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Title 

Generation of human metabolites of 7-ethoxycoumarin by bacterial cytochrome P450 BM3

Authors 

D H KimK H KimK H LiuHeung Chae JungJae Gu PanC H Yun

Publisher 

American Society for Pharmacology and Experimental Therapeutics (ASPET)

Issue Date 

2008

Citation 

Drug Metabolism and Disposition, vol. 36, no. 11, pp. 2166-2170

Keywords 

7 ethoxycoumarincytochrome P450 BM3humannonhuman

Abstract 

Recently, wild-type and mutant forms of bacterial cytochrome P450 BM3 (CYP102A1) have been found to metabolize various drugs through reactions similar to those catalyzed by human cytochromes P450 (P450s). Therefore, it has been suggested that CYP102A1 may be used to produce large quantities of the metabolites of human P450-catalyzed reactions. In this report, we show that the oxidation of 7-ethoxycoumarin, a typical human P450 substrate, is catalyzed by both wild-type and mutant forms of CYP102A1. Two major products were produced as a result of O-deethylation and 3-hydroxylation reactions. These results demonstrate that CYP102A1 mutants catalyze the same reactions as human P450s. High noncompetitive intermolecular kinetic deuterium isotope effects were observed for 7-ethoxycoumarin O-deethylation in the CYP102A1 system. These results suggest that there is a common mechanism for the oxidation reactions catalyzed by both the bacterial CYP102A1 and human P450 enzymes. Copyright ⓒ 2008 by The American Society for Pharmacology and Experimental Therapeutics.

ISSN 

0090-9556

Link 

http://dx.doi.org/10.1124/dmd.108.021220

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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