Phylogenetic relationships among prokaryotic and eukaryotic catalases

Abstract

Seventy-four catalase protein sequences, including 29 bacterial, 8 fungal, 7 animal, and 30 plant sequences, were compiled, and 70 were used for phylogenetic reconstruction. The core of the resulting tree revealed unique, separate groups of plant and animal catalases, two groups of fungal catalases, and three groups of bacterial catalases. The only overlap of kingdoms occurred within one branch and involved fungal and bacterial large-subunit enzymes. The other fungal branch was closely linked to the group of animal enzymes. Group I bacterial catalases were more closely related to the plant enzymes and contained such diverse taxa as the Gram-positive Listeria seeligeri, Deinocococcus radiodurans, and gamma-proteobacteria. Group III bacterial sequences were more closely related to fungal and animal sequences and included enzymes from a broad range of bacteria including high- and low-GC Gram positives, proteobacteria, and a bacteroides species. Group II was composed of large-subunit catalases from diverse sources including Gram positives (low-GC Bacilli and high-GC Mycobacteria), proteobacteria, and species of the filamentous fungus Aspergillus. These data can be interpreted in terms of two gene duplication events that produced a minimum of three catalase gene family members that subsequently evolved in response to environmental demands. Horizontal gene transfer may have been responsible for the group II mixture of bacterial and fungal large-subunit catalases.

Comparative study of catalase-peroxidases (KatGs)

“…(Fita and Rossman, 1985 (Klotz and Loewen, 2003 (Murshudov eÍ al., 1982), Proteus ntirabilis (PMC) (Gouet et al, 1995), E'çcherichia coli (HPII) (Bravo et a\.,1995 and, human erythrocytes (HEC) (Ko el al',1999;Puntam et al, lggg), Pseudomonas syrengae (CatF) (Carpena et a\.,2001 and (Murshudov et a|.,1996) (Kono and Irridovich, 1983), but now are more commonly called Mn-containing catalases (Allgood and Pery, 1986), with the terms non-heme (Nicholls, 2001) (Hillar et a\.,1999). The overall reaction can be summarized as: (Dunford, 1991 .ln the HPC structure, the elongated electron density associated with the iron in subunit B resembles the maps of oxymyoglobin (Vojtechovsky et a\.,1999) and compound III of horseradish peroxidase (Berglund et al,20OZ (Klotz, 1997 (Zhang et al, 1992), the front line antituberculosis drug, and were the leading cause of the world-wide resurgence of tuberculosis (Deretic et al, 1996). This gave rise to significant interest among researchers, worldwide.…”

The Gene Expression Profile by RT-PCR and Immunohistochemical Expression Pattern of Catalase in the Kidney Tissue of Both Healthy and Diabetic Mice

“…Bu enzim, yaygın olarak ökaryotlar, bitkiler ve mikroorganizmalarda bulunmaktadır 16 . Değişik canlı familyalarından 74 türün CAT geni karşılaştırıldığında insan, sığır, fare ve ratlara ait CAT'ın hem baz dizilimi hem de amino asit dizilimi bakımından diğer 70 türe nazaran birbirine daha yakın olduğu bildirilmiştir 17 . Dokulardaki CAT enzimi aktivitesi büyük değişiklikler göstermektedir.…”

Exogenous Catalase Gene Expression as a Tool for Enhancing Metabolic Activity and Production of Biomaterials in Host Microorganisms

“…In the second step, compound I oxidizes a second H 2 O 2 molecule to molecular oxygen and water (eqs. 1 and 2; Deisseroth & Dounce, 1970;Schonbaum & Chance, 1976 Phylogenic analysis based on the amino-acid sequence deduced from the gene sequence of typical catalases has revealed their subdivision into three distinct clades (Klotz et al, 1997 Most aerobic bacteria contain one or more catalases, which are produced in response to oxidative stress or depending on the growth phase. Escherichia coli possess two types of catalase gene, katG and katE.…”