An analysis of substrate binding interactions in the heme peroxidase enzymes: a structural perspective

Arch Biochem Biophys. 2010 Aug 1;500(1):13-20. doi: 10.1016/j.abb.2010.02.015. Epub 2010 Mar 4.

Abstract

The interactions of heme peroxidase enzymes with their substrates have been studied for many years, but only in the last decade or so has structural information begun to appear. This review looks at crystal structures for a number of heme peroxidases in complex with a number of (mainly organic) substrates. It examines the nature and location of the binding interaction, and explores functional similarities and differences across the family.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Heme / chemistry*
  • Heme / metabolism
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Peroxidases / chemistry*
  • Peroxidases / metabolism*
  • Plant Proteins / chemistry
  • Plant Proteins / metabolism
  • Substrate Specificity

Substances

  • Plant Proteins
  • Heme
  • Peroxidases