Comparative Analysis of Three Trypanosomatid Catalases of Different Origin.

Ľubomíra Chmelová,Richard Wheeler,Vyacheslav Yurchenko,Jana Režnarová,Amanda T S Albanaz,Claretta Bianchi,Natalya Kraeva,Alexei Yu Kostygov

doi:10.3390/antiox11010046

Ľubomíra Chmelová, Richard Wheeler + Show 6 more

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https://doi.org/10.3390/antiox11010046

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Abstract

Most trypanosomatid flagellates do not have catalase. In the evolution of this group, the gene encoding catalase has been independently acquired at least three times from three different bacterial groups. Here, we demonstrate that the catalase of Vickermania was obtained by horizontal gene transfer from Gammaproteobacteria, extending the list of known bacterial sources of this gene. Comparative biochemical analyses revealed that the enzymes of V. ingenoplastis, Leptomonas pyrrhocoris, and Blastocrithidia sp., representing the three independent catalase-bearing trypanosomatid lineages, have similar properties, except for the unique cyanide resistance in the catalase of the latter species.

Highlights

Catalase (EC 1.11.1.6) is one of the most widespread enzymes in aerobic organisms [1].Most of the typical catalases are homo-tetramers with four prosthetic heme b groups and, in some cases, another cofactor—NADPH [2]
We demonstrate that the catalase of Vickermania spp. was acquired by horizontal gene transfer (HGT) from Gammaproteobacteria, i.e., independently from those of Leishmaniinae and Blastocrithidiinae, and provide comparative biochemical analysis of different trypanosomatid catalases of Leptomonas pyrrhocoris, Blastocrithidia sp., and Vickermania ingenoplastis
The catalase of Vickermania ingenoplastis was revealed to be most closely related to that of Acinetobacter spp. of the family Moraxellaceae belonging to the order Moraxellales of the class Gammaproteobacteria (Figure 1B)

Summary

Introduction

Most of the typical catalases are homo-tetramers with four prosthetic heme b groups and, in some cases, another cofactor—NADPH [2] This enzyme catalyzes the decomposition of hydrogen peroxide, which is produced during aerobic metabolism, into oxygen and water in a two-step process. This compound reacts with the second H2 O2 molecule, resulting in two single-electron reductions in the enzyme, followed by the production of oxygen and the second molecule of water [3,4]. The kinetics of this reaction depends on the distal side residues [5]. Catalases were studied for over 100 years [8] and experimentally determined structures of several representative enzymes (for example, those from bovine liver [9], Penicillium vitale [10], and Saccharomyces cerevisiae [11]) were published

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