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Analysis of the catalytic specificity of cytochrome P450 enzymes through site-directed mutagenesis

Academic Article
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Overview

authors

  • Johnson, Eric
  • Kronbach, T.
  • Hsu, M. H.

publication date

  • January 1992

journal

  • FASEB Journal  Journal

abstract

  • The way in which structural diversity encodes the capacity of individual P450 enzymes to metabolize multiple, structurally distinct substrates remains largely unknown. The tools of molecular biology provide a means of identifying amino acid residues among closely related P450s that are determinants of their distinct catalytic properties. Work in our laboratory has identified two substrate specificity-determining segments of the amino acid sequences of subfamily 2C P450s. A pattern has emerged from this work, and that of others, which suggests a model for the structural basis of P450 catalytic diversity.

subject areas

  • Amino Acid Sequence
  • Animals
  • Cytochrome P-450 Enzyme System
  • Genetic Variation
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • RNA Splicing
  • Sequence Homology, Nucleic Acid
  • Steroid 21-Hydroxylase
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Research

keywords

  • CYTOCHROME-P450
  • ENZYME ENGINEERING
  • PROGESTERONE 21-HYDROXYLATION
  • SITE-DIRECTED MUTAGENESIS
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Identity

International Standard Serial Number (ISSN)

  • 0892-6638

PubMed ID

  • 1537459
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Additional Document Info

start page

  • 700

end page

  • 705

volume

  • 6

issue

  • 2

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