Nitrosamines are a class of environmental carcinogens that requires metabolic activation to exert their carcinogenic potential. Enzymes of the cytochrome P450 family are responsible for this activation. Minor differences in nitrosamine structure lead to activation by different cytochrome P450s. Cytochrome P450s are found in all organisms from bacteria to mammals, and as of now, over 500 cDNA sequences have been identified. Most P450s are membrane bound and no three-dimensional structures are available. Only the soluble, bacterial P450s have been crystallized, and extensive work is currently being done to model various membrane bound P450s from the crystal structure of these bacterial P450s.
Linda von Weymarn, Graduate Student Researcher
These researchers are interested in using molecular modeling to determine the amino acids in the active site of cytochrome P450 2A enzymes important in substrate specificity. The P450 2A enzymes are very good at metabolizing nitrosamines, and understanding more about how very small differences in amino acid sequence can change the substrate specificity can help these researchers to understand more about nitrosamine carcinogenesis.
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