Approach to detect substrates suitable to measure the coumarin 7-hydroxylase (Cyp 2a-5)-structure-activity relationships.
Besides coumarin, which up to now has remained the most selective substrate for the coumarin 7-hydroxylase (Coh), 7-ethoxycoumarin, quinoline, 4-methylcoumarin, 7-ethoxy-4-methylcoumarin, 7-ethoxy-4-ethylcoumarin, and psoralen are suitable for this enzyme. The quantification of the suitability of a substrate to selectively measure the coumarin 7-hydroxylase is achieved by a graphic method. Requirements for serving as a substrate of the Coh are bicyclic ring systems with an electron rich moiety.
Tegtmeier
M
M
Department of Pharmaceutical Technology, Schaper & Brümmer, Salzgitter, Germany.
Legrum
W
W
D000818:Animals; D001189:Aryl Hydrocarbon Hydroxylases; D003374:Coumarins / Q000737:chemistry / Q000378:metabolism*; D065637:Cytochrome P-450 CYP2A6; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D066298:In Vitro Techniques; D008297:Male; D051379:Mice; D008862:Microsomes, Liver / Q000201:enzymology; D006899:Mixed Function Oxygenases / Q000378:metabolism*; D013329:Structure-Activity Relationship
D003374:Coumarins; D003577:Cytochrome P-450 Enzyme System; D006899:Mixed Function Oxygenases; D001189:Aryl Hydrocarbon Hydroxylases; D065637:Cytochrome P-450 CYP2A6