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Active site structure and catalytic mechanisms of human peroxidases
- Source :
- Archives of Biochemistry and Biophysics. 445:199-213
- Publication Year :
- 2006
- Publisher :
- Elsevier BV, 2006.
-
Abstract
- Myeloperoxidase (MPO), eosinophil peroxidase, lactoperoxidase, and thyroid peroxidase are heme-containing oxidoreductases (EC 1.7.1.11), which bind ligands and/or undergo a series of redox reactions. Though sharing functional and structural homology, reflecting their phylogenetic origin, differences are observed regarding their spectral features, substrate specificities, redox properties, and kinetics of interconversion of the relevant redox intermediates ferric and ferrous peroxidase, compound I, compound II, and compound III. Depending on substrate availability, these heme enzymes path through the halogenation cycle and/or the peroxidase cycle and/or act as poor (pseudo-)catalases. Based on the published crystal structures of free MPO and its complexes with cyanide, bromide and thiocyanate as well as on sequence analysis and modeling, we critically discuss structure-function relationships. This analysis highlights similarities and distinguishing features within the mammalian peroxidases and intents to provide the molecular and enzymatic basis to understand the prominent role of these heme enzymes in host defense against infection, hormone biosynthesis, and pathogenesis.
- Subjects :
- Protein Conformation
Stereochemistry
Molecular Sequence Data
Biophysics
Biochemistry
Catalysis
Substrate Specificity
Structure-Activity Relationship
chemistry.chemical_compound
Humans
Amino Acid Sequence
Binding site
Molecular Biology
Heme
chemistry.chemical_classification
Binding Sites
biology
Lactoperoxidase
Active site
Enzyme Activation
Enzyme
Peroxidases
chemistry
Myeloperoxidase
biology.protein
Eosinophil peroxidase
Peroxidase
Subjects
Details
- ISSN :
- 00039861
- Volume :
- 445
- Database :
- OpenAIRE
- Journal :
- Archives of Biochemistry and Biophysics
- Accession number :
- edsair.doi.dedup.....22bd967646e2ddb5b684c84d74df8576