Active site model of cytochrome P-450 LM2

https://doi.org/10.1016/0006-291X(88)90727-9Get rights and content

Abstract

Based on (i) a detailed analysis of the physicochemical properties of selected benzphetamine derived substrates /1/ and (ii) the identification of Tyr-380 as active site residue trans to thiolate /2,3/ 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.

References (17)

  • D.R. Petzold et al.

    Biochim. Biophys. Acta

    (1985)
  • G.R. Jänig et al.

    FEBS Letters

    (1983)
  • W. Schwarze et al.

    Chem. Biol. Interactions

    (1985)
  • J. Singh et al.

    FEBS Letters

    (1985)
  • H. Yoshioka et al.

    J. Biol. Chem.

    (1987)
  • G.R. Jänig et al.
  • M. Claverie
  • M.J.D. Powell
There are more references available in the full text version of this article.

Cited by (0)

View full text
Copyright © 1988 Published by Elsevier Inc.