ArticleBMC evolutionary biology2008
The phylogeny of the mammalian heme peroxidases and the evolution of their diverse functions.
Article in BMC evolutionary biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 42 citations in OpenAlex.
- Possible functional origin of TPO-like genes in chordates revealed by their pleiotropic expression and disturbed phenomena in protochordates.Cell and tissue research · 2026Article
- Myeloperoxidase as a Promising Therapeutic Target after Myocardial Infarction.Antioxidants (Basel, Switzerland) · 2024Review
- Heme-Peroxidase 2 Modulated by POU2F1 and SOX5 is Involved in Pigmentation in Pacific Oyster (Crassostrea gigas).Marine biotechnology (New York, N.Y.) · 2022Article
- Bioinformatic analysis of eosinophil activity and its implications for model and target species.Parasitology · 2020Review
- Amyloid β and free heme: bloody new insights into the pathogenesis of Alzheimer's disease.Neural regeneration research · 2018Review
- Fast and Specific Assessment of the Halogenating Peroxidase Activity in Leukocyte-enriched Blood Samples.Journal of visualized experiments : JoVE · 2016Article
- Article
- Enhancing hypothiocyanite production by lactoperoxidase - mechanism and chemical properties of promotors.Biochemistry and biophysics reports · 2015Article
- Independent evolution of four heme peroxidase superfamilies.Archives of biochemistry and biophysics · 2015Article
- Hydrogen sulfide activation in hemeproteins: the sulfheme scenario.Journal of inorganic biochemistry · 2014Review
- The fluorescein-derived dye aminophenyl fluorescein is a suitable tool to detect hypobromous acid (HOBr)-producing activity in eosinophils.The Journal of biological chemistry · 2012Article
- Functional consequence of positive selection revealed through rational mutagenesis of human myeloperoxidase.Molecular biology and evolution · 2012Article
- Colon cancer associated genes exhibit signatures of positive selection at functionally significant positions.BMC evolutionary biology · 2012Article
- Article
- The two tryptophans of β2-microglobulin have distinct roles in function and folding and might represent two independent responses to evolutionary pressure.BMC evolutionary biology · 2011Article
- Comparative analysis of vertebrate PEPT1 and PEPT2 genes.Genetica · 2010Article
- Analysis of substructural variation in families of enzymatic proteins with applications to protein function prediction.BMC bioinformatics · 2010Article
- A robust and extracellular heme-containing peroxidase from Thermobifida fusca as prototype of a bacterial peroxidase superfamily.Applied microbiology and biotechnology · 2010Article
- Positive selection neighboring functionally essential sites and disease-implicated regions of mammalian reproductive proteins.BMC evolutionary biology · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe mammalian heme peroxidases (MHPs) are a medically important group of enzymes. Included in this group are myeloperoxidase, eosinophil peroxidase, lactoperoxidase, and thyroid peroxidase. These enzymes are associated with such diverse diseases as asthma, Alzheimer's disease and inflammatory vascular disease. Despite much effort to elucidate a clearer understanding of the function of the 4 major groups of this multigene family, we still do not have a clear understanding of their relationships to each other.
resultsSufficient signal exists for the resolution of the evolutionary relationships of this family of enzymes. We demonstrate, using a root mean squared deviation statistic, how the removal of the fastest evolving sites aids in the minimisation of the effect of long branch attraction and the generation of a highly supported phylogeny. Based on this phylogeny we have pinpointed the amino acid positions that have most likely contributed to the diverse functions of these enzymes. Many of these residues are in close proximity to sites implicated in protein misfolding, loss of function or disease.
conclusionOur analysis of all available genomic sequence data for the MHPs from all available completed mammalian genomes, involved sophisticated methods of phylogeny reconstruction and data treatment. Our study has (i) fully resolved the phylogeny of the MHPs and the subsequent pattern of gene duplication, and (ii), we have detected amino acids under positive selection that have most likely contributed to the observed functional shifts in each type of MHP.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.