD activity to convert 5alpha-androstanediol and allopregnanolone into 5alpha-dihydrotestosterone (5alpha-DHT) and 5alpha-dihydroprogesterone, respectively, in living cells.	5-alpha-Dihydroprogesterone	196-222	aldo-keto reductase family 1 member C4	Homo sapiens	73-83	
12416991-4	2002	We report here determination of the kinetic mechanism for 5alpha-DHP reduction catalyzed by human 3alpha-HSD type III by using steady-state kinetics studies and assessment of the ability of fluoxetine and various other small molecules to activate 3alpha-HSD type III catalyzed allopregnanolone formation.	5-alpha-Dihydroprogesterone	58-68	aldo-keto reductase family 1 member C4	Homo sapiens	247-257	
12416991-7	2002	Two-substrate kinetic analysis and dead-end inhibition studies for 5alpha-DHP reduction and allopregnanolone oxidation indicated that 3alpha-HSD type III utilized a ternary complex (sequential) kinetic mechanism, with nicotinamide adenine dinucleotide cofactor binding before steroid substrate and leaving after steroid product.	5-alpha-Dihydroprogesterone	67-77	aldo-keto reductase family 1 member C4	Homo sapiens	134-144