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Information on EC 1.11.1.11 - L-ascorbate peroxidase and Organism(s) Trypanosoma cruzi and UniProt Accession Q8I1N3

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EC Tree
     1 Oxidoreductases
         1.11 Acting on a peroxide as acceptor
             1.11.1 Peroxidases
                1.11.1.11 L-ascorbate peroxidase
IUBMB Comments
A heme protein. Oxidizes ascorbate and low molecular weight aromatic substrates. The monodehydroascorbate radical produced is either directly reduced back to ascorbate by EC 1.6.5.4 [monodehydroascorbate reductase (NADH)] or undergoes non-enzymic disproportionation to ascorbate and dehydroascorbate.
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This record set is specific for:
Trypanosoma cruzi
UNIPROT: Q8I1N3
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Word Map
The taxonomic range for the selected organisms is: Trypanosoma cruzi
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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Synonyms
ascorbate peroxidase, apex2, cytosolic ascorbate peroxidase, lmapx, ascorbate peroxidase 2, l-ascorbate peroxidase, ascorbate peroxidase 1, ascorbic acid peroxidase, osapx8, osapx2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ascorbate peroxidase
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-
-
-
ascorbic acid peroxidase
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-
-
-
L-ascorbic acid peroxidase
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-
-
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L-ascorbic acid-specific peroxidase
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-
-
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peroxidase, ascorbate
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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-
-
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oxidation
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reduction
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peroxidation
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-
SYSTEMATIC NAME
IUBMB Comments
L-ascorbate:hydrogen-peroxide oxidoreductase
A heme protein. Oxidizes ascorbate and low molecular weight aromatic substrates. The monodehydroascorbate radical produced is either directly reduced back to ascorbate by EC 1.6.5.4 [monodehydroascorbate reductase (NADH)] or undergoes non-enzymic disproportionation to ascorbate and dehydroascorbate.
CAS REGISTRY NUMBER
COMMENTARY hide
72906-87-7
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 L-ascorbate + H2O2 + 2 H+
2 monodehydroascorbate + 2 H2O
show the reaction diagram
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-
-
?
cytochrome c + H2O2
? + H2O
show the reaction diagram
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-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
show the reaction diagram
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-
?
additional information
?
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reaction includes formation of a compound I-like product, characteristic of the generation of a tryptophanyl radical-cation at residue W233. In addition, formation of a C222-derived radical is observed. electron transfer between Trp233 and Cys222 is possible and likely to participate in the catalytic cycle
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.029
cytochrome c
pH 7.4, 25°C
0.19
L-ascorbate
pH 7.4, 25°C
additional information
additional information
ascorbate can saturate the ascorbate-dependent hemoperoxidase activity indicating that the enzyme obeys Michaelis-Menten kinetics
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
210
cytochrome c
pH 7.4, 25°C
35
L-ascorbate
pH 7.4, 25°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
enzyme is closely associated with mitochondrial membranes
Manually annotated by BRENDA team
enzyme is associated with plasma membrane
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
overexpressing strains are significantly more infective to macrophages and cardiomyocytes, as well as in the mouse model of Chagas disease than wild-type
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q8I1N3_TRYCR
328
0
36501
TrEMBL
Mitochondrion (Reliability: 2)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
W233F
complete loss of cytochrome c-dependent activity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of an epitope-tagged form of the enzyme in Trypanosoma cruzi
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wilkinson, S.R.; Obado, S.O.; Mauricio, I.L.; Kelly, J.M.
Trypanosoma cruzi expresses a plant-like ascorbate-dependent hemoperoxidase localized to the endoplasmic reticulum
Proc. Natl. Acad. Sci. USA
99
13453-13458
2002
Trypanosoma cruzi (Q8I1N3)
Manually annotated by BRENDA team
Ishikawa, T.; Shigeoka, S.
Recent advances in ascorbate biosynthesis and the physiological significance of ascorbate peroxidase in photosynthesizing organisms
Biosci. Biotechnol. Biochem.
72
1143-1154
2008
Arabidopsis sp., Galdieria partita, Galdieria sulphuraria, Leishmania major (Q4Q3K2), Trypanosoma cruzi (Q8I1N3), Euglena gracilis (Q8LP26), Chlamydomonas sp. W80 (Q9SXL5)
Manually annotated by BRENDA team
Hugo, M.; Martinez, A.; Trujillo, M.; Estrada, D.; Mastrogiovanni, M.; Linares, E.; Augusto, O.; Issoglio, F.; Zeida, A.; Estrin, D.A.; Heijnen, H.F.; Piacenza, L.; Radi, R.
Kinetics, subcellular localization, and contribution to parasite virulence of a Trypanosoma cruzi hybrid type A heme peroxidase (TcAPx-CcP)
Proc. Natl. Acad. Sci. USA
114
E1326-E1335
2017
Trypanosoma cruzi (Q8I1N3)
Manually annotated by BRENDA team