Homology modelling of various members of the CYP4A subfamily based on the CYP102 template structure is reported. 2. The binding interactions of specific substrates to the CYP4A forms from rat (CYP4A1), human (CYP4A11) and rabbit (CYP4A4) are shown to be consistent with experimental evidence regarding regioselectivity of metabolism. 3. The differences in substrate specificity between CYP4A1, CYP4A11 and CYP4A4 towards fatty acids and prostaglandins respectively are rationalized in terms of variations in active site amino residues.
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Lewis et al. (1999) studied this question.
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