The CYP2 family: models, mutants and interactions

Xenobiotica. 1998 Jul;28(7):617-61. doi: 10.1080/004982598239236.


1. The construction of three-dimensional models of mammalian cytochromes P450 from the CYP2 family is reported based on protein sequence alignment with CYP102, a bacterial P450 of known crystal structure. 2. The homology models of CYP2 family enzymes appear to show self-consistency with the currently accumulated information from site-directed mutagenesis and chemical modification of amino acid residues known to affect redox partner interactions. 3. The generation of these models from the recently reported crystal structure of substrate-bound CYP102 enables the exploration of likely active site contacts with specific substrates of CYP2 family isozymes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins*
  • Binding Sites
  • Cytochrome P-450 Enzyme System / chemistry*
  • Cytochrome P-450 Enzyme System / genetics
  • Cytochrome P-450 Enzyme System / metabolism
  • Female
  • Humans
  • Male
  • Mixed Function Oxygenases / chemistry
  • Models, Molecular
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • NADPH-Ferrihemoprotein Reductase
  • Polypropylenes / chemistry
  • Protein Conformation
  • Sequence Alignment


  • Bacterial Proteins
  • Polypropylenes
  • Cytochrome P-450 Enzyme System
  • Mixed Function Oxygenases
  • NADPH-Ferrihemoprotein Reductase
  • flavocytochrome P450 BM3 monoxygenases