Cytochrome P450 2A6 (human) Yeast Reductase
Stability : 2 years
Cytochrome P450 2A6 is principally involved in the break down of nicotine in the bloodstream as it circulates through the liver. Oxidation of nicotine by this P450 leads to detoxication, but the enzyme also activates tobacco-specific procarcinogens to mutagenic products (1-4).P450 2A6 structures were solved with the alternative substrate, coumarin, and with the inhibitor, methoxsalen, bound in the active site of the enzyme, adjacent to its iron containing heme group. The compact, hydrophobic active site contains one hydrogen bond donor, Asn297, which orients coumarin for regioselective oxidation (Fig. 1a). Methoxsalen also interacts with Asn297 and effectively fills the active site cavity without significantly perturbing the structure (Fig. 1b). Precise knowledge of these molecular details and interactions is critical for the rational design of new inhibitors. This structural information is being used in on-going high resolution experiments at SSRL to probe the active site of P450 2A6 with additional small molecule compounds. An effective inhibitor of P450 2A6 could be used to diminish smoking and tobacco-related cancers by reducing dependence on nicotine and by blocking formation of carcinogens.
Storage : -80°C
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