Understanding functional diversity and substrate specificity in haem peroxidases: what can we learn from ascorbate peroxidase?
This review summarizes the most recent advances in our understanding of the haem enzyme ascorbate peroxidase. The aim is to show how the combined applications of protein engineering, mechanistic and structural studies can be used to provide an overall picture of enzyme catalysis, and how this information can be used to provide new insight into other, more well-characterized peroxidases (in particular cytochrome c peroxidase). It contains 212 references and covers literature up to March 2003.
Raven
Emma Lloyd
EL
Department of Chemistry, University of Leicester, University Road, Leicester, UK LE1 7RH. emma.raven@le.ac.uk
D000595:Amino Acid Sequence; D060387:Ascorbate Peroxidases; D002384:Catalysis; D006418:Heme; D008969:Molecular Sequence Data; D015394:Molecular Structure; D010544:Peroxidases / Q000737:chemistry / Q000378:metabolism; D010945:Plants, Edible / Q000201:enzymology; D011487:Protein Conformation; D015202:Protein Engineering; D013379:Substrate Specificity
D006418:Heme; D010544:Peroxidases; D060387:Ascorbate Peroxidases