Molecular evolution of hydrogen peroxide degrading enzymes.

Archives of Biochemistry and Biophysics
Marcel ZámockýChristian Obinger

Abstract

For efficient removal of intra- and/or extracellular hydrogen peroxide by dismutation to harmless dioxygen and water (2H(2)O(2) → O(2) + 2H(2)O), nature designed three metalloenzyme families that differ in oligomeric organization, monomer architecture as well as active site geometry and catalytic residues. Here we report on the updated reconstruction of the molecular phylogeny of these three gene families. Ubiquitous typical (monofunctional) heme catalases are found in all domains of life showing a high structural conservation. Their evolution was directed from large subunit towards small subunit proteins and further to fused proteins where the catalase fold was retained but lost its original functionality. Bifunctional catalase-peroxidases were at the origin of one of the two main heme peroxidase superfamilies (i.e. peroxidase-catalase superfamily) and constitute a protein family predominantly present among eubacteria and archaea, but two evolutionary branches are also found in the eukaryotic world. Non-heme manganese catalases are a relatively small protein family with very old roots only present among bacteria and archaea. Phylogenetic analyses of the three protein families reveal features typical (i) for the evolution of wh...Continue Reading

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Citations

Apr 17, 2013·Archives of Microbiology·Marcel ZámockýBystrík Polek
Jun 3, 2014·BMC Microbiology·Jaeyoung ChoiYong-Hwan Lee
May 23, 2014·Cellular and Molecular Life Sciences : CMLS·Marcel ZámockýChristian Obinger
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