The active site structure and the substrate specificity of cytochrome P-450(cam).

摘要

Cytochrome P-450;The substrate analogue 1-methyl-norcamphor indicates that reduction of complementarity between Val-295 and the camphor gem-dimethyl group is essential for all aspects of substrate specificity, including tight substrate binding, spin state regulation, regiospecificity of hydroxylation, and efficient coupling of NADH consumption with formation of hydroxylated products. The substrate analogue norcamphor, which lacks all of the methyl groups present on camphor, is processed by P-450;Utilizing norcamphor as a substrate skeleton, the substrate specificity of P-450