PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 2870898-4 1986 It is likely, therefore, that the mechanism of action of these compounds is the same as that for allylisopropylacetamide (AIA) and related monosubstituted olefins, which are converted by cytochrome P-450 to chemically reactive species which bind covalently to the prosthetic heme moiety of the cytochrome and thereby destroy the enzyme. Alkenes 155-162 cytochrome P450, family 2, subfamily g, polypeptide 1 Rattus norvegicus 187-203 2870898-6 1986 These findings, together with data from related metabolic studies on AIA, support the view that the efficiency of the initial double bond oxidation reaction determines the extent of cytochrome P-450 destruction during the metabolism of terminal olefins, rather than any subsequent step. Alkenes 245-252 cytochrome P450, family 2, subfamily g, polypeptide 1 Rattus norvegicus 182-198 6652073-0 1983 Olefin oxidation by cytochrome P-450: evidence for group migration in catalytic intermediates formed with vinylidene chloride and trans-1-phenyl-1-butene. Alkenes 0-6 cytochrome P450, family 2, subfamily g, polypeptide 1 Rattus norvegicus 20-36 6833252-2 1983 Hepatic microsomal cytochrome P-450 from phenobarbital-pretreated rats is inactivated during the metabolism of linear olefins (ethylene, propene, and octene) and acetylenes (acetylene, propyne, and octyne). Alkenes 118-125 cytochrome P450, family 2, subfamily g, polypeptide 1 Rattus norvegicus 19-35 8735469-0 1996 CYP enzymes catalyze the formation of a terminal olefin from 2-ethylhexanoic acid in rat and human liver. Alkenes 49-55 cytochrome P450, family 2, subfamily g, polypeptide 1 Rattus norvegicus 0-3 3101178-4 1987 Desaturation of a nonactivated alkyl substituent represents a novel metabolic function of cytochrome P-450 and probably proceeds via the conversion of substrate to a transient free radical intermediate, which partitions between recombination (alcohol formation) and elimination (olefin production) pathways. Alkenes 279-285 cytochrome P450, family 2, subfamily g, polypeptide 1 Rattus norvegicus 90-106 8735469-13 1996 The data indicate that (1) several CYP families (CYP2A, CYP2B, CYP2D and CYP3A) could be responsible for the hepatic metabolism of 2-EHA, (2) the same metabolites were formed in rats and man and (3) an unsaturated terminal olefin, 2-ethyl-5-hexenoic acid is formed in the liver. Alkenes 223-229 cytochrome P450, family 2, subfamily g, polypeptide 1 Rattus norvegicus 35-38