Cited by 170Neutrophil, Myeloperoxidase and Oxidative MechanismsHemoglobin structure and functionRedox biology and oxidative stress

The peroxidase–cyclooxygenase superfamily: Reconstructed evolution of critical enzymes of the innate immune system

Zamocky, Marcel, Jakopitsch, Christa, Furtmüller, Paul G., Dunand, Christophe, Obinger, Christian·2008·Proteins: Structure, Function, and Bioinformatics

Abstract

The authors have reconstructed the phylogenetic relationships of the main evolutionary lines of mammalian heme containing peroxidases. The sequences of intensively investigated human myeloperoxidase, eosinophil peroxidase, and lactoperoxidase, which participate in host defence against infections, were aligned together with newly found open reading frames coding for highly similar putative peroxidase domains in all kingdoms of life. The evolutionary relationships were reconstructed using neighbor‐joining, maximum parsimony, and maximum likelihood methods. It is demonstrated that this enzyme superfamily obeys the rules of birth‐and‐death model of multigene family evolution and contains proteins with a variety of function that could be grouped in seven subfamilies. On the basis of occurrence and the fact that two main enzymatic activities are related with these metalloproteins, they propose the name peroxidase–cyclooxygenase superfamily for this widely spread group of heme‐containing oxidoreductases. Well known structure–function relationships in mammalian peroxidases formed the basis for the critical inspection of all subfamilies. The presented data unequivocally suggest that predecessor genes of mammalian heme peroxidases have segregated very early in evolution. Before organisms developed an acquired immunity, their antimicrobial defence depended on enzymes that were recruited upon pathogen invasion and could produce antimicrobial reaction products. Thus, these peroxidatic heme proteins evolved to important components in the innate immune defence system. This work shows that even in certain prokaryotic organisms, genes encoding putative antimicrobial enzymes are found providing a group of bacteria with an evolutionary advantage over the others. Proteins 2008. © 2008 Wiley‐Liss, Inc.

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Crossref · 10.1002/prot.21950

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Authors
Zamocky, M., Jakopitsch, C., Furtmüller, P. G., Dunand, C., & Obinger, C.
Affiliations
  • BOKU University (AT)
  • University of Geneva (CH)
Venue
Proteins: Structure, Function, and Bioinformatics
Publisher
Wiley
Published
2008-02-04
Volume
72
Issue
2
Pages
589-605
ISSN
  • 0887-3585 (ISSN-L)
  • 1097-0134
OpenAlex
W2153047806
Cited by
170
References
42
Citations by year
2026: 4 · 2025: 5 · 2024: 8 · 2023: 10 · 2022: 10 · 2021: 8 · 2020: 13 · 2019: 7 · 2018: 14 · 2017: 9 · 2016: 4 · 2015: 11 · 2014: 15 · 2013: 11 · 2012: 14
FWCI
3.75
Type
journal article
Language
en
Open access
closed
Locations
  • Proteins Structure Function and Bioinformatics (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Keywords
heme peroxidase, myeloperoxidase, eosinophil peroxidase, lactoperoxidase, phylogenetic relationships, multigene family evolution, innate immunity, antimicrobial defense, structure-function relationship, gene family evolution
MeSH terms
Animals, Biological Evolution, Immunity, Innate, Peroxidases, Phylogeny, Prostaglandin-Endoperoxide Synthases, Likelihood Functions, Open Reading Frames, Sequence Alignment

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