Literature summary for 1.11.1.11 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 .

Search for more literature for 1.11.1.11

Cloned(Commentary)

Cloned (Comment)	Organism
enzyme expression analysis, phylogenetic analysis and tree	Leptomonas seymouri
enzyme expression analysis, phylogenetic analysis and tree	Euglena gracilis
enzyme expression analysis, phylogenetic analysis and tree	Crithidia thermophila
enzyme expression analysis, phylogenetic analysis and tree	Novymonas esmeraldas
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
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

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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

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

Organism

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

Source Tissue

Source Tissue	Comment	Organism	Textmining
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]

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

Substrates and Products (Substrate)

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

Subunits

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

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

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

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

Expression

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

General Information

General Information	Comment	Organism
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
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
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
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
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
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
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
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
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
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
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
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
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
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

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Release 2023.1 (January 2023)