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Literature summary extracted from

  • Skodova-Sverakova, I.; Zahonova, K.; Buckova, B.; Fuessy, Z.; Yurchenko, V.; Lukes, J.
    Catalase and ascorbate peroxidase in Euglenozoan protists (2020), Pathogens, 9, 317 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.11.1.11 enzyme expression analysis, phylogenetic analysis and tree Leptomonas seymouri
1.11.1.11 enzyme expression analysis, phylogenetic analysis and tree Euglena gracilis
1.11.1.11 enzyme expression analysis, phylogenetic analysis and tree Crithidia thermophila
1.11.1.11 enzyme expression analysis, phylogenetic analysis and tree Novymonas esmeraldas
1.11.1.11 enzyme expression analysis, phylogenetic analysis and tree, in Blastocrithidia sp. P57 very low APX activity is detected, despite the fact that the species apparently lacks the corresponding gene Blastochritidia sp. P57
1.11.1.11 enzyme expression analysis, phylogenetic analysis and tree, in Rhynchopus humris very low APX activity is detected, despite the fact that the species apparently lacks the corresponding gene Rhynchopus humris

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.11.1.11 chloroplast
-
 Euglena gracilis 9507
-
1.11.1.11 kinetoplast
-
 Leptomonas seymouri 20023
-
1.11.1.11 kinetoplast
-
 Crithidia thermophila 20023
-
1.11.1.11 kinetoplast
-
 Novymonas esmeraldas 20023
-
1.11.1.11 additional information subcellular localization analysis Leptomonas seymouri
-
-
1.11.1.11 additional information subcellular localization analysis Euglena gracilis
-
-
1.11.1.11 additional information subcellular localization analysis Blastochritidia sp. P57
-
-
1.11.1.11 additional information subcellular localization analysis Crithidia thermophila
-
-
1.11.1.11 additional information subcellular localization analysis Novymonas esmeraldas
-
-
1.11.1.11 additional information subcellular localization analysis Rhynchopus humris
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.11.1.11 Fe2+ in the heme group Leptomonas seymouri
1.11.1.11 Fe2+ in the heme group Euglena gracilis
1.11.1.11 Fe2+ in the heme group Blastochritidia sp. P57
1.11.1.11 Fe2+ in the heme group Crithidia thermophila
1.11.1.11 Fe2+ in the heme group Novymonas esmeraldas
1.11.1.11 Fe2+ in the heme group Rhynchopus humris

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.11.1.11 2 L-ascorbate + H2O2 + 2 H+ Leptomonas seymouri
-
 L-ascorbate + L-dehydroascorbate + 2 H2O
-
 ?
1.11.1.11 2 L-ascorbate + H2O2 + 2 H+ Euglena gracilis
-
 L-ascorbate + L-dehydroascorbate + 2 H2O
-
 ?
1.11.1.11 2 L-ascorbate + H2O2 + 2 H+ Blastochritidia sp. P57
-
 L-ascorbate + L-dehydroascorbate + 2 H2O
-
 ?
1.11.1.11 2 L-ascorbate + H2O2 + 2 H+ Crithidia thermophila
-
 L-ascorbate + L-dehydroascorbate + 2 H2O
-
 ?
1.11.1.11 2 L-ascorbate + H2O2 + 2 H+ Novymonas esmeraldas
-
 L-ascorbate + L-dehydroascorbate + 2 H2O
-
 ?
1.11.1.11 2 L-ascorbate + H2O2 + 2 H+ Rhynchopus humris
-
 L-ascorbate + L-dehydroascorbate + 2 H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.11.1.11 Blastochritidia sp. P57
-
-
-
1.11.1.11 Crithidia thermophila
-
-
-
1.11.1.11 Euglena gracilis Q8LP26
-
-
1.11.1.11 Leptomonas seymouri
-
-
-
1.11.1.11 no activity in Diplonema papillatum
-
-
-
1.11.1.11 no activity in Euglena longa
-
-
-
1.11.1.11 no activity in Trypanosoma brucei
-
-
-
1.11.1.11 Novymonas esmeraldas
-
-
-
1.11.1.11 Rhynchopus humris
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.11.1.11 additional information transcriptomic analysis, the organisms possesses kinetoplastid-specific hAPX-CCP. Gene expression shows the highest number of transcripts at 14°C and its decrease with elevated temperature Leptomonas seymouri
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.11.1.11 0.01
-
 below, pH 7.2, 25°C Blastochritidia sp. P57
1.11.1.11 0.01
-
 below, pH 7.2, 25°C Rhynchopus humris
1.11.1.11 0.039 0.055 different samples grown at different temperatures from 14-34°C, assay at pH 7.2, 25°C Leptomonas seymouri
1.11.1.11 0.048 0.06 different samples grown at different temperatures from 14-34°C, assay at pH 7.2, 25°C Crithidia thermophila
1.11.1.11 0.206
-
 pH 7.2, 25°C Novymonas esmeraldas
1.11.1.11 0.625
-
 light-grown culture, pH 7.2, 25°C. No activity in the dark-grown culture Euglena gracilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.11.1.11 2 L-ascorbate + H2O2 + 2 H+
-
 Leptomonas seymouri L-ascorbate + L-dehydroascorbate + 2 H2O
-
 ?
1.11.1.11 2 L-ascorbate + H2O2 + 2 H+
-
 Euglena gracilis L-ascorbate + L-dehydroascorbate + 2 H2O
-
 ?
1.11.1.11 2 L-ascorbate + H2O2 + 2 H+
-
 Blastochritidia sp. P57 L-ascorbate + L-dehydroascorbate + 2 H2O
-
 ?
1.11.1.11 2 L-ascorbate + H2O2 + 2 H+
-
 Crithidia thermophila L-ascorbate + L-dehydroascorbate + 2 H2O
-
 ?
1.11.1.11 2 L-ascorbate + H2O2 + 2 H+
-
 Novymonas esmeraldas L-ascorbate + L-dehydroascorbate + 2 H2O
-
 ?
1.11.1.11 2 L-ascorbate + H2O2 + 2 H+
-
 Rhynchopus humris L-ascorbate + L-dehydroascorbate + 2 H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
1.11.1.11 More the catalytic properties of APX depend on the architecture of its domains, substrate binding and orienting sites, enzyme domain structure, overview Leptomonas seymouri
1.11.1.11 More the catalytic properties of APX depend on the architecture of its domains, substrate binding and orienting sites, enzyme domain structure, overview Euglena gracilis
1.11.1.11 More the catalytic properties of APX depend on the architecture of its domains, substrate binding and orienting sites, enzyme domain structure, overview Crithidia thermophila
1.11.1.11 More the catalytic properties of APX depend on the architecture of its domains, substrate binding and orienting sites, enzyme domain structure, overview Novymonas esmeraldas

Synonyms

EC Number Synonyms Comment Organism
1.11.1.11 APX
-
 Leptomonas seymouri
1.11.1.11 APX
-
 Euglena gracilis
1.11.1.11 APX
-
 Blastochritidia sp. P57
1.11.1.11 APX
-
 Crithidia thermophila
1.11.1.11 APX
-
 Novymonas esmeraldas
1.11.1.11 APX
-
 Rhynchopus humris
1.11.1.11 ascorbate peroxidase
-
 Leptomonas seymouri
1.11.1.11 ascorbate peroxidase
-
 Euglena gracilis
1.11.1.11 ascorbate peroxidase
-
 Blastochritidia sp. P57
1.11.1.11 ascorbate peroxidase
-
 Crithidia thermophila
1.11.1.11 ascorbate peroxidase
-
 Novymonas esmeraldas
1.11.1.11 ascorbate peroxidase
-
 Rhynchopus humris

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.11.1.11 25
-
 assay at Leptomonas seymouri
1.11.1.11 25
-
 assay at Euglena gracilis
1.11.1.11 25
-
 assay at Blastochritidia sp. P57
1.11.1.11 25
-
 assay at Crithidia thermophila
1.11.1.11 25
-
 assay at Novymonas esmeraldas
1.11.1.11 25
-
 assay at Rhynchopus humris

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.11.1.11 7.2
-
 assay at Leptomonas seymouri
1.11.1.11 7.2
-
 assay at Euglena gracilis
1.11.1.11 7.2
-
 assay at Blastochritidia sp. P57
1.11.1.11 7.2
-
 assay at Crithidia thermophila
1.11.1.11 7.2
-
 assay at Novymonas esmeraldas
1.11.1.11 7.2
-
 assay at Rhynchopus humris

Cofactor

EC Number Cofactor Comment Organism Structure
1.11.1.11 heme
-
 Leptomonas seymouri
1.11.1.11 heme
-
 Euglena gracilis
1.11.1.11 heme
-
 Blastochritidia sp. P57
1.11.1.11 heme
-
 Crithidia thermophila
1.11.1.11 heme
-
 Novymonas esmeraldas
1.11.1.11 heme
-
 Rhynchopus humris

Expression

EC Number Organism Comment Expression
1.11.1.11 Leptomonas seymouri gene expression shows the highest number of transcripts at 14°C and its decrease with elevated temperature additional information
1.11.1.11 Crithidia thermophila gene expression shows the highest number of transcripts at 14°C and its decrease with elevated temperature additional information

General Information

EC Number General Information Comment Organism
1.11.1.11 evolution Euglena gracilis contains a photosynthesis-specific APX shared with other phototrophic euglenophytes, along with a putative plastidial APX acquired from and limited to Chloroplastida. Moreover, both diplonemids and euglenids encode a novel clade of peroxidases with a yet unknown function, while most kinetoplastids share a unique hAPX-CCP enzyme exhibiting both the APX and cytochrome c peroxidases (CCP) activities Euglena gracilis
1.11.1.11 evolution the complex phylogenetic pattern, diversity, and distribution of catalase and APX in euglenozoans testify to their importance for these protists. The distribution of APX and catalase (CAT) in diplonemids is best explained by a scenario, in which the predecessor of these marine protists lacked both enzymes, which were reacquired by horizontal gene transfer from either prokaryotic or eukaryotic sources. Moreover, both diplonemids and euglenids encode a novel clade of peroxidases with a yet unknown function, while most kinetoplastids share a unique hAPX-CCP enzyme exhibiting both the APX and cytochrome c peroxidases (CCP) activities Leptomonas seymouri
1.11.1.11 evolution the complex phylogenetic pattern, diversity, and distribution of catalase and APX in euglenozoans testify to their importance for these protists. The distribution of APX and catalase (CAT) in diplonemids is best explained by a scenario, in which the predecessor of these marine protists lacked both enzymes, which were reacquired by horizontal gene transfer from either prokaryotic or eukaryotic sources. Moreover, both diplonemids and euglenids encode a novel clade of peroxidases with a yet unknown function, while most kinetoplastids share a unique hAPX-CCP enzyme exhibiting both the APX and cytochrome c peroxidases (CCP) activities Crithidia thermophila
1.11.1.11 evolution the complex phylogenetic pattern, diversity, and distribution of catalase and APX in euglenozoans testify to their importance for these protists. The distribution of APX and catalase (CAT) in diplonemids is best explained by a scenario, in which the predecessor of these marine protists lacked both enzymes, which were reacquired by horizontal gene transfer from either prokaryotic or eukaryotic sources. Moreover, both diplonemids and euglenids encode a novel clade of peroxidases with a yet unknown function, while most kinetoplastids share a unique hAPX-CCP enzyme exhibiting both the APX and cytochrome c peroxidases (CCP) activities Novymonas esmeraldas
1.11.1.11 additional information the enzyme contains a H2O2 binding domain, the critical residues that coordinate binding of H2O2 by APX are R158,W161, and H162(numbering according to the chloroplastic ascorbate peroxidase from tobacco plants) Leptomonas seymouri
1.11.1.11 additional information the enzyme contains a H2O2 binding domain, the critical residues that coordinate binding of H2O2 by APX are R158,W161, and H162(numbering according to the chloroplastic ascorbate peroxidase from tobacco plants) Euglena gracilis
1.11.1.11 additional information the enzyme contains a H2O2 binding domain, the critical residues that coordinate binding of H2O2 by APX are R158,W161, and H162(numbering according to the chloroplastic ascorbate peroxidase from tobacco plants) Crithidia thermophila
1.11.1.11 additional information the enzyme contains a H2O2 binding domain, the critical residues that coordinate binding of H2O2 by APX are R158,W161, and H162(numbering according to the chloroplastic ascorbate peroxidase from tobacco plants). Enzyme domain structure, overview Novymonas esmeraldas
1.11.1.11 physiological function Euglenozoa recruit APXs as detoxifying enzymes for specific molecular tasks, such as photosynthesis in euglenids and membrane-bound peroxidase activity in kinetoplastids and some diplonemids Novymonas esmeraldas
1.11.1.11 physiological function Euglenozoa recruit APXs as detoxifying enzymes for specific molecular tasks, such as photosynthesis in euglenids and membrane-bound peroxidase activity in kinetoplastids and some diplonemids. The diplonemid Rhynchopus humris shows very low APX activity despite the fact that the species apparently lacks the corresponding gene. The kinetic parameters of catalase (CAT) suggest yet another explanation for the lack of measurable activity in Rhynchopus humris. The low affinity of CAT to H2O2 implies that it is responsible for the removal of excessive ROS when their concentration is high, while high-affinity APX modulates low concentration of ROS, necessary for cell signaling Rhynchopus humris
1.11.1.11 physiological function Euglenozoa recruit APXs as detoxifying enzymes for specific molecular tasks, such as photosynthesis in euglenids and membrane-bound peroxidase activity in kinetoplastids and some diplonemids. The kinetoplastid Blastochritidia sp. P57 shows very low APX activity despite the fact that the species apparently lacks the corresponding gene. The kinetic parameters of catalase (CAT) suggest yet another explanation for the lack of measurable activity in Blastocrithidia sp. P57. The low affinity of CAT to H2O2 implies that it is responsible for the removal of excessive ROS when their concentration is high, while high-affinity APX modulates low concentration of ROS, necessary for cell signaling Blastochritidia sp. P57
1.11.1.11 physiological function Euglenozoa recruit APXs as detoxifying enzymes for specific molecular tasks, such as photosynthesis in euglenids and membrane-bound peroxidase activity in kinetoplastids and some diplonemids. The respiration rate does not correlate with APX activity Leptomonas seymouri
1.11.1.11 physiological function Euglenozoa recruit APXs as detoxifying enzymes for specific molecular tasks, such as photosynthesis in euglenids and membrane-bound peroxidase activity in kinetoplastids and some diplonemids. The respiration rate does not correlate with APX activity Euglena gracilis
1.11.1.11 physiological function Euglenozoa recruit APXs as detoxifying enzymes for specific molecular tasks, such as photosynthesis in euglenids and membrane-bound peroxidase activity in kinetoplastids and some diplonemids. The respiration rate does not correlate with APX activity Crithidia thermophila