Potemkin V A, Grishina M A, Bartashevich E V, Zrakova T Iu, Pogrebnoĭ A A
Biofizika. 2005 May-Jun;50(3):418-22.
The interactions between the substrates of the 2E1 isoform of the human cytochrome P450 and receptor were simulated. It was found that the CP4 isoform of the cytochrome of the bacterial cell is highly homologous to the 2E1 isoform of the human cytochrome P450. The orientation of the substrates of the 2E1 isoform in the CP4 isoform of the bacterial cell cytochrome was performed. A cavity in the receptor was found that is responsible for the binding of the substrate. Amino acid residues Phe87, Pro89, Val119, Thr185, Leu244, Leu245, Leu246, Val247, Gly248, Gly249, Thr252, Val295, Asp297, Cys357, Ile395, and Val396, the heme, and water molecules are involved in the formation of the cavity. The mode of the interactions of the substrate molecule with cytochrome was analyzed. Active sites of the receptor, and a part of the substrate molecule responsible for the binding to cytochrome were found. Equations for the dependence of the Michaelis constant on the structural parameters of complexes of substrates with cytochrome were derived.
