The phylogeny of the mammalian heme peroxidases and the evolution of their diverse functions

Loughran, Noeleen B.; O’Connor, Brendan; Ó’Fágáin, Ciarán; O’Connell, Mary J.

doi:10.1186/1471-2148-8-101

Cited by 34 publications

(31 citation statements)

References 60 publications

(104 reference statements)

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“…For example, thyroid peroxidase (TPO), an enzyme that participates in hormone biosynthesis and uses H 2 O 2 as a substrate, is inactivated by MMI possibly through the formation of a sulfheme like derivative [43]. The sulfheme TPO complex may also be produced in the presence of H 2 S. In fact, amino acid sequence alignment shows that TPO has His in the active distal site, which is involved in the enzyme catalytic activity and probably may play a crucial role in sulfheme formation [57, 74]. Although we focus in human peroxidases, the dehaloperoxidase-hemoglobin from the invertebrate Amphitrite ornate forms the sulfheme product and has His near the heme [75].…”

Section: Interaction Of H2s With Enzymesmentioning

confidence: 99%

Hydrogen sulfide activation in hemeproteins: The sulfheme scenario

Ríos-González¹,

Román-Morales²,

Pietri³

et al. 2014

Journal of Inorganic Biochemistry

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Traditionally known as a toxic gas, hydrogen sulfide (H2S) is now recognized as an important biological molecule involved in numerous physiological functions. Like nitric oxide (•NO) and carbon monoxide (CO), H2S is produced endogenously in tissues and cells and can modulate biological processes by acting on target proteins. For example, interaction of H2S with the oxygenated form of human hemoglobin and myoglobin produces a sulfheme protein complex that has been implicated in H2S degradation. The presence of this sulfheme derivative has also been used as a marker for endogenous H2S synthesis and metabolism. Remarkably, human catalases and peroxidases also generate this sulfheme product. In this review, we describe the structural and functional aspects of the sulfheme derivative in these proteins and postulate a generalized mechanism for sulfheme protein formation. We also evaluate the possible physiological function of this complex and highlight the issues that remain to be assessed to determine the role of sulheme proteins in H2S metabolism, detection and physiology.

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Section: Interaction Of H2s With Enzymesmentioning

confidence: 99%

Hydrogen sulfide activation in hemeproteins: The sulfheme scenario

Ríos-González¹,

Román-Morales²,

Pietri³

et al. 2014

Journal of Inorganic Biochemistry

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“…However, several animal peroxidases have been studied with regards to roles in disease and aging [13][14][15]. Recently, evolutionary relationships among mammalian heme peroxidases have been proposed by advanced phylogenetic analysis [16]. Several studies have examined the properties of heme peroxidases and numerous reviews on this topic have been published.…”

Section: Introductionmentioning

confidence: 99%

DyP-type peroxidases comprise a novel heme peroxidase family

Sugano

2008

Cell. Mol. Life Sci.

226

261

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Dye-decolorizing peroxidase (DyP) is produced by a basidiomycete (Thanatephorus cucumeris Dec 1) and is a member of a novel heme peroxidase family (DyP-type peroxidase family) that appears to be distinct from general peroxidases. Thus far, 80 putative members of this family have been registered in the PeroxiBase database (http://peroxibase.isbsib.ch/) and more than 400 homologous proteins have been detected via PSI-BLAST search. Although few studies have characterized the function and structure of these proteins, they appear to be bifunctional enzymes with hydrolase or oxygenase, as well as typical peroxidase activities. DyP-type peroxidase family suggests an ancient root compared with other general peroxidases because of their widespread distribution in the living world. In this review, firstly, an outline of the characteristics of DyP from T. cucumeris is presented and then interesting characteristics of the DyP-type peroxidase family are discussed.

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“…Two lineage-specific heterogeneous models were used: Model A and Model A Null. These models have been applied similarly elsewhere [40]. …”

Section: Methodsmentioning

confidence: 99%

Colon cancer associated genes exhibit signatures of positive selection at functionally significant positions

et al. 2012

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BackgroundCancer, much like most human disease, is routinely studied by utilizing model organisms. Of these model organisms, mice are often dominant. However, our assumptions of functional equivalence fail to consider the opportunity for divergence conferred by ~180 Million Years (MY) of independent evolution between these species. For a given set of human disease related genes, it is therefore important to determine if functional equivalency has been retained between species. In this study we test the hypothesis that cancer associated genes have different patterns of substitution akin to adaptive evolution in different mammal lineages.ResultsOur analysis of the current literature and colon cancer databases identified 22 genes exhibiting colon cancer associated germline mutations. We identified orthologs for these 22 genes across a set of high coverage (>6X) vertebrate genomes. Analysis of these orthologous datasets revealed significant levels of positive selection. Evidence of lineage-specific positive selection was identified in 14 genes in both ancestral and extant lineages. Lineage-specific positive selection was detected in the ancestral Euarchontoglires and Hominidae lineages for STK11, in the ancestral primate lineage for CDH1, in the ancestral Murinae lineage for both SDHC and MSH6 genes and the ancestral Muridae lineage for TSC1.ConclusionIdentifying positive selection in the Primate, Hominidae, Muridae and Murinae lineages suggests an ancestral functional shift in these genes between the rodent and primate lineages. Analyses such as this, combining evolutionary theory and predictions - along with medically relevant data, can thus provide us with important clues for modeling human diseases.

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The phylogeny of the mammalian heme peroxidases and the evolution of their diverse functions

Cited by 34 publications

References 60 publications

Hydrogen sulfide activation in hemeproteins: The sulfheme scenario

Hydrogen sulfide activation in hemeproteins: The sulfheme scenario

DyP-type peroxidases comprise a novel heme peroxidase family

Colon cancer associated genes exhibit signatures of positive selection at functionally significant positions

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