title: Active site model of cytochrome P-450 LM2.
abstract: Based on (i) a detailed analysis of the physicochemical properties of selected benzphetamine derived substrates and (ii) the identification of Tyr-380 as active site residue trans to thiolate theoretical studies (computer aided molecular design) revealed a model of the substrate binding site of cytochrome P-450 LM2. The results indicate that substrates with a butterfly-like bulky conformation exhibit the highest intrinsic activity. Those substrates which preferably exist in an extended conformation are sterically hindered to intensively interact with the binding site which is demonstrated by computer graphics.
authors.affiliation: Central Institute of Molecular Biology, Academy of Sciences of GDR, Berlin.
authors.forename: W
authors.initials: W
authors.lastname: Schwarze
authors.forename: J
authors.initials: J
authors.lastname: Jaeger
authors.forename: G R
authors.initials: GR
authors.lastname: Jänig
authors.forename: K
authors.initials: K
authors.lastname: Ruckpaul
mesh_terms: D001589:Benzphetamine; D001665:Binding Sites; D055598:Chemical Phenomena; D002621:Chemistry; D003196:Computer Graphics; D003577:Cytochrome P-450 Enzyme System; D008958:Models, Molecular; D008968:Molecular Conformation; D011487:Protein Conformation; D013379:Substrate Specificity; D014443:Tyrosine
chemical_list: D001589:Benzphetamine; D014443:Tyrosine; D003577:Cytochrome P-450 Enzyme System