PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
6814537-5	1982	The coincidence of the values of the rate constants and activation energy (56 +/- 5 kJ/mol) for the fast phase of NADPH-dependent reduction of cytochrome P-450 with values of catalytic constants and activation energy for demethylation of tertiary amines suggests that the first electron transfer process from NADPH-cytochrome P-450 reductase to cytochrome P-450 may be the rate-limiting step.	Amines	247-253	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	143-159	
8082573-2	1994	Inherent substrate factors, such as basicity, electronic state, lipophilicity, and conformation control binding of the diverse classes of amines to cytochrome P-450.	Amines	138-144	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	148-164	
8082573-6	1994	Certain amines appear to regulate O2 association with cytochrome P-450 and stabilize the various oxy species formed.	Amines	8-14	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	54-70	
8082573-7	1994	Considering the selective prerequisites for oxidative attack by cytochrome P-450 at vulnerable nitrogen centers, many cytotoxic amines belonging to the category of relatively rigid, planar molecules undergo N-oxidative activation by the cytochrome P-450IA subfamily, while more bulky amines with flexible conformation are N-oxygenated preferentially by phenobarbital-inducible cytochromes P-450.	Amines	128-134	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	64-80	
8082573-7	1994	Considering the selective prerequisites for oxidative attack by cytochrome P-450 at vulnerable nitrogen centers, many cytotoxic amines belonging to the category of relatively rigid, planar molecules undergo N-oxidative activation by the cytochrome P-450IA subfamily, while more bulky amines with flexible conformation are N-oxygenated preferentially by phenobarbital-inducible cytochromes P-450.	Amines	284-290	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	64-80	
2322954-6	1990	Similarities are found between alcohol inhibition and the binding of alkyl amines to cytochrome P-450, suggesting that alcohols may bind to the amine binding site.	Amines	75-80	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	85-101	
6341732-1	1983	The metabolism of tertiary amines is mediated primarily by cytochrome P-450 and MFAO, leading to alpha-C oxidation and N-oxidation, respectively.	Amines	27-33	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	59-84	
6341732-3	1983	The proposed oxidation of tertiary amines to iminium ions by cytochrome P-450 may explain the isolation of various intramolecular and cyanide-trapped metabolites.	Amines	35-41	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	61-77	
8847710-0	1995	Some aspects of the role of cytochrome P-450 isozymes in the N-oxidative transformation of secondary and tertiary amine compounds.	Amines	114-119	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	28-44	
1930182-3	1991	In cases where iminium-enamine coupling is sterically prevented, the iminium in equilibrium with enamine species can be studied independently and are found to be more potent metabolism-dependent inactivators of cytochrome P-450 than are the corresponding parent amines.	Amines	262-268	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	211-227	
2600595-1	1989	Initial reaction rates of oxygen consumption and hydrogen peroxide formation in a cytochrome P-450 catalyzed reaction are practically independent of the nature of tertiary amines that were used as substrates.	Amines	172-178	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	82-98	
23870-0	1978	[Kinetics of N-dealkylation of amines with participation of microsomal cytochrome P-450].	Amines	31-37	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	71-87	
7296714-0	1981	Oxidative dealkylation of tertiary amines by iron(III) porphyrin-iodosoxylene system as a model of cytochrome P-450.	Amines	35-41	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	99-115	
647071-0	1978	[Kinetic and spectral parameters of the amines oxidative N-dealkylation with participation of the liver microsomal cytochrome P-450.	Amines	40-46	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	115-131	
647071-2	1978	Kinetics of demethylation of a number of amines involving hepatic microsomal cytochrome P-450 and organic hydroperoxides (tret-butyl- and cumylhydroperoxide) have been investigated.	Amines	41-47	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	77-93	
23870-1	1978	Within the temperature range of 20-37 degrees C the kinetics of the demethylation reactions of a variety of amines with participation of hepatic microsomal cytochrome P-450, NADPH and O2 has been studied.	Amines	108-114	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	156-172	
23870-6	1978	The nature of the limiting step of the enzymatic amine demethylation involving cytochrome P-450 of hepatic microsomes is discussed.	Amines	49-54	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	79-95	
21504003-6	2011	The suggested reaction pathways included N-methylation leading to iminium formation in primary and/or secondary amines preceded by cytochrome P450 (CYP)-mediated reactions.	Amines	112-118	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	131-146	
4149397-0	1973	The role of cytochrome P-450 in the N-oxidation of individual amines.	Amines	62-68	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	12-28	
26598170-0	2011	Do Two Different Reaction Mechanisms Contribute to the Hydroxylation of Primary Amines by Cytochrome P450?	Amines	80-86	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	90-105	
26598170-1	2011	Three possible mechanisms have been suggested for the hydroxylation of primary and secondary amines by the cytochrome P450 enzyme family.	Amines	93-99	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	107-122	
21504003-6	2011	The suggested reaction pathways included N-methylation leading to iminium formation in primary and/or secondary amines preceded by cytochrome P450 (CYP)-mediated reactions.	Amines	112-118	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	148-151	
16922637-4	2005	These interactions may occur not only in the liver, but also in the brain, and may change the activity of CYP towards the metabolism of drugs, sex steroids, neurosteroids and amine neurotransmitters.	Amines	175-180	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	106-109	
12564927-1	2003	Human cytochrome P450 (P450) 2D6 is an important enzyme involved in the metabolism of drugs, many of which are amines or contain other basic nitrogen atoms.	Amines	111-117	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	6-32