Three-dimensional models of human and other mammalian microsomal P450s constructed from an alignment with P450102 (P450bm3)

Xenobiotica. 1995 Apr;25(4):333-66. doi: 10.3109/00498259509061857.


1. A novel modelling alignment for P450s, utilizing NADPH-P450 reductase for electron transfer, is proposed on the basis of analysis of their amino acid sequences. 2. Information used to facilitate the alignment process includes: the recent X-ray crystal structure of P450102 (P450bm3), site-directed mutagenesis experiments, chemical modification of specific residues, and antibody recognition studies. 3. The alignment has been used to construct a number of microsomal P450s of relevance to xenobiotic and endogenous metabolism.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Bacterial Proteins*
  • Binding Sites
  • Cytochrome P-450 Enzyme System / chemistry*
  • Humans
  • Mammals
  • Microsomes / enzymology
  • Mixed Function Oxygenases / chemistry*
  • Models, Molecular
  • Molecular Sequence Data
  • NADPH-Ferrihemoprotein Reductase
  • Protein Structure, Secondary
  • Sequence Alignment


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