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Information on EC 1.11.1.11 - L-ascorbate peroxidase and Organism(s) Leishmania major and UniProt Accession Q4Q3K2

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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:
Leishmania major
UNIPROT: Q4Q3K2
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Word Map
The taxonomic range for the selected organisms is: Leishmania major
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide(Overall reactions are displayed. Show all >>)
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
ascorbic acid peroxidase
-
-
-
-
L-ascorbic acid peroxidase
-
-
-
-
L-ascorbic acid-specific peroxidase
-
-
-
-
peroxidase, ascorbate
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
reduction
peroxidation
-
-
-
-
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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Cytochrome c + H2O
?
show the reaction diagram
-
-
-
-
?
cytochrome c + H2O2
?
show the reaction diagram
-
able to use both ascorbate and cytochrome c as reducing electron donors
-
-
?
dihydrorhodamine 123 + H2O2
?
show the reaction diagram
-
assay, peroxidase substrate
-
-
?
guaiacol + H2O2
?
show the reaction diagram
-
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-ascorbate + H2O2
dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.025 - 6
cytochrome c
0.017 - 6.7
guaiacol
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.53
ascorbate
-
25°C, wild-type enzyme
1.83
cytochrome c
-
25°C, wild-type enzyme
2.5
guaiacol
-
25°C, wild-type enzyme
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
peroxidase assay
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q4Q3K2_LEIMA
303
1
33873
TrEMBL
Mitochondrion (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000
-
determined by SDS-PAGE and Western blot analysis, LmAPX in the intermembrane space of the mitochondrial inner membrane is appr. 3.6 kDa shorter than the full-length gene
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
W208F
-
the optical spectrum of the W208F mutant closely resembles that of wild type LmAPX at pH 7.5 in the absence of ascorbate. W208F mutant causes a spectral red shift from high spin to low spin, indicating that the mutant can react with H2O2. Cytochrome c binding affinity to the enzyme does not alter after mutation. The mutant is 1000times less active than the wild type in cytochrome c oxidation
W208Y
-
mutant shows low spin hem. The mutant does not react with H2O2
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mitochondria are prepared and fractionated
-
wild-type and mutant enzyme W208F expressed in Escherichia coli
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
into the vector pXG B2863 for transfection of Leishmania major cells
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into the vector pXG-B2863 for transfection of Leishmania major cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of LmAPX is increased when cells are treated with exogenous H2O2
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yadav, R.K.; Dolai, S.; Pal, S.; Adak, S.
Role of tryptophan-208 residue in cytochrome c oxidation by ascorbate peroxidase from Leishmania major-kinetic studies on Trp208Phe mutant and wild type enzyme
Biochim. Biophys. Acta
1784
863-871
2008
Leishmania major
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
Dolai, S.; Yadav, R.K.; Pal, S.; Adak, S.
Overexpression of mitochondrial Leishmania major ascorbate peroxidase shows enhanced tolerance to oxidative stress-induced programmed cell death and protein damage
Eukaryot. Cell
8
1721-1731
2009
Leishmania major
Manually annotated by BRENDA team
Dolai, S.; Yadav, R.K.; Pal, S.; Adak, S.
Leishmania major ascorbate peroxidase overexpression protects cells against reactive oxygen species-mediated cardiolipin oxidation
Free Radic. Biol. Med.
45
1520-1529
2008
Leishmania major, Leishmania major 5ASKH
Manually annotated by BRENDA team