A close family resemblance: the importance of structure in understanding cytochromes P450.
Cytochromes P450 comprise a very large superfamily of hemeproteins which generally monooxygenate hydrophobic compounds. P450s appear to have a common conserved structural core, yet are variable in regions involved in substrate recognition and binding, and in redox-partner binding. These differences can be identified by an analysis in which structural alignments and homology models are used to compare the various classes and families of P450s.
Peterson
J A
JA
Department of Biochemistry The University of Texas Southwestern Medical Center, Dallas 5323 Harry Hines Blvd, Dallas, TX 75235-9038, USA. Bill@P450BM3.swmed.edu
Graham
S E
SE
D000818:Animals; D020134:Catalytic Domain; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry*; D006801:Humans; D007091:Image Processing, Computer-Assisted; D008958:Models, Molecular; D010084:Oxidation-Reduction; D011487:Protein Conformation
D003577:Cytochrome P-450 Enzyme System