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Information on EC 1.11.1.11 - L-ascorbate peroxidase and Organism(s) Glycine max and UniProt Accession Q43758
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1.11.1.11 L-ascorbate peroxidaseIUBMB 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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Word Map
- 1.11.1.11
- catalase
- dismutase
- sod
- malondialdehyde
- seedling
-
chlorophyl
- dehydroascorbate
- guaiacol
- shoot
- drought
- biomass
- phenol
- chloroplast
- cultivar
- monodehydroascorbate
-
electrolyte
-
carotenoid
-
non-enzymatic
- cadmium
- peroxidases
- asa
- lipoxygenase
- thylakoidal
-
foliar
-
abscisic
- photosystem
-
stomatal
-
hydroponic
-
postharvest
- mdhar
- aestivum
- triticum
-
ascorbate-glutathione
-
photochemical
-
phytotoxicity
-
1.6.4.2
-
chilling
- phytochelatins
-
irrigation
-
non-photochemical
-
cd-induced
-
phytoextraction
-
transpiration
-
salt-stressed
-
hoagland
-
photoinhibition
- fe-sod
- juncea
- synthesis
- analysis
- agriculture
-
phytoremediation
-
ros-scavenging
The taxonomic range for the selected organisms is: Glycine max
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
ascorbate peroxidase, apex2, cytosolic ascorbate peroxidase, lmapx, ascorbate peroxidase 2, l-ascorbate peroxidase, ascorbate peroxidase 1, ascorbic acid peroxidase, osapx8, osapx2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ascorbate peroxidase
-
-
-
-
ascorbic acid peroxidase
-
-
-
-
L-ascorbic acid peroxidase
-
-
-
-
L-ascorbic acid-specific peroxidase
-
-
-
-
peroxidase, ascorbate
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 L-ascorbate + H2O2 + 2 H+ = 2 monodehydroascorbate + 2 H2O
mechanism for electron transfer
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
peroxidation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -
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
72906-87-7
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,2'-azino-di-(3-ethyl-benzothiazoline-(6)-sulfonic acid) + H2O2
? + H2O
-
3% relative activity to L-ascorbate
-
?
o-dianisidine + H2O2
?
-
reaction rate approximately equal to the rate with L-ascorbate
-
?
additional information
?
-
-
no activity with: NAD(P)H, reduced glutathione or urate
-
-
?
guaiacol + H2O2
?
-
the reaction rate is approximately equal to the rate with L-ascorbate
-
?
guaiacol + H2O2
?
-
recombinant enzyme 1: 6% activity relative to L-ascorbate, recombinant enzyme 2: 11% relative activity to L-ascorbate
-
?
L-ascorbate + H2O2
dehydroascorbate + 2 H2O
-
the enzyme is responsible for most H2O2 removal outside of peroxisomes in root nodules
-
?
L-ascorbate + H2O2
dehydroascorbate + 2 H2O
-
physiological role of the enzyme: removal of H2O2, prevention of H2O2 accumulation
-
?
pyrogallol + H2O2
3-hydroxybenzo-1,2-quinone + H2O
-
the reaction rate is 38-fold higher than the rate with L-ascorbate
-
?
pyrogallol + H2O2
3-hydroxybenzo-1,2-quinone + H2O
-
recombinant enzyme 1: 355% activity relative to L-ascorbate, recombinant enzyme 2: 304% activity relative to L-ascorbate
-
?
pyrogallol + H2O2
3-hydroxybenzo-1,2-quinone + H2O
-
723% activity relative to L-ascorbate
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-ascorbate + H2O2
dehydroascorbate + 2 H2O
-
the enzyme is responsible for most H2O2 removal outside of peroxisomes in root nodules
-
?
L-ascorbate + H2O2
dehydroascorbate + 2 H2O
-
physiological role of the enzyme: removal of H2O2, prevention of H2O2 accumulation
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
electronic, EPR, and NMR spectra are consistent with a high-spin ferric resting state for the enzyme at 298K, low temperature EPR and electronic absorption experiments indicate formation of a low-spin heme derivative at these temperatures, the midpoint reduction potential for the Fe(III)/Fe(II) redox couple, determined by spectroelectrochemistry is -159 mV vs SHE, sodium phosphate: pH 7, 25°C, 0.10 M
-
heme
covalent linking of Trp41 to the heme group in ascorbate peroxidase can occur on exposure of the enzyme to peroxide. A reaction mechanism involving formation of a protein radical at Trp41 is implicated to account for this observation
heme
-
determination of the redox potential for the Fe3+/Fe2+, CI/Fe3+, CI/II, and CII/Fe3+ redox couples in rsAPX and various site-directed variants by direct potentiometric titration
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
hydroxylamine
-
recombinant enzyme 1: 74% inhibition at 1 mM and 100% inhibition at 10 mM, recombinant enzyme 2: 86% inhibition at 1 mM and 100% inhibition at 10 mM
p-chloromercuriphenyl sulfonic acid
-
100% inhibition at 0.05 mM, recombinant enzyme 1 and 2
C2H2
-
recombinant enzyme 1: 94% inhibition at 0.1 ml per l, recombinant enzyme 2: 2% inhibition at 0.1 ml per l
KCN
-
recombinant enzyme 1: 69% inhibition at 0.1 mM and 100% inhibition at 0.5 mM, recombinant enzyme 2: 81% inhibition at 0.1 mM and 100% inhibition at 0.5 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
nitric oxide
-
causes an increase in the total enzymatic activity of ascorbate peroxidase. The nitric oxide-induced changes in ascorbate peroxidase enzymatic activity are coupled to altered nodule H2O2 content. Enzymatic activity of the largest isoform, Apx1 is upregulated by 11% in response to 5 microM of nitric oxide donor DETA/NO and 21% in response to 10 microM DETA/NO. 5 microM of DETA/NO increase the enzymatic activity of the second largest isoform Apx2 by about 57%. Treatment of nodulated soybean with 5 microM DETA/NO upregulates the smallest nodule isoform Apx3 enzymatic activity by 228% compared to untreated controls
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
the reaction does not follow Michaelis-Menten kinetics, Hill plots
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
cAPX 2 is involved in flooding stress responses in young soybean seedlings
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
the doublet in cytosolic enzyme activity observed in the native-PAGE of soybean leaf and root nodule extracts could represent either the products of two cytosolic soybean enzyme genes or a single gene product with some post-translational modification, the cultivar Roanoke has a single isozyme
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Q43758_SOYBN
250
0
27052
TrEMBL
other Location (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30000
30000
-
1 * 30000, SDS-PAGE, discrepancy to value from gel filtration probably due to enzyme conformation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
-
1 * 30000, SDS-PAGE, discrepancy to value from gel filtration probably due to enzyme conformation
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
W41A
the mutant is a six-coordinate heme peroxidase which has bis-histidine coordination, like a cytochrome, but that is catalytically active because the distal histidine reversibly dissociates to form a five-coordinate heme in response to binding of hydrogen peroxide
K14D/W41F/E112K/A134P
K14D/W41F/E112K/A134P
APEX2, i.e. engineered mutant of APX. APEX2 fused to a protein of interest covalently tags nearby proteins with biotin-phenol when H2O2 is added. High osmolarity and disruption of cell wall integrity permits live-cell biotin labeling in Schizosaccharomyces pombe and Saccharomyces cerevisiae, respectively. APEX2 permits targeted and proximity-dependent labeling of proteins
K14D/W41F/E112K/A134P
i.e. APEX2, engineered mutant of APX used for biotinylation of neighboring endogenous proteins. APEX labeling functions effectively in multiple Drosophila melanogaster tissues for different subcellular compartments and maps the mitochondrial matrix proteome of Drosophila muscle in different physiological conditions
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
49
-
melting temperature of the ferric derivative, monitored by circular dichroism spectroscopy
57
-
melting temperature of the ferric-cyanide derivative, monitored by circular dichroism spectroscopy
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C or -80°C, crude extracts of root nodules, 50 mM potassium phosphate buffer, pH 7.0, several months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
of recombinant enzyme 1: using column chromatography on DEAE Bio-Gel A agarose and column chromatography on Sephacryl S-300, of recombinant enzyme 2: using column chromatography on DEAE Bio-Gel A agarose, ammonium sulfate fractionation, dialysis, chromatofocusing on a polybuffer 94 exchanger and column chromatography on Sephacryl S-300
-
using ammonium sulfate precipitation, dialysis and column chromatography on DEAE, Sephacryl und hydroxyapatite
-
using Ni2+-agarose affinity chromatography and gel filtration after reconstitution with hemin
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cotransformation of a soybean cDNA library and the Bax gene into yeast cells, screening for expressed genes that prevent Bax-induced apoptosis, the soybean ascorbate peroxidase inhibits the generation of reactive oxygen species by Bax, which in turn suppresses Bax-induced cell death in yeast
-
expression in Escherichia coli, most of the enzyme produced is present in the apo-form, without heme
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
the apo-recombinant protein is easily converted to the holo-recombinant form by in vitro reconstitution with hemin
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
-
under flooding stress, Apx enzyme activity decreases and expression is not detected in 5- and 9-day-old seedlings treated with flooding. Under drought stress Apx activity gradually increases from 5-day-old till 9-day-old seedlings. The expression of Apx also increases from 5-day-old till 9-day-old soybean seedlings. Trends in Apx expressions both in hypocotyl and root of drought treated soybean seedlings are similar
analysis
analysis
APEX2, i.e. engineered mutant K14D/W41F/E112K/A134P of APX used for biotinylation of neighboring endogenous proteins, can be applicated for effective labeling in multiple Drosophila melanogaster tissues for different subcellular compartments and maps the mitochondrial matrix proteome of Drosophila muscle in different physiological conditions
analysis
APEX2, i.e. engineered mutant K14D/W41F/E112K/A134P of APX, fused to a protein of interest covalently tags nearby proteins with biotin-phenol when H2O2 is added. High osmolarity and disruption of cell wall integrity permits live-cell biotin labeling in Schizosaccharomyces pombe and Saccharomyces cerevisiae, respectively. APEX2 permits targeted and proximity-dependent labeling of proteins
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dalton, D.A.; Hanus, F.J.; Russell, S.A.; Evans, H.J.
Purification, properties, and distribution of ascorbate peroxidase in legume root nodules
Plant Physiol.
83
789-794
1987
Alnus rubra, Arachis hypogaea, Vicia faba, Glycine max, Medicago sativa, Lupinus albus, Pisum sativum, Trifolium subterraneum, Vicia sativa, Vigna unguiculata
Dalton, D.A.; Diaz del Castillo, L.; Kahn, M.L.; Joyner, S.L.; Chatfield, J.M.
Heterologous expression and characterization of soybean cytosolic ascorbate peroxidase
Arch. Biochem. Biophys.
328
1-8
1996
Glycine max
Caldwell, C.R.; Turano, F.J.; McMahon, M.B.
Identification of two cytosolic ascorbate peroxidase cDNAs from soybean leaves and characterization of their products by functional expression in E. coli
Planta
204
120-126
1998
Glycine max
Jones, D.K.; Dalton, D.A.; Rosell, F.I.; Raven, E.L.
Class I heme peroxidases: characterization of soybean ascorbate peroxidase
Arch. Biochem. Biophys.
360
173-178
1998
Glycine max
Moon, H.; Baek, D.; Lee, B.; Prasad, D.T.; Lee, S.Y.; Cho, M.J.; Lim, C.O.; Choi, M.S.; Bahk, J.; Kim, M.O.; Hong, J.C.; Yun, D.J.
Soybean ascorbate peroxidase suppresses Bax-induced apoptosis in yeast by inhibiting oxygen radical generation
Biochem. Biophys. Res. Commun.
290
457-462
2002
Glycine max
Sharp, K.H.; Mewies, M.; Moody, P.C.; Raven, E.L.
Crystal structure of the ascorbate peroxidase-ascorbate complex
Nat. Struct. Biol.
10
303-307
2003
Glycine max (Q43758)
Pipirou, Z.; Bottrill, A.R.; Metcalfe, C.M.; Mistry, S.C.; Badyal, S.K.; Rawlings, B.J.; Raven, E.L.
Autocatalytic formation of a covalent link between tryptophan 41 and the heme in ascorbate peroxidase
Biochemistry
46
2174-2180
2007
Glycine max (Q43758)
Efimov, I.; Papadopoulou, N.D.; McLean, K.J.; Badyal, S.K.; Macdonald, I.K.; Munro, A.W.; Moody, P.C.; Raven, E.L.
The redox properties of ascorbate peroxidase
Biochemistry
46
8017-8023
2007
Glycine max
Shi, F.; Yamamoto, R.; Shimamura, S.; Hiraga, S.; Nakayama, N.; Nakamura, T.; Yukawa, K.; Hachinohe, M.; Matsumoto, H.; Komatsu, S.
Cytosolic ascorbate peroxidase 2 (cAPX 2) is involved in the soybean response to flooding
Phytochemistry
69
1295-1303
2008
Glycine max (Q76LA8), Glycine max
Badyal, S.K.; Metcalfe, C.L.; Basran, J.; Efimov, I.; Moody, P.C.; Raven, E.L.
Iron oxidation state modulates active site structure in a heme peroxidase
Biochemistry
47
4403-4409
2008
Glycine max (Q43758)
Kausar, R.; Hossain, Z.; Makino, T.; Komatsu, S.
Characterization of ascorbate peroxidase in soybean under flooding and drought stresses
Mol. Biol. Rep.
39
10573-10579
2012
Glycine max
Keyster, M.; Klein, A.; Egbichi, I.; Jacobs, A.; Ludidi, N.
Nitric oxide increases the enzymatic activity of three ascorbate peroxidase isoforms in soybean root nodules
Plant Signal. Behav.
6
38-43
2011
Glycine max
Hwang, J.; Espenshade, P.J.
Proximity-dependent biotin labelling in yeast using the engineered ascorbate peroxidase APEX2
Biochem. J.
473
2463-2469
2016
Glycine max (Q76LA6)
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