caa a22 4500 46905347X CHVBK 20180323132836.0 cr unu---uuuuu 170328e19920601xx s 000 0 eng 10.1007/BF00123379 doi (NATIONALLICENCE)springer-10.1007/BF00123379 The sequence homologies of cytochromes P-450 and active-site geometries [Elektronische Daten] [David Lewis, Henri Moereels] Summary: The amino acid sequence alignment of 16 cytochrome P-450 proteins representative of the major families is reported. The sequence matching process has been carried out on the basis of maximum homology by residue type, retention of secondary structure and minimization of deletions/insertions except where additional loop regions exist. From the starting point of known reported sequence homology matching from the literature, a realignment on the basis of conserved residues involved in both structure and function gives rise to a self-consistent set of sequences which correlates with known mechanistic and structural data. Once fitted, these archetypal sequences form a straightforward template for the alignment of all P-450 subfamilies. Computer modelling of the active-site regions constructed from homology with the bacterial form of the enzyme (P-450CAM) evinces the correct substrate specificity. Furthermore, the construction of the macromolecular assembly of components of the cytochrome P-450 system on the microsomal endoplasmic reticular membrane is presented from the evidence of site-directed mutagenesis, analysis by molecular probes, X-ray crystallography and molecular modelling. ESCOM Science Publishers B.V, 1992 Cytochromes P-450 nationallicence Sequence homology nationallicence Active site models nationallicence Lewis David Department of Biochemistry, University of Surrey, GU2 5XH, Guildford, Surrey, U.K. aut Moereels Henri Department of Theoretical Medicinal Chemistry, Janssen Research Foundation, B-2340, Beerse, Belgium aut Journal of Computer-Aided Molecular Design Kluwer Academic Publishers 6/3(1992-06-01), 235-252 0920-654X 6:3<235 1992 6 10822 https://doi.org/10.1007/BF00123379 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF00123379 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Lewis David Department of Biochemistry, University of Surrey, GU2 5XH, Guildford, Surrey, U.K aut NATIONALLICENCE 700 1- Moereels Henri Department of Theoretical Medicinal Chemistry, Janssen Research Foundation, B-2340, Beerse, Belgium aut NATIONALLICENCE 773 0- Journal of Computer-Aided Molecular Design Kluwer Academic Publishers 6/3(1992-06-01), 235-252 0920-654X 6:3<235 1992 6 10822 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer