An analysis of substrate binding interactions in the heme peroxidase enzymes: a structural perspective.
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.
Gumiero
Andrea
A
Department of Chemistry, University of Leicester, England, UK.
Murphy
Emma J
EJ
Metcalfe
Clive L
CL
Moody
Peter C E
PC
Raven
Emma Lloyd
EL
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
D010940:Plant Proteins; D006418:Heme; D010544:Peroxidases