title: An analysis of substrate binding interactions in the heme peroxidase enzymes: a structural perspective.
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.
authors.affiliation: Department of Chemistry, University of Leicester, England, UK.
authors.forename: Andrea
authors.initials: A
authors.lastname: Gumiero
authors.forename: Emma J
authors.initials: EJ
authors.lastname: Murphy
authors.forename: Clive L
authors.initials: CL
authors.lastname: Metcalfe
authors.forename: Peter C E
authors.initials: PC
authors.lastname: Moody
authors.forename: Emma Lloyd
authors.initials: EL
authors.lastname: Raven
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D006418:Heme / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010544:Peroxidases / Q000737:chemistry* / Q000378:metabolism*; D010940:Plant Proteins / Q000737:chemistry / Q000378:metabolism; D013379:Substrate Specificity
chemical_list: D010940:Plant Proteins; D006418:Heme; D010544:Peroxidases