Metabolism of polychlorinated dibenzo-p-dioxins by cytochrome P450 BM-3 and its mutant
Related Articles
- Prediction of Human Drug Metabolizing Enzyme Induction. Mankowski, Dayna C.; Ekins, Sean // Current Drug Metabolism;Oct2003, Vol. 4 Issue 5, p381
New chemical entities are routinely screened in vitro and in vivo for their ability to induce cytochrome P450s (CYP), other drug-metabolizing enzymes and possibly transporters in an attempt to more accurately predict clinical parameters such as drug-drug interactions and clearance in humans....
- Phosphotransbutyrylase Expression in Bacillus megaterium. Vazquez, Gustavo J.; Pettinari, M. Julia; Méndez, Beatriz S. // Current Microbiology;May2001, Vol. 42 Issue 5, p345
The molecular analysis of a genomic region of B. megaterium revealed the presence of a gene coding for the enzyme phosphotransbutyrylase (Ptb). The enzyme activity was measured throughout the different phases of growth in B. megaterium, and its activity was found to be maximal in the late...
- Electronic and Structural Aspects of P450-Mediated Drug Metabolism. Lewis, David F. V.; Ito, Yuko; Lake, Brian G. // Drug Metabolism Letters;Apr2009, Vol. 3 Issue 2, p87
From a consideration of first principles for enzymes kinetics, we have employed theoretical methods which enable one to analyse the kinetics of cytochrome P450-mediated reactions which have been based on the known physicochemical principles underlying the majority of chemical or enzymatic...
- Role of residue 87 in substrate selectivity and regioselectivity of drug-metabolizing cytochrome P450 CYP102A1 M11. Vottero, Eduardo; Rea, Vanina; Lastdrager, Jeroen; Honing, Maarten; Vermeulen, Nico; Commandeur, Jan // Journal of Biological Inorganic Chemistry;Aug2011, Vol. 16 Issue 6, p899
CYP102A1, originating from Bacillus megaterium, is a highly active enzyme which has attracted much attention because of its potential applicability as a biocatalyst for oxidative reactions. Previously we developed drug-metabolizing mutant CYP102A1 M11 by a combination of site-directed and random...
- Cloning, expression and characterisation of CYP102A7, a self-sufficient P450 monooxygenase from Bacillus licheniformis. Dietrich, Matthias; Eiben, Sabine; Asta, Chimene; Do, Tuan; Pleiss, Juergen; Urlacher, Vlada // Applied Microbiology & Biotechnology;Jul2008, Vol. 79 Issue 6, p931
Cytochrome P450 monooxygenases of the CYP102A subfamily are single-component natural fusion proteins consisting of a heme domain and a diflavin reductase. The characterised CYP102A enzymes are fatty acid hydroxylases with turnover rates of several thousands per minute. In search of new P450s...
- Construction of a thermostable cytochrome P450 chimera derived from self-sufficient mesophilic parents. // Applied Microbiology & Biotechnology;Jul2007, Vol. 75 Issue 5, p1055
The P450 monooxygenases CYP102A1 from Bacillus megaterium and CYP102A3 from Bacillus subiilis are fusion flavocytochromes comprising of a P450 heme domain and a FAD/FMN reductase domain. This protein organization is responsible for the extraordinary catalytic activities making both...
- Covalent immobilization of cytochrome P450 BM3 (R966D/W1046S) on glutaraldehyde activated SPIONs. Bahrami, Atieh; Garnier, Alain; Larachi, Faïçal; Iliuta, Maria C. // Canadian Journal of Chemical Engineering;Oct2018, Vol. 96 Issue 10, p2227
Abstract: Selective hydroxylation of the Câ€H bond of saturated hydrocarbon chains at room temperature is the signature of an invaluable biocatalyst, cytochrome P450 BM3 from Bacillus megaterium. Despite this remarkable ability, because of the enzyme's inherent low stability and dependence...
- Kidney CYP450 Enzymes: Biological Actions Beyond Drug Metabolism. Zhao, X.; Imig, J.D. // Current Drug Metabolism;Feb2003, Vol. 4 Issue 1, p73
Arachidonic acid can be metabolized by cytochrome P450 (CYP450) enzymes to 5,6-, 8,9-, 11,12-, and 14,15-epoxyeicosatrienoic acids (EETs), their corresponding dihydroxyeicosatrienoic acids (DHETs), and 20-hydroxyeicosatetraenoic acid (20-HETE). These arachidonic acid metabolites are involved in...
- Human Cytochromes P450 Associated with the Phase 1 Metabolism of Drugs and other Xenobiotics: A Compilation of Substrates and Inhibitors of the CYP1, CYP2 and CYP3 Families. Lewis, David F.V. // Current Medicinal Chemistry;Oct2003, Vol. 10 Issue 19, p1955
This review represents a compilation of typical substrates and inhibitors for human cytochrome P450 (CYP) enzymes that are involved in drug metabolism, specifically those from the CYP1, CYP2 and CYP3 families. Relatively recent literature on substrates and inhibitors has been collected and the...
