Information on EC 1.11.1.11 - L-ascorbate peroxidase:
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The expected taxonomic range for this enzyme is: Magnoliophyta

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EC NUMBERCOMMENTARY
1.11.1.11-

RECOMMENDED NAMEGeneOntology No.
L-ascorbate peroxidaseGO:0016688

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
2 L-ascorbate + H2O2 + 2 H+ = 2 monodehydroascorbate + 2 H2O
show the reaction diagram		(1a)---
2 L-ascorbate + H2O2 + 2 H+ = 2 monodehydroascorbate + 2 H2O
show the reaction diagram		mechanism involves accumulation of a transient enzyme intermediatePisum sativum-655435
2 L-ascorbate + H2O2 + 2 H+ = 2 monodehydroascorbate + 2 H2O
show the reaction diagram		mechanismPisum sativum-655789
2 L-ascorbate + H2O2 + 2 H+ = 2 monodehydroascorbate + 2 H2O
show the reaction diagram		mechanism, structural hints to instability during catalysisNicotiana tabacum-655921
2 L-ascorbate + H2O2 + 2 H+ = 2 monodehydroascorbate + 2 H2O
show the reaction diagram		mechanism; mechanism for electron transferGlycine maxQ43758656853
2 L-ascorbate + H2O2 + 2 H+ = L-ascorbate + L-dehydroascorbate + 2 H2O
show the reaction diagram		overall reaction---
2 monodehydroascorbate = L-ascorbate + L-dehydroascorbate
show the reaction diagram		spontaneous---

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
oxidation----
oxidationSaccharomyces cerevisiae--696216
oxidationStylosanthes guianensis--696567
oxidationHordeum vulgare--697013
oxidationLeishmania major 5ASKH, Leishmania major Friedlin, Leishmania major Friedlin V9, Leishmania major LV-39, Leishmania major LV39, Leishmania major MHOM/IL/80/Friedlin, Leishmania major MHOM/IL/81, Leishmania major MHOM/IL/81/Friedlin, Leishmania major MRHO/IR/75/ER, Leishmania major V1--697682
oxidationLeishmania major--697682, 698047
oxidationCenchrus americanusA4ZYP9-699802
oxidationSolanum lycopersicumQ09Y74, Q09Y76, Q09Y77, Q09Y78, Q3I5C3, Q3I5C4, Q3SC88-700220
oxidationSolanum pennellii--700220
oxidationEmbryophyta--700626
oxidationPopulus tomentosa--700703
oxidationArabidopsis thaliana--698848, 700728
oxidationCyanidioschyzon merolae, Cyanidioschyzon merolae CMA035C--700728
oxidationGossypium hirsutumA7KIX5, C6ZDA9, C6ZDB0, Q39780-700842
oxidationOryza sativa--700843
peroxidation----
redox reaction----
reduction----
reductionSaccharomyces cerevisiae--696216
reductionStylosanthes guianensis--696567
reductionHordeum vulgare--697013
reductionLeishmania major--697682, 698047
reductionCenchrus americanusA4ZYP9-699802
reductionSolanum lycopersicumQ09Y74, Q09Y76, Q09Y77, Q09Y78, Q3I5C3, Q3I5C4, Q3SC88-700220
reductionSolanum pennellii--700220
reductionEmbryophyta--700626
reductionPopulus tomentosa--700703
reductionArabidopsis thaliana--698848, 700728
reductionCyanidioschyzon merolae, Cyanidioschyzon merolae CMA035C--700728
reductionGossypium hirsutumA7KIX5, C6ZDA9, C6ZDB0, Q39780-700842
reductionOryza sativa--700843

PATHWAYKEGG LinkMetaCyc Link
Ascorbate and aldarate metabolism00053 -
Glutathione metabolism00480 -
L-ascorbate degradation II (bacterial, aerobic)-PWY-6961
L-ascorbate degradation III-PWY-6960
L-ascorbate degradation V-PWY-6959

SYSTEMATIC NAMEIUBMB Comments
L-ascorbate:hydrogen-peroxide oxidoreductaseA 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-enzymatic disproportionation to ascorbate and dehydroascorbate.

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
Am-pAPX1Avicennia marinaA7LIY1-689652
APOXRiccia fluitans--694642
APXNicotiana tabacum--686710
APXSaccharum officinarum--689350
APXSaccharomyces cerevisiae--696216
APXGlycine max--696257
APXStylosanthes guianensis--696567
APXHordeum vulgare--697013
APXSolanum pennellii--700220
APXEmbryophyta--700626
APXGossypium hirsutumA7KIX5, C6ZDA9, C6ZDB0, Q39780-700842
APXPopulus simonii x Populus pyramidalis--710779
APXBrassica napusC5IUM6-710788
APXEuglena gracilis--711139
APXDunaliella salina--713220
APXPallavicinia lyellii--713299
APX 1Oryza sativa--657113
APX 2Oryza sativa--657113
APX1Arabidopsis thaliana--698848
APX1Solanum lycopersicumQ09Y74, Q09Y76, Q09Y77, Q09Y78, Q3I5C3, Q3I5C4, Q3SC88-700220
APX1Gossypium hirsutumA7KIX5, C6ZDA9, C6ZDB0, Q39780-700842
APX1Hordeum vulgareO23983, Q945R5isoform713234
APX2Solanum lycopersicumQ09Y74, Q09Y76, Q09Y77, Q09Y78, Q3I5C3, Q3I5C4, Q3SC88-700220
APX2Gossypium hirsutumA7KIX5, C6ZDA9, C6ZDB0, Q39780-700842
APX2Hordeum vulgareO23983, Q945R5isoform713234
APX3Solanum lycopersicumQ09Y74, Q09Y76, Q09Y77, Q09Y78, Q3I5C3, Q3I5C4, Q3SC88-700220
APX4Solanum lycopersicumQ09Y74, Q09Y76, Q09Y77, Q09Y78, Q3I5C3, Q3I5C4, Q3SC88-700220
APX5Solanum lycopersicumQ09Y74, Q09Y76, Q09Y77, Q09Y78, Q3I5C3, Q3I5C4, Q3SC88-700220
APX6Solanum lycopersicumQ09Y74, Q09Y76, Q09Y77, Q09Y78, Q3I5C3, Q3I5C4, Q3SC88-700220
APX7Solanum lycopersicumQ09Y74, Q09Y76, Q09Y77, Q09Y78, Q3I5C3, Q3I5C4, Q3SC88-700220
APx8Oryza sativa--700843
ascorbate peroxidase----
ascorbate peroxidaseSaccharomyces cerevisiae--696216
ascorbate peroxidaseGlycine max--696257
ascorbate peroxidaseStylosanthes guianensis--696567
ascorbate peroxidaseHordeum vulgare--697013
ascorbate peroxidaseLeishmania major--697682, 698047
ascorbate peroxidaseCenchrus americanusA4ZYP9-699802
ascorbate peroxidaseSolanum pennellii--700220
ascorbate peroxidaseEmbryophyta--700626
ascorbate peroxidaseArabidopsis thaliana, Cyanidioschyzon merolae--700728
ascorbate peroxidaseGossypium hirsutumA7KIX5, C6ZDA9, C6ZDB0, Q39780; 700842
ascorbate peroxidasePopulus simonii x Populus pyramidalis--710779
ascorbate peroxidaseBrassica napusC5IUM6-710788
ascorbate peroxidaseEuglena gracilis--711139
ascorbate peroxidaseDunaliella salina--713220
ascorbate peroxidaseHordeum vulgareO23983, Q945R5; 713234
ascorbate peroxidasePallavicinia lyellii--713299
ascorbate peroxidase 1Oryza sativaP0C0L0, P0C0L1, Q0JEQ2, Q10N21, Q69SV0, Q6ZJJ1, Q7XJ02, Q9FE01-688083
ascorbate peroxidase 1Arabidopsis thaliana--698848
ascorbate peroxidase 1Solanum lycopersicumQ09Y74, Q09Y76, Q09Y77, Q09Y78, Q3I5C3, Q3I5C4, Q3SC88-700220
ascorbate peroxidase 1Gossypium hirsutumA7KIX5, C6ZDA9, C6ZDB0, Q39780-700842
ascorbate peroxidase 2Oryza sativaP0C0L0, P0C0L1, Q0JEQ2, Q10N21, Q69SV0, Q6ZJJ1, Q7XJ02, Q9FE01-688083
ascorbate peroxidase 2Glycine maxQ76LA8-689427
ascorbate peroxidase 2Solanum lycopersicumQ09Y74, Q09Y76, Q09Y77, Q09Y78, Q3I5C3, Q3I5C4, Q3SC88-700220
ascorbate peroxidase 2Gossypium hirsutumA7KIX5, C6ZDA9, C6ZDB0, Q39780-700842
ascorbate peroxidase 3Oryza sativaP0C0L0, P0C0L1, Q0JEQ2, Q10N21, Q69SV0, Q6ZJJ1, Q7XJ02, Q9FE01-688083
ascorbate peroxidase 3Solanum lycopersicumQ09Y74, Q09Y76, Q09Y77, Q09Y78, Q3I5C3, Q3I5C4, Q3SC88-700220
ascorbate peroxidase 4Oryza sativaP0C0L0, P0C0L1, Q0JEQ2, Q10N21, Q69SV0, Q6ZJJ1, Q7XJ02, Q9FE01-688083
ascorbate peroxidase 4Solanum lycopersicumQ09Y74, Q09Y76, Q09Y77, Q09Y78, Q3I5C3, Q3I5C4, Q3SC88-700220
ascorbate peroxidase 5Oryza sativaP0C0L0, P0C0L1, Q0JEQ2, Q10N21, Q69SV0, Q6ZJJ1, Q7XJ02, Q9FE01-688083
ascorbate peroxidase 5Solanum lycopersicumQ09Y74, Q09Y76, Q09Y77, Q09Y78, Q3I5C3, Q3I5C4, Q3SC88-700220
ascorbate peroxidase 6Oryza sativaP0C0L0, P0C0L1, Q0JEQ2, Q10N21, Q69SV0, Q6ZJJ1, Q7XJ02, Q9FE01-688083
ascorbate peroxidase 6Solanum lycopersicumQ09Y74, Q09Y76, Q09Y77, Q09Y78, Q3I5C3, Q3I5C4, Q3SC88-700220
ascorbate peroxidase 7Oryza sativaP0C0L0, P0C0L1, Q0JEQ2, Q10N21, Q69SV0, Q6ZJJ1, Q7XJ02, Q9FE01-688083
ascorbate peroxidase 7Solanum lycopersicumQ09Y74, Q09Y76, Q09Y77, Q09Y78, Q3I5C3, Q3I5C4, Q3SC88-700220
ascorbate peroxidase 8Oryza sativa--688083, 700843
ascorbic acid peroxidase----
AtstAPXArabidopsis thaliana--700728
cAPX 2Glycine maxQ76LA8-689427
CmstAPXCyanidioschyzon merolae--700728
cytoplasmic ascorbate peroxidase 1Cenchrus americanusA4ZYP9-699802
cytosolic ascorbate peroxidaseArabidopsis thaliana--698848
GhAPX1Gossypium hirsutumA7KIX5-689240
glyoxysomal APXGossypium hirsutumA7KIX5, C6ZDA9, C6ZDB0, Q39780-700842
HvAPX1Hordeum vulgare--697013
L-ascorbate peroxidaseRiccia fluitans--694642
L-ascorbic acid peroxidase----
L-ascorbic acid-specific peroxidase----
LmAPXLeishmania major--685400, 697682, 698047
OsAPx1Oryza sativaP0C0L0, P0C0L1, Q0JEQ2, Q10N21, Q69SV0, Q6ZJJ1, Q7XJ02, Q9FE01-688083
OsAPx2Oryza sativaP0C0L0, P0C0L1, Q0JEQ2, Q10N21, Q69SV0, Q6ZJJ1, Q7XJ02, Q9FE01-688083
OsAPx3Oryza sativaP0C0L0, P0C0L1, Q0JEQ2, Q10N21, Q69SV0, Q6ZJJ1, Q7XJ02, Q9FE01-688083
OsAPx4Oryza sativaP0C0L0, P0C0L1, Q0JEQ2, Q10N21, Q69SV0, Q6ZJJ1, Q7XJ02, Q9FE01-688083
OsAPx5Oryza sativaP0C0L0, P0C0L1, Q0JEQ2, Q10N21, Q69SV0, Q6ZJJ1, Q7XJ02, Q9FE01-688083
OsAPx6Oryza sativaP0C0L0, P0C0L1, Q0JEQ2, Q10N21, Q69SV0, Q6ZJJ1, Q7XJ02, Q9FE01-688083
OsAPx7Oryza sativaP0C0L0, P0C0L1, Q0JEQ2, Q10N21, Q69SV0, Q6ZJJ1, Q7XJ02, Q9FE01-688083
OsAPx8Oryza sativa--688083, 700843
OsAPXaOryza sativaQ10N21, Q9FE01-689513
OsAPXbOryza sativaQ10N21, Q9FE01-689513
pAPXHordeum vulgare--697013
peroxidase, ascorbate----
peroxisomal ascorbate peroxidasePopulus tomentosa--700703
PgAPX1Cenchrus americanusA4ZYP9-699802
PpAPXPopulus tomentosaQ5S1V5-688913, 700703
sAPXArabidopsis thalianaQ42592, Q42593-685002
stromal APXGossypium hirsutumA7KIX5, C6ZDA9, C6ZDB0, Q39780-700842
stromal ascorbate peroxidaseArabidopsis thaliana--685002, 700728
stromal ascorbate peroxidaseCyanidioschyzon merolae--700728
TaAPXTriticum aestivum--657053
tAPXArabidopsis thalianaQ42592, Q42593-685002
thylakoid-bound ascorbate peroxidaseArabidopsis thalianaQ42592, Q42593-685002

CAS REGISTRY NUMBERCOMMENTARY
72906-87-7-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Alnus rubra-439855--Manually annotated by BRENDA team
Arabidopsis sp.-685676--Manually annotated by BRENDA team
Arabidopsis thaliana-698848, 700728--Manually annotated by BRENDA team
Arabidopsis thalianaecotype Columbia685002Q42592, Q42593SwissProtManually annotated by BRENDA team
Arabidopsis thalianagrowth at 14°C, decrease in membrane-bound enzyme activity, increase in total chlorophyll, growth at 22°C, increase in membrane-bound enzyme activity, and decrease in total chlorophyll. Before flowering, significantly negative correlation of membrane-bound enzyme with flowering time. Soluble enzyme shows irregular pattern of growth656620--Manually annotated by BRENDA team
Arabidopsis thalianaoverexpression of thylakoidal isozyme657008--Manually annotated by BRENDA team
Arabidopsis thalianawild type plants and plants overexpressing heat shock transcription factor 3, following heat stress, enzyme activity in wild type increased due to induction of a thermostable isoform probably identical with APX2, in transgenic plants, the thermostable isoform was detectable at normal temperature and persisted after severe heat stress at 44°C657041--Manually annotated by BRENDA team
Arachis hypogaea-439855--Manually annotated by BRENDA team
Avicennia marina-689652A7LIY1UniprotManually annotated by BRENDA team
Brassica napuscytoplasmic male sterility line710788C5IUM6UniProtManually annotated by BRENDA team
Brassica rapa-439865--Manually annotated by BRENDA team
Camellia sinensistea439870--Manually annotated by BRENDA team
Cenchrus americanus-699802A4ZYP9UniProtManually annotated by BRENDA team
Chlamydomonas sp.W80 strain439874Q9SXL5UniprotManually annotated by BRENDA team
Chlamydomonas sp. W80-685676Q9SXL5UniprotManually annotated by BRENDA team
Chlorella vulgaris-439871--Manually annotated by BRENDA team
Crocus sativusL. corm654139--Manually annotated by BRENDA team
Cyanidioschyzon merolae-700728--Manually annotated by BRENDA team
Dunaliella salina-713220--Manually annotated by BRENDA team
Dunaliella salina IR-1 and Gh-U-713220--Manually annotated by BRENDA team
Embryophyta-700626--Manually annotated by BRENDA team
Eremosphaera viridis-439859--Manually annotated by BRENDA team
Euglena gracilis-439857, 439858, 711139--Manually annotated by BRENDA team
Euglena gracilis-685676Q8LP26UniprotManually annotated by BRENDA team
Galdieria partita-439876, 439881, 685676, 686710--Manually annotated by BRENDA team
Galdieria sulphuraria-685676--Manually annotated by BRENDA team
Glycine max-685131, 696257Q43758SwissProtManually annotated by BRENDA team
Glycine max; expression in Escherichia coli656853Q43758SwissProtManually annotated by BRENDA team
Glycine maxcultivar Enrei689427Q76LA8UniprotManually annotated by BRENDA team
Glycine maxrecombinant685177--Manually annotated by BRENDA team
Glycine maxsoybean439855, 439864, 439869, 439872, 439878--Manually annotated by BRENDA team
Gossypium hirsutum-700842A7KIX5SwissProtManually annotated by BRENDA team
Gossypium hirsutum-700842C6ZDA9, C6ZDB0, Q39780UniProtManually annotated by BRENDA team
Gossypium hirsutumL. cv. Xuzhou 142689240A7KIX5SwissProtManually annotated by BRENDA team
Helicoverpa zealarvae439867--Manually annotated by BRENDA team
Hordeum vulgare-697013--Manually annotated by BRENDA team
Hordeum vulgare-713234O23983, Q945R5UniProtManually annotated by BRENDA team
Leishmania major-685400, 697682--Manually annotated by BRENDA team
Leishmania major-685676Q4Q3K2UniprotManually annotated by BRENDA team
Leishmania majorstrain 5ASKH698047--Manually annotated by BRENDA team
Leishmania major 5ASKHstrain 5ASKH698047--Manually annotated by BRENDA team
Lupinus albuslow activity439855--Manually annotated by BRENDA team
Medicago sativaalfalfa439855--Manually annotated by BRENDA team
Nicotiana tabacum-439863, 439870, 655921--Manually annotated by BRENDA team
Nicotiana tabacum-686657, 686710Q9TNL9SwissProtManually annotated by BRENDA team
Nicotiana tabacumBright-Yellow 2 cells, decrease in enzyme amount and activity upon heat shock leading to programmed cell death657063--Manually annotated by BRENDA team
Nicotiana tabacumrecombinant enzyme684930Q9TNL9SwissProtManually annotated by BRENDA team
Oryza sativa-656625--Manually annotated by BRENDA team
Oryza sativa-689513Q10N21, Q9FE01SwissProtManually annotated by BRENDA team
Oryza sativachloroplast; cv. Taichung Native 1688083Q69SV0SwissProtManually annotated by BRENDA team
Oryza sativacv. Taichung Native 1688083P0C0L0, P0C0L1, Q0JEQ2, Q6ZJJ1, Q7XJ02SwissProtManually annotated by BRENDA team
Oryza sativacytosol; cv. Taichung Native 1688083Q10N21, Q9FE01SwissProtManually annotated by BRENDA team
Oryza sativaeight types of APx have been desribed in Oryza sativa, two cytosolic, OsAPx1 and OsAPx2, two putative peroxisomal, OsAPx3 and OsAPx4, and four chloroplastic isoforms OsAPx5, OsAPx6, OsAPx7 and OsAPx8700843--Manually annotated by BRENDA team
Oryza sativaisoforms APX 1, APX 2657113--Manually annotated by BRENDA team
Pallavicinia lyellii-713299--Manually annotated by BRENDA team
Pisum sativum-439862, 439866, 655435--Manually annotated by BRENDA team
Pisum sativumcv Alaska and cv Austrian winter; pea439855--Manually annotated by BRENDA team
Pisum sativumcv. Puget656405--Manually annotated by BRENDA team
Pisum sativumpea439859, 439873, 439877--Manually annotated by BRENDA team
Pisum sativumpea; var. Kleine Rheinlaenderin439856--Manually annotated by BRENDA team
Pisum sativumrecombinant enzyme655789--Manually annotated by BRENDA team
Populus simonii x Populus pyramidalisvariant Opera 8277710779--Manually annotated by BRENDA team
Populus tomentosa-688913, 700703Q5S1V5SwissProtManually annotated by BRENDA team
Raphanus sativus-439868--Manually annotated by BRENDA team
Riccia fluitans-694642--Manually annotated by BRENDA team
Ricinus communis-654378--Manually annotated by BRENDA team
Saccharomyces cerevisiae-696216--Manually annotated by BRENDA team
Saccharum officinarum-689350--Manually annotated by BRENDA team
Solanum lycopersicumcv. M82700220Q09Y77, Q3I5C3UniProtManually annotated by BRENDA team
Solanum lycopersicumfragment; cv. M82700220Q09Y74, Q09Y76, Q09Y78, Q3SC88UniProtManually annotated by BRENDA team
Solanum lycopersicumMill. cv. Lichun688200--Manually annotated by BRENDA team
Solanum lycopersicumSolanum lycopersicum cv. M82700220Q3I5C4UniProtManually annotated by BRENDA team
Solanum pennelliiSolanum pennellii acc. Atico700220--Manually annotated by BRENDA team
Solanum tuberosum-439875--Manually annotated by BRENDA team
Spinacia oleraceaspinach439859, 439860--Manually annotated by BRENDA team
Stylosanthes guianensis-696567--Manually annotated by BRENDA team
Trifolium subterraneum-439855--Manually annotated by BRENDA team
Triticum aestivum-439859--Manually annotated by BRENDA team
Triticum aestivumthree isozymes657053--Manually annotated by BRENDA team
Trypanosoma cruzi-439880, 685676Q8I1N3UniprotManually annotated by BRENDA team
Vicia faba-439855--Manually annotated by BRENDA team
Vicia sativa-439855--Manually annotated by BRENDA team
Vigna unguiculata-439855--Manually annotated by BRENDA team
Zea mays-439861, 439879--Manually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
physiological functionEuglena gracilis 1224-5/25, Euglena gracilis 1224-5/9, Euglena gracilis, Euglena gracilis mutant, Euglena gracilis SM-ZK, Euglena gracilis Z-APX is physiologically important to the metabolism of H2O2711139

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY/
Substrate		 LITERATURE/
Substrate		 COMMENTARY/
Product		 LITERATURE/
Product		 Reversibility
r=reversible
ir=irreversible
?=not specified
2,2'-azino-di-(3-ethyl-benzothiazoline-(6)-sulfonic acid) + H2O2? + H2O
show the reaction diagram		Glycine max-3% relative activity to L-ascorbate439864-439864?
2,2'-azino-di-[3-ethylbenzothiazoline-(6)-sulfonic acid] + H2O2?
show the reaction diagram		Vicia faba, Vicia sativa, Pisum sativum, Glycine max, Arachis hypogaea, Medicago sativa, Lupinus albus, Vigna unguiculata, Trifolium subterraneum, Alnus rubra--439855--?
2,2'-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2?
show the reaction diagram		Pallavicinia lyellii-cytosolic ascorbate peroxidase shows 3% activity compared to L-ascorbate, in the presence of 0.1 mM H2O2 and 3.6% activity compared to L-ascorbate in the presence of 0.5 mM H2O2713299--?
cysteine + H2O2? + H2O
show the reaction diagram		Helicoverpa zea-enzyme partially purified from whole body homogenate, 40% of the activity with L-ascorbate439867-439867?
Cytochrome c + H2O?
show the reaction diagram		Leishmania major--685400--?
cytochrome c + H2O2? + H2O
show the reaction diagram		Euglena gracilis-no activity439857, 439858---
cytochrome c + H2O2? + H2O
show the reaction diagram		Chlamydomonas sp.Q9SXL5no activity439874---
cytochrome c + H2O2? + H2O
show the reaction diagram		Raphanus sativus-no activity439868---
cytochrome c + H2O2? + H2O
show the reaction diagram		Chlorella vulgaris-no activity439871---
cytochrome c + H2O2? + H2O
show the reaction diagram		Brassica rapa-no activity439865---
cytochrome c + H2O2? + H2O
show the reaction diagram		Helicoverpa zea-enzyme partially purified from whole body homogenate, 44% of the activity with L-ascorbate439867-439867?
cytochrome c + H2O2?
show the reaction diagram		Leishmania major-able to use both ascorbate and cytochrome c as reducing electron donors697682--?
D-araboascorbic acid + H2O2dehydroascorbate + H2O
show the reaction diagram		Euglena gracilis-56% activity relative to L-ascorbate439858-439858?
D-iso-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Chlamydomonas sp.Q9SXL5native enzyme: the activity with D-isoascorbate corresponds to 131% of that found with ascorbate, recombinant enzyme: the activity with D-isoascorbate corresponds to 129% of that found with ascorbate439874-439874?
D-isoascorbate + H2O2?
show the reaction diagram		Euglena gracilis-60.3% activity compared to L-ascorbate711139--?
dihydrorhodamine 123 + H2O2?
show the reaction diagram		Leishmania major-assay, peroxidase substrate698047--?
ethyl phenyl sulfide + H2O2? + H2O
show the reaction diagram		Pisum sativum--439877--?
ferrocyanide + H2O2ferricyanide + H2O
show the reaction diagram		Pisum sativum-the Cys32Ser mutation has little effect on the kinetics of ferrocyanide turnover, but the DTNB modification decreases activity by approximately 90% at 300 mM ferrocyanide439873-439873?
glutathione + H2O2? + H2O
show the reaction diagram		Euglena gracilis-no activity439857---
glutathione + H2O2? + H2O
show the reaction diagram		Glycine max-no activity439855---
glutathione + H2O2? + H2O
show the reaction diagram		Chlamydomonas sp.Q9SXL5no activity439874---
glutathione + H2O2? + H2O
show the reaction diagram		Chlorella vulgaris-no activity439871---
glutathione + H2O2? + H2O
show the reaction diagram		Brassica rapa-no activity439865---
glutathione + H2O2? + H2O
show the reaction diagram		Helicoverpa zea-enzyme partially purified from whole body homogenate: 22% of the activity with L-ascorbate, enzyme partially purified from regurgitant: 0% relative activity to L-ascorbate, when assayed at the same concentration439867-439867?
glutathione + H2O2? + H2O
show the reaction diagram		Oryza sativa-30% of the activity with ascorbate, APX 1, 13% of the activity with ascorbate, APX 2657113--?
GSSG + H2O2?
show the reaction diagram		Gossypium hirsutumA7KIX5about 20% of the activity with L-ascorbate689240--?
guaiacol + H2O2?
show the reaction diagram		Pisum sativum--439855-439855?
guaiacol + H2O2?
show the reaction diagram		Leishmania major--685400--?
guaiacol + H2O2?
show the reaction diagram		Raphanus sativus-no activity439868---
guaiacol + H2O2?
show the reaction diagram		Chlorella vulgaris-no activity439871---
guaiacol + H2O2?
show the reaction diagram		Helicoverpa zea-no activity439867---
guaiacol + H2O2?
show the reaction diagram		Brassica rapa-no reaction439865---
guaiacol + H2O2?
show the reaction diagram		Solanum tuberosum-the activity is lower than with L-ascorbate439875-439875?
guaiacol + H2O2?
show the reaction diagram		Spinacia oleracea-low activity compared to L-ascorbate439860-439860?
guaiacol + H2O2?
show the reaction diagram		Pisum sativum-the DTNB-modified enzyme exhibits full activity439873-439873?
guaiacol + H2O2?
show the reaction diagram		Glycine max-30.5% activity relative to L-ascorbate439864-439864?
guaiacol + H2O2?
show the reaction diagram		Glycine max-the reaction rate is approximately equal to the rate with L-ascorbate439855-439855?
guaiacol + H2O2?
show the reaction diagram		Zea mays-poor electron donor439861-439861?
guaiacol + H2O2?
show the reaction diagram		Glycine max-recombinant enzyme 1: 6% activity relative to L-ascorbate, recombinant enzyme 2: 11% relative activity to L-ascorbate439869-439869?
guaiacol + H2O2?
show the reaction diagram		Pisum sativum-form C enzyme, only onesixteenth the rate observed with L-ascorbate439856-439856?
guaiacol + H2O2?
show the reaction diagram		Euglena gracilis-8% activity relative to L-ascorbate439858-439858?
guaiacol + H2O2?
show the reaction diagram		Chlamydomonas sp.Q9SXL5native enzyme: the activity corresponds to 7.2% of that found with L-ascorbate, recombinant enzyme: the activity corresponds to 8% of that found with L-ascorbate439874-439874?
guaiacol + H2O2?
show the reaction diagram		Gossypium hirsutumA7KIX5about 30% of the activity with L-ascorbate689240--?
guaiacol + H2O2?
show the reaction diagram		Pallavicinia lyellii-cytosolic ascorbate peroxidase shows 12% activity compared to L-ascorbate, in the presence of 0.1 mM H2O2 and 24.7% activity compared to L-ascorbate in the presence of 0.5 mM H2O2713299--?
guaiacol + H2O2? + H2O
show the reaction diagram		Pisum sativum--655435--?
guaiacol + H2O2? + H2O
show the reaction diagram		Ricinus communis-20% of the activity with ascorbate654378--?
guaiacol + H2O2? + H2O
show the reaction diagram		Oryza sativa-45% of the activity with ascorbate, APX 1, 15% of the activity with ascorbate, APX 2657113--?
iodide + H2O2?
show the reaction diagram		Euglena gracilis-2.3% activity relative to L-ascorbate439858-439858?
isopropyl phenyl sulfide + H2O2? + H2O
show the reaction diagram		Pisum sativum--439877-439877-
L-ascorbate + cumene hydroperoxide?
show the reaction diagram		Euglena gracilis-8.0% activity compared to H2O2711139--?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Vicia faba, Vicia sativa--439855-439855?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Saccharomyces cerevisiae--696216--?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Euglena gracilis--439857-439857?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Hordeum vulgare--697013--?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Spinacia oleracea--439859-439859?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Spinacia oleracea--439860-439860?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Pisum sativum--439855-439855?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Pisum sativum--439856-439856?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Pisum sativum--439859-439859?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Pisum sativum--439862-439862?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Pisum sativum--439877-439877?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Pisum sativum--655789--?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Zea mays--439861-439861?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Nicotiana tabacum--439863-439863?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Nicotiana tabacum--439870-439870?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Nicotiana tabacum--657063--?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Nicotiana tabacumQ9TNL9-686657--?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Nicotiana tabacum--686710--?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Glycine max--439855-439855?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Glycine max--439864-439864?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Glycine max--439869-439869?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Glycine max--439872-439872?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Glycine maxQ43758-685131--?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Glycine maxQ76LA8-689427--?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Arabidopsis thaliana--698848, 700728--?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Camellia sinensis--439870-439870?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Arachis hypogaea, Medicago sativa--439855-439855?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Ricinus communis--654378--?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Trypanosoma cruziQ8I1N3-439880-439880?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Lupinus albus--439855-439855?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Embryophyta--700626--?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Oryza sativa--657113, 700843--?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Chlorella vulgaris--439871-439871?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Vigna unguiculata--439855-439855?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Leishmania major--685400, 697682, 698047--?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Dunaliella salina--713220--?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Saccharum officinarum--689350--?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Trifolium subterraneum, Alnus rubra--439855-439855?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Galdieria partita--439876-439876?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Galdieria partita--439881-439881?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Galdieria partita--686710--?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Cyanidioschyzon merolae--700728--?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Crocus sativus--654139--?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Populus tomentosaQ5S1V5-688913--?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Populus tomentosa--700703--?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Gossypium hirsutumA7KIX5-689240, 700842--?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Gossypium hirsutumC6ZDA9, C6ZDB0, Q39780-700842--?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Oryza sativaQ10N21, Q9FE01-689513--?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Nicotiana tabacumQ9TNL9-684930--?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Solanum pennellii--700220--?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Stylosanthes guianensis--696567--?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Solanum lycopersicumQ09Y74, Q09Y76, Q09Y77, Q09Y78, Q3I5C3, Q3I5C4, Q3SC88-700220--?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Glycine max--696257--?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Cenchrus americanusA4ZYP9-699802--?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Populus simonii x Populus pyramidalis--710779--?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Brassica napusC5IUM6-710788--?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Hordeum vulgareO23983, Q945R5-713234--?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Solanum tuberosum-highly specific for439875-439875?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Euglena gracilis-tert-butyl hydroperoxide and cumene hydroperoxide also serve as electron acceptor439858-439858?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Helicoverpa zea-tert-butyl hydroperoxide and cumene hydroperoxide also serve as electron acceptor439867-439867?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Brassica rapa-L-ascorbate is the most effective natural electron donor439865-439865?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Helicoverpa zea-L-ascorbate is the most effective natural electron donor439867-439867?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Pisum sativum-the DTNB-modified enzyme exhibits only 1.3% wild-type activity when ascorbate is used as substrate, the DTNB-modified enzyme reacts normally with peroxide to give compound I but the rates of reduction of both compounds I and II by ascorbate are dramatically slowed. The Cys32Ser mutant has one-third wild-type activity. The ascorbate interactions with the enzyme are partly mediated through electrostatic interactions439873-439873?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Chlamydomonas sp.Q9SXL5native and recombinant enzyme, no activation is observed, when the enzyme is incubated with H2O2 under anaerobic conditions, thus one of the reasons for the stability mechanism in the enzyme may be the insusceptibility of compound I to H2O2439874-439874?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Pisum sativum-an equimolar mixture of native enzyme and H2O2 forms some transient compound I which, within 60 s is converted to compound II, addition of 5 mM ascorbate rapidly reduces compound II back to the native enzyme439866-439866?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Raphanus sativus-highly specific for L-ascorbate439868-439868?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Euglena gracilis-100% activity711139--?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Pallavicinia lyellii-cytosolic ascorbate peroxidase shows 100% activity in the presence of 0.1 mM and 0.5 mM H2O2713299--?
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Cyanidioschyzon merolae CMA035C--700728--?
L-ascorbate + H2O2dehydroascorbate + 2 H2O
show the reaction diagram		Pisum sativum--439855-439855?
L-ascorbate + H2O2dehydroascorbate + 2 H2O
show the reaction diagram		Brassica rapa--439865-439865?
L-ascorbate + H2O2dehydroascorbate + 2 H2O
show the reaction diagram		Riccia fluitans--694642--?
L-ascorbate + H2O2dehydroascorbate + 2 H2O
show the reaction diagram		Solanum tuberosum-role of the mitochondrial enzyme in the scanvenging of toxic oxygen species inside potato tuber mitochondria439875-439875?
L-ascorbate + H2O2dehydroascorbate + 2 H2O
show the reaction diagram		Euglena gracilis-the enzyme works for protection of cell membrane, by reducing the peroxide compounds generated endogenously from unsaturated fatty acids439858-439858?
L-ascorbate + H2O2dehydroascorbate + 2 H2O
show the reaction diagram		Helicoverpa zea-the enzyme may be important in removing H2O2 and lipid peroxides in insects439867-439867?
L-ascorbate + H2O2dehydroascorbate + 2 H2O
show the reaction diagram		Euglena gracilis-the enzyme appears to be the sole agent destroying H2O2439857-439857?
L-ascorbate + H2O2dehydroascorbate + 2 H2O
show the reaction diagram		Glycine max-the enzyme is responsible for most H2O2 removal outside of peroxisomes in root nodules439855-439855?
L-ascorbate + H2O2dehydroascorbate + 2 H2O
show the reaction diagram		Euglena gracilis-physiological role of the enzyme: removal of H2O2, prevention of H2O2 accumulation439857-439857?
L-ascorbate + H2O2dehydroascorbate + 2 H2O
show the reaction diagram		Euglena gracilis-physiological role of the enzyme: removal of H2O2, prevention of H2O2 accumulation439858-439858?
L-ascorbate + H2O2dehydroascorbate + 2 H2O
show the reaction diagram		Pisum sativum-physiological role of the enzyme: removal of H2O2, prevention of H2O2 accumulation439856-439856?
L-ascorbate + H2O2dehydroascorbate + 2 H2O
show the reaction diagram		Glycine max-physiological role of the enzyme: removal of H2O2, prevention of H2O2 accumulation439864-439864?
L-ascorbate + H2O2? + H2O
show the reaction diagram		Pisum sativum--655435--?
L-ascorbate + tert-butyl hydroperoxide?
show the reaction diagram		Euglena gracilis-17.4% activity compared to H2O2711139--?
L-ascorbic acid + cumene hydroperoxidedehydroascorbate + 1,1-dimethylbenzylalcohol + H2O
show the reaction diagram		Euglena gracilis--439858-439858?
L-ascorbic acid + cumene hydroperoxidedehydroascorbate + 1,1-dimethylbenzylalcohol + H2O
show the reaction diagram		Chlamydomonas sp.Q9SXL5no activity439874---
L-ascorbic acid + cumene hydroperoxidedehydroascorbate + 1,1-dimethylbenzylalcohol + H2O
show the reaction diagram		Chlorella vulgaris-no activity439871---
L-ascorbic acid + cumene hydroperoxidedehydroascorbate + 1,1-dimethylbenzylalcohol + H2O
show the reaction diagram		Helicoverpa zea-34% of the activity with H2O2439867-439867?
L-ascorbic acid + tert-butylhydroperoxidedehydroascorbate + tert-butylalcohol
show the reaction diagram		Euglena gracilis--439858-439858?
L-ascorbic acid + tert-butylhydroperoxidedehydroascorbate + tert-butylalcohol
show the reaction diagram		Chlamydomonas sp.Q9SXL5no activity439874---
L-ascorbic acid + tert-butylhydroperoxidedehydroascorbate + tert-butylalcohol
show the reaction diagram		Chlorella vulgaris-no activity439871---
L-ascorbic acid + tert-butylhydroperoxidedehydroascorbate + tert-butylalcohol
show the reaction diagram		Galdieria partita-both enzymes A and B439876-439876?
L-ascorbic acid + tert-butylhydroperoxidedehydroascorbate + tert-butylalcohol
show the reaction diagram		Helicoverpa zea-92% of the activity with H2O2439867-439867?
methyl naphthalene sulfide + H2O2? + H2O
show the reaction diagram		Pisum sativum--439877-439877?
n-propyl phenyl sulfide + H2O2? + H2O
show the reaction diagram		Pisum sativum--439877-439877?
NADH + H+ + H2O2NAD+ + H2O
show the reaction diagram		Oryza sativa-10% of the activity with ascorbate, APX 1, 1% of the activity with ascorbate, APX 2657113--?
NADPH + H+ + H2O2NADP+ + H2O
show the reaction diagram		Oryza sativa-27% of the activity with ascorbate, APX 1, 21% of the activity with ascorbate, APX 2657113--?
NADPH + H2O2? + H2O
show the reaction diagram		Euglena gracilis-no activity439857, 439858---
NADPH + H2O2? + H2O
show the reaction diagram		Glycine max-no activity439855---
NADPH + H2O2? + H2O
show the reaction diagram		Chlamydomonas sp.Q9SXL5no activity439874---
NADPH + H2O2? + H2O
show the reaction diagram		Chlorella vulgaris-no activity439871---
NADPH + H2O2? + H2O
show the reaction diagram		Brassica rapa-no activity439865---
NADPH + H2O2? + H2O
show the reaction diagram		Helicoverpa zea-enzyme partially purified from whole body homogenate: 93% of the activity with L-ascorbate, enzyme partially purified from regurgitant: 36% of the activity with L-ascorbate, when assayed at the same concentration439867-439867?
o-dianisidine + H2O2?
show the reaction diagram		Glycine max-reaction rate approximately equal to the rate with L-ascorbate439855-439855?
o-dianisidine + H2O2?
show the reaction diagram		Raphanus sativus-the oxidation rate is only 8.6% of that with L-ascorbate439868-439868?
p-chlorophenyl methyl sulfide + H2O2? + H2O
show the reaction diagram		Pisum sativum--439877-439877?
p-cresol + cumene-hydroperoxide4a,9b-dihydro-8,9b-dimethyl-3(4H)-dibenzofuranone + 2,2'-dihydroxy-5,5'-dimethylbiphenyl + 1,1-dimethylbenzylalcohol + bis-(1-methyl-1-phenylethyl)peroxide
show the reaction diagram		Pisum sativum--439877the formation of bis-(1-methyl-1-phenylethyl)peroxide derives from the reaction of 1,1-dimethylbenzylalcohol with either p-cresol or 2,2'-dihydroxy-5,5'-dimethylbiphenyl439877?
p-cresol + H2O24a,9b-dihydro-8,9b-dimethyl-3(4H)-dibenzofuranone + 2,2'-dihydroxy-5,5'-dimethylbiphenyl + H2O
show the reaction diagram		Pisum sativum--439877these products, which are derived from reactions of the p-methylphenoxy radical, itself form as a direct result of single-electron oxidation of p-cresol by the enzyme, can be accommodated from the known chemistry of the radical products, the product ratio 4alpha,9beta-dihydro-8,9beta-dimethyl-3(4H)-dibenzofuranone: 2,2'-dihydroxy-5,5'-dimethylbiphenyl is found to depend on enzyme concentration439877?
p-nitrophenyl methyl sulfide + H2O2? + H2O
show the reaction diagram		Pisum sativum--439877-439877?
pyrocatechol + H2O21,2-benzoquinone + H2O
show the reaction diagram		Spinacia oleracea-low activity compared to L-ascorbate439860-439860?
pyrogallol + H2O2?
show the reaction diagram		Dunaliella salina-little activity713220--?
pyrogallol + H2O2?
show the reaction diagram		Euglena gracilis-90.1% activity compared to L-ascorbate711139--?
pyrogallol + H2O2?
show the reaction diagram		Pallavicinia lyellii-cytosolic ascorbate peroxidase shows 29% activity compared to L-ascorbate, in the presence of 0.1 mM H2O2 and 208% activity compared to L-ascorbate in the presence of 0.5 mM H2O2713299--?
pyrogallol + H2O2? + H2O
show the reaction diagram		Ricinus communis-32% of the activity with ascorbate654378--?
pyrogallol + H2O23-hydroxybenzo-1,2-quinone + H2O
show the reaction diagram		Euglena gracilis--439857-439857?
pyrogallol + H2O23-hydroxybenzo-1,2-quinone + H2O
show the reaction diagram		Pisum sativum--439855-439855?
pyrogallol + H2O23-hydroxybenzo-1,2-quinone + H2O
show the reaction diagram		Chlamydomonas sp.Q9SXL5native enzyme: the activity corresponds to 121% of that found with L-ascorbate, recombinant enzyme: the activity corresponds to 130% of that found with L-ascorbate439874-439874?
pyrogallol + H2O23-hydroxybenzo-1,2-quinone + H2O
show the reaction diagram		Glycine max-the reaction rate is 38-fold higher than the rate with L-ascorbate439855-439855?
pyrogallol + H2O23-hydroxybenzo-1,2-quinone + H2O
show the reaction diagram		Zea mays-238% activity relative to L-ascorbate439861--?
pyrogallol + H2O23-hydroxybenzo-1,2-quinone + H2O
show the reaction diagram		Glycine max-recombinant enzyme 1: 355% activity relative to L-ascorbate, recombinant enzyme 2: 304% activity relative to L-ascorbate439869-439869?
pyrogallol + H2O23-hydroxybenzo-1,2-quinone + H2O
show the reaction diagram		Chlorella vulgaris-62.6% activity relative to L-ascorbate439871-439871?
pyrogallol + H2O23-hydroxybenzo-1,2-quinone + H2O
show the reaction diagram		Raphanus sativus-the oxidation rate is only 5.5% of that with L-ascorbate439868-439868?
pyrogallol + H2O23-hydroxybenzo-1,2-quinone + H2O
show the reaction diagram		Solanum tuberosum-the activity is lower than with L-ascorbate439875-439875?
pyrogallol + H2O23-hydroxybenzo-1,2-quinone + H2O
show the reaction diagram		Brassica rapa-2.5-fold higher rate than that of L-ascorbate439865-439865?
pyrogallol + H2O23-hydroxybenzo-1,2-quinone + H2O
show the reaction diagram		Glycine max-723% activity relative to L-ascorbate439864-439864?
pyrogallol + H2O23-hydroxybenzo-1,2-quinone + H2O
show the reaction diagram		Euglena gracilis-73.1% activity relative to L-ascorbate439858-439858?
pyrogallol + H2O23-hydroxybenzo-1,2-quinone + H2O
show the reaction diagram		Spinacia oleracea-low activity compared to L-ascorbate439860-439860?
pyrogallol + H2O23-hydroxybenzo-1,2-quinone + H2O
show the reaction diagram		Pisum sativum-the DTNB-modified enzyme exhibits full activity439873-439873?
reductic acid + H2O2?
show the reaction diagram		Euglena gracilis-i.e. 2,3-dihydroxy-2-cyclopenten-1-one, 7.1% activity relative to L-ascorbate439858-439858?
methyl phenyl sulfide + H2O2? + H2O
show the reaction diagram		Pisum sativum--439877-439877?
additional information?-Pisum sativum--439855---
additional information?-Zea mays-no activity with NADH439861---
additional information?-Chlorella vulgaris-no activity with: glutathione, cytochrome c, NADH and NADPH439871---
additional information?-Glycine max-no activity with: NAD(P)H, reduced glutathione or urate439855---
additional information?-Euglena gracilis-the activity with glutathione is less than 1.1% of that with L-ascorbic acid, no activity with: cytochrome c, NADH, NADPH, palmitic acid and triose reductone439858---
additional information?-Pisum sativum-experimental and modelled enantiomeric ratios R: S for oxidation of thioethers by recombinant enzyme and mutant Trp-41-Ala439877---
additional information?-Chlamydomonas sp.Q9SXL5native and recombinant enzyme, no activity with: glutathione, NADPH and cytochrome c439874---
additional information?-Helicoverpa zea-no activity with guaiacol439867---
additional information?-Euglena gracilis-no activity with: NADH, NADPH, cytochrome c, glutathione and palmitic acid as the natural electron donor439857---
additional information?-Raphanus sativus-no activity with: cytochrome c, reduced glutathione, NADH, NADPH, 6-palmityl-ascorbate, ascorbate-2-sulfate, guaiacol, 3,3'-diaminobenzidine, pyrocatechol or D-iso-ascorbate439868---
additional information?-Brassica rapa-the cytosolic enzyme exhibits no activity with: glutathione, cytochrome c and NAD(P)H439865---
additional information?-Ricinus communis-can cooperate with monodehydroascorbate reductase in glyoxysomal membrane to oxidize NADH, regenerate ascorbate, detoxify H2O2654378---
additional information?-Triticum aestivum-essential for photosynthesis657053---
additional information?-Gossypium hirsutumA7KIX5GhAPX1 is involved in hydrogen peroxide homeostasis during cotton fibre development689240---
additional information?-Pallavicinia lyellii-cytosolic and chloroplastic ascorbate peroxidase shows no activity with tert-butyl hydroperoxide and cumene hydroperoxide, pyrocatechol, hydroxyurea, GSH, cytochrome c, NADH, and NADPH. Chlorplastic ascorbate peroxidase displays no activity with pyrogallol, guaiacol, pyrocatechol, and 2,2'-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid)713299---
additional information?-Euglena gracilis-no activity with guaiacol and NADPH711139---

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)		COMMENTARY PRODUCTLITERATURE
(Product)
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Saccharomyces cerevisiae--696216--
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Hordeum vulgare--697013--
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Arabidopsis thaliana--698848, 700728--
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Embryophyta--700626--
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Oryza sativa--700843--
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Leishmania major--697682, 698047--
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Cyanidioschyzon merolae--700728--
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Populus tomentosa--700703--
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Gossypium hirsutumA7KIX5, C6ZDA9, C6ZDB0, Q39780-700842--
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Solanum pennellii--700220--
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Stylosanthes guianensis--696567--
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Solanum lycopersicumQ09Y74, Q09Y76, Q09Y77, Q09Y78, Q3I5C3, Q3I5C4, Q3SC88-700220--
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Cenchrus americanusA4ZYP9-699802--
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Brassica napusC5IUM6-710788--
L-ascorbate + H2O2dehydroascorbate + 2 H2O
show the reaction diagram		Pisum sativum--439855-439855
L-ascorbate + H2O2dehydroascorbate + 2 H2O
show the reaction diagram		Brassica rapa--439865-439865
L-ascorbate + H2O2dehydroascorbate + 2 H2O
show the reaction diagram		Riccia fluitans--694642--
L-ascorbate + H2O2dehydroascorbate + 2 H2O
show the reaction diagram		Solanum tuberosum-role of the mitochondrial enzyme in the scanvenging of toxic oxygen species inside potato tuber mitochondria439875-439875
L-ascorbate + H2O2dehydroascorbate + 2 H2O
show the reaction diagram		Euglena gracilis-the enzyme works for protection of cell membrane, by reducing the peroxide compounds generated endogenously from unsaturated fatty acids439858-439858
L-ascorbate + H2O2dehydroascorbate + 2 H2O
show the reaction diagram		Helicoverpa zea-the enzyme may be important in removing H2O2 and lipid peroxides in insects439867-439867
L-ascorbate + H2O2dehydroascorbate + 2 H2O
show the reaction diagram		Euglena gracilis-the enzyme appears to be the sole agent destroying H2O2439857-439857
L-ascorbate + H2O2dehydroascorbate + 2 H2O
show the reaction diagram		Glycine max-the enzyme is responsible for most H2O2 removal outside of peroxisomes in root nodules439855-439855
L-ascorbate + H2O2dehydroascorbate + 2 H2O
show the reaction diagram		Euglena gracilis-physiological role of the enzyme: removal of H2O2, prevention of H2O2 accumulation439857-439857
L-ascorbate + H2O2dehydroascorbate + 2 H2O
show the reaction diagram		Euglena gracilis-physiological role of the enzyme: removal of H2O2, prevention of H2O2 accumulation439858-439858
L-ascorbate + H2O2dehydroascorbate + 2 H2O
show the reaction diagram		Pisum sativum-physiological role of the enzyme: removal of H2O2, prevention of H2O2 accumulation439856-439856
L-ascorbate + H2O2dehydroascorbate + 2 H2O
show the reaction diagram		Glycine max-physiological role of the enzyme: removal of H2O2, prevention of H2O2 accumulation439864-439864
L-ascorbate + H2O2dehydroascorbate + H2O
show the reaction diagram		Cyanidioschyzon merolae CMA035C--700728--
additional information?-Ricinus communis-can cooperate with monodehydroascorbate reductase in glyoxysomal membrane to oxidize NADH, regenerate ascorbate, detoxify H2O2654378--
additional information?-Triticum aestivum-essential for photosynthesis657053--
additional information?-Gossypium hirsutumA7KIX5GhAPX1 is involved in hydrogen peroxide homeostasis during cotton fibre development689240--

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
hemeAlnus rubra, Arachis hypogaea, Arachis hypogaea Nongda 818, Lupinus albus, Medicago sativa, Trifolium subterraneum, Vicia faba, Vicia sativa, Vigna unguiculata--439855 2D-image
hemeSpinacia oleracea--439860 2D-image
hemeZea mays-one protoheme moiety per molecule439861 2D-image
hemePisum sativum--439855, 439856, 439862 2D-image
hemeBrassica rapa--439865 2D-image
hemeRaphanus sativus--439868 2D-image
hemeChlorella vulgaris--439871 2D-image
hemeChlamydomonas sp.Q9SXL5-439874 2D-image
hemeGaldieria partita--439876 2D-image
hemeTrypanosoma cruzi--439880 2D-image
hemeGlycine max-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 observation685131 2D-image
hemeGlycine max-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 titration685177 2D-image
hemeSaccharomyces cerevisiae--696216 2D-image
hemeGlycine max--439855, 439872, 696257 2D-image
hemeLeishmania major--697682, 698047 2D-image
hemeCenchrus americanusA4ZYP9-699802 2D-image
hemeEuglena gracilis--439858, 711139 2D-image
hemeHordeum vulgareO23983, Q945R5; 713234 2D-image
NADPHRiccia fluitans--694642 2D-image
hemePallavicinia lyellii--713299 2D-image
additional informationHelicoverpa zea-the enzyme may not be a heme-peroxidase439867-
additional informationGlycine max-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 M439872-

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
FeAlnus rubra, Arachis hypogaea, Glycine max, Lupinus albus, Medicago sativa, Trifolium subterraneum, Vicia faba, Vicia sativa, Vigna unguiculata-hemoprotein439855
FePisum sativum-hemoprotein439855, 439856
FeEuglena gracilis-hemoprotein439858
FeSpinacia oleracea-hemoprotein439860
FeRaphanus sativus--439868
IronPisum sativum-predominantly five-coordinate high-spin iron655435
Ni2+Oryza sativa-below 0.01 mM, activation, inhibition above657113

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
2,2,6,6-tetramethylpiperidinyl-1-oxideNicotiana tabacum-formation of 2,2,6,6-tetramethylpiperidinyl-1-oxy-adducts and subsequent oxidation of the cysteine residue located near the propionate group of heme leads to loss of enzyme activity686710 2D-image
2,2,6,6-tetramethylpiperidinyl-1-oxyl radicalGaldieria partita-formation of 2,2,6,6-tetramethylpiperidinyl-1-oxy-adducts and subsequent oxidation of the cysteine residue located near the propionate group of heme leads to loss of enzyme activity686710 2D-image
2,6-dichloroisonicotinic acidNicotiana tabacum-54% inhibition at 0.1 mM, 95% inhibition at 1 mM, the inhibition is not time-dependent439863 2D-image
2,6-dihydroxybenzoic acidNicotiana tabacum-biologically active, 72% inhibition at 0.2 mM439863 2D-image
2-mercaptoethanolPisum sativum-enzyme form C: 50% inhibition at 5 mM, 6 min, 100% inhibition after 18 min439856 2D-image
2-mercaptoethanolRaphanus sativus-not inhibitory at 0.5 mM, 31% inhibition at 5 mM439868 2D-image
3,3'-dithiobis(6-nitrobenzoic acid)Oryza sativa-5 mM, 80% residual activity, APX 1, 24% residual activity, APX 2657113 2D-image
3,5-dichlorosalicylic acidNicotiana tabacum-biologically active, 59% inhibition at 0.2 mM439863 2D-image
3-Hydroxybenzoic acidNicotiana tabacum-biologically inactive, 28% inhibition at 0.2 mM439863 2D-image
4-aminosalicylic acidNicotiana tabacum-biologically inactive, 9% inhibition at 0.2 mM439863 2D-image
4-chlorosalicylic acidNicotiana tabacum-biologically active, 58% inhibition at 0.2 mM439863 2D-image
5,5'-dithiobis(2-nitrobenzoic acid)Raphanus sativus-40% inhibition at 0.1 mM439868 2D-image
5,5'-dithiobis(2-nitrobenzoic acid)Pallavicinia lyellii-96% inhibition at 0.5 mM713299 2D-image
5-chlorosalicylic acidNicotiana tabacum-biologically active, 73% inhibition at 0.2 mM439863 2D-image
Al3+Euglena gracilis--439858 2D-image
Al3+Oryza sativa-inhibition in the range of 0.01-0.5 mM657113 2D-image
azideLeishmania major--698047 2D-image
azidePallavicinia lyellii-46% inhibition at 0.5 mM713299 2D-image
beta-mercaptoethanolPallavicinia lyellii-29% inhibition at 3 mM713299 2D-image
Br-Euglena gracilis-marked inhibition at 1 mM439858 2D-image
C2H2Glycine max-potent inhibitor439855 2D-image
C2H2Glycine max-recombinant enzyme 1: 94% inhibition at 0.1 ml per l, recombinant enzyme 2: 2% inhibition at 0.1 ml per l439869 2D-image
Ca2+Euglena gracilis--439858 2D-image
COGlycine max-potent inhibitor439855 2D-image
cyanidePallavicinia lyellii--713299 2D-image
cysteineRaphanus sativus-50% inhibition at 5 mM439868 2D-image
cysteineSolanum tuberosum-100% inhibition at 5 mM439875 2D-image
diethylenetriamine pentaacetic acidPallavicinia lyellii-9% inhibition at 5 mM713299 2D-image
dithioerythritolRaphanus sativus-67% inhibition at 0.05 mM439868 2D-image
dithioerythritolPallavicinia lyellii-37% inhibition at 3 mM713299 2D-image
dithiothreitolPisum sativum-enzyme form C: 100% inhibition at 0.1 mM for 5 min, 57% of the inhibition can be recovered by filtration on Sephadex G-25 and a further 14% is recovered after the addition of homocystine at 2 mM439856 2D-image
dithiothreitolRaphanus sativus-54% inhibition at 0.05 mM439868 2D-image
dithiothreitolPallavicinia lyellii-40% inhibition at 3 mM713299 2D-image
EDTAEuglena gracilis-slight inhibition, but when the enzyme is incubated with EDTA 1 mM at 37°C for 3 min in the absence of sucrose and ferrous sulfate there is nearly complete inhibition439858 2D-image
EDTARaphanus sativus-not inhibitory439868 2D-image
EDTAPallavicinia lyellii-97% inhibition at 3 mM713299 2D-image
F-Euglena gracilis--439858 2D-image
H2O2Nicotiana tabacumQ9TNL9wild-type enzyme has a half-time of inactivation of less than 10 sec. Triple mutant C26S/W35F/C126A retains 50% of the initial activity after H2O2 treatment for 3 min684930 2D-image
H2O2Nicotiana tabacum-when inactivated by H2O2, heme is irreversibly cross-linked to the APX apoprotein. tsAPXW35F is inactivated in 3 min by H2O2. It is possible that tsAPXW35F is inactivated by adistinct mechanism because the heme can no longer be cross-linked to the enzyme686657 2D-image
Hg2+Euglena gracilis-complete inhibition at 1 mM439858 2D-image
hydroxylamineGlycine max-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 mM439869 2D-image
hydroxylamineCenchrus americanusA4ZYP9-699802 2D-image
HydroxyureaHelicoverpa zea-26% inhibition at 1 mM439867 2D-image
HydroxyureaPallavicinia lyellii--713299 2D-image
I-Euglena gracilis--439858 2D-image
iodoacetamideSolanum tuberosum-30% inhibition at 1 mM, 65% inhibition at 5 mM439875 2D-image
iodoacetamidePallavicinia lyellii-19% inhibition at 3 mM713299 2D-image
iodoacetateZea mays-potent inhibitor439861 2D-image
iodoacetateRaphanus sativus-not inhibitory439868 2D-image
KCNGlycine max-potent inhibitor439855 2D-image
KCNPisum sativum-enzyme form C: 74% inhibition at 0.1 mM439856 2D-image
KCNEuglena gracilis-96.4% inhibition at 1 mM439858 2D-image
KCNZea mays-87% inhibition at 1 mM439861 2D-image
KCNBrassica rapa-complete inhibition at 0.05 mM439865 2D-image
KCNHelicoverpa zea-10% inhibition at 5 mM439867 2D-image
KCNRaphanus sativus-95% inhibition at 0.1 mM439868 2D-image
KCNGlycine max-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 mM439869 2D-image
KCNChlorella vulgaris-strong inhibition at 1 mM439871 2D-image
KCNChlamydomonas sp.Q9SXL5complete inhibition at 0.1 mM439874 2D-image
KCNSolanum tuberosum-100% inhibition at 0.5 mM439875 2D-image
KCNGaldieria partita--439876 2D-image
KCNOryza sativa-1 mM, 69% residual activity, APX 1, 20% residual activity, APX 2657113 2D-image
L-cysteinePallavicinia lyellii-28% inhibition at 3 mM713299 2D-image
Li+Euglena gracilis--439858 2D-image
MersalylSolanum tuberosum-58% inhibition at 0.005 mM, 100% inhibition at 0.05 mM439875 2D-image
Mg2+Euglena gracilis--439858 2D-image
N-ethylmaleimideSolanum tuberosum-33% inhibition at 0.05 mM, 28% inhibition at 0.5 mM439875 2D-image
Na2HAsO4Oryza sativa-inhibition in the range of 0.01-0.5 mM657113 2D-image
NaN3Glycine max-potent inhibitor439855 2D-image
NaN3Pisum sativum-enzyme form C: 27% inhibition at 5 mM439856 2D-image
NaN3Euglena gracilis-91.5% inhibition at 1 mM439858 2D-image
NaN3Zea mays-13% inhibition at 5 mM439861 2D-image
NaN3Brassica rapa-complete inhibition at 1 mM439865 2D-image
NaN3Raphanus sativus-17% inhibition at 1 mM, 87% inhibition at 10 mM439868 2D-image
NaN3Chlorella vulgaris-strong inhibition at 5 mM439871 2D-image
NaN3Chlamydomonas sp.Q9SXL5complete inhibition at 4 mM439874 2D-image
NaN3Solanum tuberosum-80% inhibition at 1 mM439875 2D-image
NaN3Galdieria partita--439876 2D-image
Ni2+Euglena gracilis--439858 2D-image
Ni2+Oryza sativa-below 0.01 mM, activation, inhibition above657113 2D-image
p-AminophenolNicotiana tabacum-time-dependent inhibition439863 2D-image
p-AminophenolHelicoverpa zea-not inhibitory439867 2D-image
p-chloromercuribenzoateZea mays-95% inhibition at 0.05 mM439861 2D-image
p-chloromercuribenzoateRaphanus sativus-87% inhibition at 0.005 mM, inactivation is partially reversible, 2-mercaptoethanol protects439868 2D-image
p-chloromercuribenzoateChlorella vulgaris-82% inhibition at 0.2 mM for 5 min439871 2D-image
p-chloromercuribenzoateChlamydomonas sp.Q9SXL584% inhibition at 0.2 mM for 5 min439874 2D-image
p-chloromercuribenzoatePallavicinia lyellii-27% inhibition at 3 mM713299 2D-image
p-Chloromercuriphenyl sulfonic acidGlycine max-100% inhibition at 0.05 mM, recombinant enzyme 1 and 2439869 2D-image
p-hydroxymercuribenzoateSolanum tuberosum-43% inhibition at 0.005 mM, 100% inhibition at 0.05 mM439875 2D-image
reduced glutathionePisum sativum-enzyme form C: 75% inhibition at 0.25 mM for 10 min439856 2D-image
reduced glutathioneRaphanus sativus-33% inhibition at 5 mM439868 2D-image
reduced glutathionePallavicinia lyellii-25% inhibition at 3 mM713299 2D-image
salicylic acidNicotiana tabacum-biologically active, reversible inhibition, 59% inhibition at 0.1 mM, 83% inhibition at 0.2 mM, 95% inhibition at 1 mM, the inhibition is not time-dependent439863 2D-image
salicylic acidCamellia sinensis, Nicotiana tabacum-reducing substrate, not inhibitory439870 2D-image
salicylic acidCenchrus americanusA4ZYP9-699802 2D-image
salicylic acidPallavicinia lyellii-98% inhibition at 0.5 mM713299 2D-image
Sodium azideOryza sativa-1 mM, 72% residual activity, APX 1, 55% residual activity, APX 2657113 2D-image
sodium nitroprussideArabidopsis thaliana-partial657008 2D-image
Zn2+Euglena gracilis--439858 2D-image
Zn2+Zea mays-leaves of plants grown with both low and high Zn show accumulation of lipid peroxides, ascorbate and dehydroascorbate, associated with a decrease in the activity of the enzyme439879 2D-image
Mn2+Euglena gracilis-marked inhibition at 1 mM439858 2D-image
additional informationCrocus sativus-not inhibitory up to 100 mM: cyanide, azide, aminotriazole654139-
additional informationOryza sativa-not inhibitory: alpha,alpha’-dipyridyl, EDTA657113-

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
H2O2Leishmania major, Leishmania major 5ASKH, Leishmania major Friedlin, Leishmania major Friedlin V9, Leishmania major LV-39, Leishmania major LV39, Leishmania major MHOM/IL/80/Friedlin, Leishmania major MHOM/IL/81, Leishmania major MHOM/IL/81/Friedlin, Leishmania major MRHO/IR/75/ER, Leishmania major V1--698047 2D-image
phenanthreneRiccia fluitans-exposure to 0.5 microM phenanthrene results in significant increase in the levels of both enzymatic and non-enzymatic antioxidants, with the levels of total glutathione and ascorbate doubling, the activitiy of APOX increasing by 2fold after 72 h of exposure to phenanthrene694642 2D-image
ZincHordeum vulgare--697013 2D-image

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.07-ascorbateCenchrus americanusA4ZYP9recombinant PgAPX699802 2D-image
0.076-ascorbateSolanum tuberosum--439875 2D-image
0.111-ascorbateChlorella vulgaris--439871 2D-image
0.14-ascorbateHelicoverpa zea--439867 2D-image
0.2-ascorbateOryza sativa-pH 7.0, APX 2657113 2D-image
0.3-ascorbateRicinus communis-pH 7.5, 25°C654378 2D-image
0.333-ascorbateGlycine max-recombinant enzyme 1439869 2D-image
0.34-ascorbateChlamydomonas sp.Q9SXL5native and recombinant enzyme439874 2D-image
0.35-ascorbateGlycine max-recombinant enzyme439864 2D-image
0.38-ascorbateZea mays--439861 2D-image
0.402-ascorbateBrassica rapa--439865 2D-image
0.467-ascorbateGlycine max-recombinant enzyme 2439869 2D-image
0.77-ascorbateRaphanus sativus--439868 2D-image
2.9-ascorbatePisum sativum-enzyme form C439856 2D-image
6.5-ascorbatePisum sativum-enzyme form B439856 2D-image
0.025-cytochrome cLeishmania major-25°C, mutant enzyme W208F685400 2D-image
6-cytochrome cLeishmania major-25°C, wild-type enzyme685400 2D-image
0.017-guaiacolLeishmania major-25°C, mutant enzyme W208F685400 2D-image
1.8-guaiacolGlycine max-recombinant enzyme439864 2D-image
2.9-guaiacolPisum sativum-pH 7.0, 25°C, mutant H42E655435 2D-image
4.2-guaiacolPisum sativum-will-type enzyme439873 2D-image
6.1-guaiacolPisum sativum-Cys32Ser mutant439873 2D-image
6.7-guaiacolLeishmania major-25°C, wild-type enzyme685400 2D-image
7.4-guaiacolPisum sativum-enzyme form C439856 2D-image
9.7-guaiacolPisum sativum-DTNB-modified enzyme439873 2D-image
12.3-guaiacolPisum sativum-pH 7.0, 25°C, wild-type655435 2D-image
0.011-H2O2Glycine max-recombinant enzyme 1439869 2D-image
0.02-H2O2Glycine max-recombinant enzyme439864 2D-image
0.02-H2O2Chlorella vulgaris--439871 2D-image
0.0217-H2O2Nicotiana tabacum-wild-type enzyme686657 2D-image
0.022-H2O2Nicotiana tabacumQ9TNL9wild-type enzyme684930 2D-image
0.022-H2O2Nicotiana tabacum-wild-type enzyme686710 2D-image
0.024-H2O2Brassica rapa--439865 2D-image
0.024-H2O2Glycine max-recombinant enzyme 2439869 2D-image
0.0287-H2O2Pallavicinia lyellii-in 50 mM potassium phosphate (pH 7.0), at 22°C713299 2D-image
0.033-H2O2Oryza sativa-pH 6.5, APX 1657113 2D-image
0.0343-H2O2Nicotiana tabacumQ9TNL9mutant enzyme C126A684930 2D-image
0.035-H2O2Zea mays--439861 2D-image
0.038-H2O2Nicotiana tabacum-pH 6.4, untreated cells657063 2D-image
0.042-H2O2Galdieria partita-wild-type enzyme686710 2D-image
0.047-H2O2Nicotiana tabacum-pH 6.4, heat-shock cells657063 2D-image
0.05-H2O2Chlamydomonas sp.Q9SXL5native and recombinant enzyme439874 2D-image
0.05-H2O2Crocus sativus-pH 8.0654139 2D-image
0.05-H2O2Galdieria partita-mutant enzyme C25S686710 2D-image
0.052-H2O2Galdieria partita-mutant enzyme C25S/C121S686710 2D-image
0.0537-H2O2Nicotiana tabacumQ9TNL9mutant enzyme C26S/C126A684930 2D-image
0.056-H2O2Euglena gracilis-substrate: L-ascorbic acid439858 2D-image
0.06-H2O2Ricinus communis-pH 7.5, 25°C654378 2D-image
0.0606-H2O2Nicotiana tabacumQ9TNL9mutant enzyme C26S684930 2D-image
0.061-H2O2Nicotiana tabacum-mutant enzyme C26S686710 2D-image
0.076-H2O2Oryza sativa-pH 7.0, APX 2657113 2D-image
0.08-H2O2Solanum tuberosum--439875 2D-image
0.0939-H2O2Nicotiana tabacumQ9TNL9mutant enzyme W35F684930 2D-image
0.0939-H2O2Nicotiana tabacum-mutant enzyme W35F686657 2D-image
0.12-H2O2Helicoverpa zea--439867 2D-image
0.12-H2O2Populus tomentosa-25°C688913 2D-image
0.12-H2O2Gossypium hirsutumA7KIX5-689240 2D-image
0.13-H2O2Raphanus sativus--439868 2D-image
0.136-H2O2Nicotiana tabacumQ9TNL9mutant enzyme C26S/W35F/C126A684930 2D-image
0.22-H2O2Euglena gracilis-substrate: pyrogallol439858 2D-image
0.041-L-ascorbateNicotiana tabacum-pH 6.4, heat-shock cells657063 2D-image
0.102-L-ascorbatePisum sativum-mutant S160M, pH 7.0, 25°C655789 2D-image
0.117-L-ascorbateGaldieria partita-wild-type enzyme686710 2D-image
0.123-L-ascorbatePallavicinia lyellii-in 50 mM potassium phosphate (pH 7.0), at 22°C713299 2D-image
0.15-L-ascorbateCrocus sativus-pH 8.0654139 2D-image
0.167-L-ascorbateNicotiana tabacumQ9TNL9mutant enzyme W35F684930 2D-image
0.17-L-ascorbatePisum sativum-pH 7.0, 25°C, mutant H42E655435 2D-image
0.17-L-ascorbateNicotiana tabacum-mutant enzyme W35F686657 2D-image
0.19-L-ascorbateNicotiana tabacumQ9TNL9mutant enzyme C26S/W35F/C126A684930 2D-image
0.198-L-ascorbateNicotiana tabacumQ9TNL9mutant enzyme C126A684930 2D-image
0.229-L-ascorbateNicotiana tabacum-pH 6.4, untreated cells657063 2D-image
0.355-L-ascorbatePisum sativum-wild-type, pH 7.0, 25°C655789 2D-image
0.394-L-ascorbateGaldieria partita-mutant enzyme C25S/C121S686710 2D-image
0.395-L-ascorbateNicotiana tabacumQ9TNL9wild-type enzyme684930 2D-image
0.395-L-ascorbateNicotiana tabacum-wild-type enzyme686657, 686710 2D-image
0.4-L-ascorbateOryza sativa-pH 6.5, APX 1657113 2D-image
0.41-L-ascorbatePisum sativum-pH 7.0, 25°C, wild-type655435 2D-image
0.43-L-ascorbateGossypium hirsutumA7KIX5-689240 2D-image
0.493-L-ascorbateEuglena gracilis-recombinant full length enzyme, in 50 mM potassium phosphate buffer, pH 7.0, at 22°C711139 2D-image
0.496-L-ascorbateGaldieria partita-mutant enzyme C25S686710 2D-image
0.506-L-ascorbateNicotiana tabacumQ9TNL9mutant enzyme C26S/C126A684930 2D-image
0.53-L-ascorbatePopulus tomentosa-25°C688913 2D-image
0.566-L-ascorbateNicotiana tabacumQ9TNL9mutant enzyme C26S684930 2D-image
0.566-L-ascorbateNicotiana tabacum-mutant enzyme C26S686710 2D-image
2.4-pyrogallolGlycine max-recombinant enzyme439864 2D-image
9.6-pyrogallolEuglena gracilis--439858 2D-image
0.41-L-ascorbic acidEuglena gracilis--439858 2D-image
additional information-additional informationGlycine max-the reaction does not follow Michaelis-Menten kinetics, Hill plots439855-
additional information-additional informationPisum sativum--439855-
additional information-additional informationPisum sativum-both forms of the enzyme show a very high affinity for H2O2, Km values below 0.005439856-
additional information-additional informationGaldieria partita-Km values comparable with those of higher plants439876-
additional information-additional informationTrypanosoma cruzi-ascorbate can saturate the ascorbate-dependent hemoperoxidase activity indicating that the enzyme obeys Michaelis-Menten kinetics439880-
additional information-additional informationGaldieria partita-Km of recombinant enzyme-B produced in E. coli439881-
additional information-additional informationNicotiana tabacum-untreated cells, sigmoidal dependence of reaction rate on ascorbate concentration, in heat shock cells, hyperbolic dependence of reaction rate on ascorbate concentration and 5-fold decrease in Km-value657063-

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.2-ascorbateSaccharomyces cerevisiae-CCP2APX696216 2D-image
0.53-ascorbateLeishmania major-25°C, wild-type enzyme685400 2D-image
696-ascorbateChlorella vulgaris--439871 2D-image
1.83-cytochrome cLeishmania major-25°C, wild-type enzyme685400 2D-image
1.5-guaiacolPisum sativum-pH 7.0, 25°C, mutant H42E655435 2D-image
2.5-guaiacolLeishmania major-25°C, wild-type enzyme685400 2D-image
66-guaiacolPisum sativum-pH 7.0, 25°C, wild-type655435 2D-image
2.03-H2O2Populus tomentosa-25°C688913 2D-image
46.71-H2O2Gossypium hirsutumA7KIX5-689240 2D-image
577-H2O2Euglena gracilis, Euglena gracilis 1224-5/25, Euglena gracilis 1224-5/9, Euglena gracilis mutant, Euglena gracilis SM-ZK, Euglena gracilis Z-recombinant full length enzyme, in 50 mM potassium phosphate buffer, pH 7.0, at 22°C711139 2D-image
1230-H2O2Galdieria partita-mutant enzyme C25S686710 2D-image
1310-H2O2Galdieria partita-mutant enzyme C25S/C121S686710 2D-image
1580-H2O2Nicotiana tabacumQ9TNL9mutant enzyme C26S684930 2D-image
1580-H2O2Nicotiana tabacum-mutant enzyme C26S686710 2D-image
1630-H2O2Nicotiana tabacumQ9TNL9mutant enzyme C126A684930 2D-image
1730-H2O2Nicotiana tabacumQ9TNL9mutant enzyme C26S/C126A684930 2D-image
1800-H2O2Nicotiana tabacumQ9TNL9wild-type enzyme684930 2D-image
1800-H2O2Nicotiana tabacum-wild-type enzyme686710 2D-image
2190-H2O2Galdieria partita-wild-type enzyme686710 2D-image
3280-H2O2Nicotiana tabacumQ9TNL9mutant enzyme C26S/W35F/C126A684930 2D-image
3410-H2O2Nicotiana tabacumQ9TNL9mutant enzyme W35F684930 2D-image
1.74-L-ascorbatePopulus tomentosa-25°C688913 2D-image
3.9-L-ascorbatePisum sativum-pH 7.0, 25°C, mutant H42E655435 2D-image
156-L-ascorbatePisum sativum-mutant S160M, pH 7.0, 25°C655789 2D-image
159-L-ascorbatePisum sativum-wild-type, pH 7.0, 25°C655789 2D-image
248-L-ascorbatePisum sativum-pH 7.0, 25°C, wild-type655435 2D-image
260-L-ascorbateGossypium hirsutumA7KIX5-689240 2D-image
754-L-ascorbateEuglena gracilis, Euglena gracilis 1224-5/25, Euglena gracilis 1224-5/9, Euglena gracilis mutant, Euglena gracilis SM-ZK, Euglena gracilis Z-recombinant full length enzyme, in 50 mM potassium phosphate buffer, pH 7.0, at 22°C711139 2D-image
760-L-ascorbatePallavicinia lyellii-in 50 mM potassium phosphate (pH 7.0), at 22°C713299 2D-image
1490-L-ascorbateGaldieria partita-mutant enzyme C25S/C121S686710 2D-image
1570-L-ascorbateGaldieria partita-mutant enzyme C25S686710 2D-image
1710-L-ascorbateNicotiana tabacumQ9TNL9mutant enzyme C126A684930 2D-image
1910-L-ascorbateNicotiana tabacumQ9TNL9mutant enzyme C26S/W35F/C126A684930 2D-image
1980-L-ascorbateGaldieria partita-wild-type enzyme686710 2D-image
2040-L-ascorbateNicotiana tabacumQ9TNL9mutant enzyme C26S684930 2D-image
2040-L-ascorbateNicotiana tabacum-mutant enzyme C26S686710 2D-image
2400-L-ascorbateNicotiana tabacumQ9TNL9mutant enzyme C26S/C126A684930 2D-image
2510-L-ascorbateNicotiana tabacumQ9TNL9wild-type enzyme684930 2D-image
2510-L-ascorbateNicotiana tabacum-wild-type enzyme686710 2D-image
160-pyrogallolPisum sativum-wild-type, Cys32Ser mutant and DTNB-modified enzyme439873 2D-image
2833-L-ascorbateNicotiana tabacumQ9TNL9mutant enzyme W35F684930 2D-image
additional information-additional informationPisum sativum-substrate: guaiacol, effects of Cys32Ser mutagenesis and DTNB-modification439873-
additional information-additional informationGaldieria partita-of recombinant enzyme-B produced in E. coli439881-

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
16500-H2O2Euglena gracilis, Euglena gracilis 1224-5/25, Euglena gracilis 1224-5/9, Euglena gracilis mutant, Euglena gracilis SM-ZK, Euglena gracilis Z-recombinant full length enzyme, in 50 mM potassium phosphate buffer, pH 7.0, at 22°C71113911283
1530-L-ascorbateEuglena gracilis, Euglena gracilis 1224-5/25, Euglena gracilis 1224-5/9, Euglena gracilis mutant, Euglena gracilis SM-ZK, Euglena gracilis Z-recombinant full length enzyme, in 50 mM potassium phosphate buffer, pH 7.0, at 22°C71113912104
6600-L-ascorbatePallavicinia lyellii-in 50 mM potassium phosphate (pH 7.0), at 22°C71329912104

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.0308-hydroxylamineCenchrus americanusA4ZYP9-699802 2D-image
0.0018-KCNEuglena gracilis, Euglena gracilis 1224-5/25, Euglena gracilis 1224-5/9, Euglena gracilis mutant, Euglena gracilis SM-ZK, Euglena gracilis Z-competitive inhibition against H2O2439858 2D-image
0.0083-KCNEuglena gracilis-uncompetitive inhibition against L-ascorbic acid439858 2D-image
0.059-NaN3Euglena gracilis-uncompetitive inhibition against H2O2439858 2D-image
0.085-NaN3Euglena gracilis, Euglena gracilis 1224-5/25, Euglena gracilis 1224-5/9, Euglena gracilis mutant, Euglena gracilis SM-ZK, Euglena gracilis Z-competitive inhibition against L-ascorbic acid439858 2D-image
0.1905-salicylic acidCenchrus americanusA4ZYP9-699802 2D-image

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
0.01-Lupinus albus-crude extract of root nodules, the activity is rapidly lost after extraction439855
0.092-Trifolium subterraneum-crude extract of root nodules439855
0.096-Pisum sativum-crude extract of root nodules, cv Alaska439855
0.1-Pisum sativum-purified enzyme439859
0.11-Medicago sativa-crude extract of root nodules439855
0.161-Pisum sativum-crude extract of root nodules, cv Austrian winter439855
0.213-Vicia sativa-crude extract of root nodules439855
0.241-Vicia faba-crude extract of root nodules439855
0.258-Vigna unguiculata-crude extract of root nodules439855
0.26-Stylosanthes guianensis-effect of abscisic acid and EGTA on APX activity, 1 day following chilling stress696567
0.27-Stylosanthes guianensis-effect of abscisic acid and EGTA on APX activity, 7 days, under normal temperature696567
0.28-Stylosanthes guianensis-effect of abscisic acid and EGTA on APX activity, 4 days following chilling stress; effect of abscisic acid and LaCl3 on APX activity, 4 days following chilling stress696567
0.284-Glycine max-crude extract of root nodules439855
0.3-Stylosanthes guianensis-effect of EGTA on APX activity, 4 days following chilling stress; in water, 4 days following chilling stress696567
0.31-Stylosanthes guianensis-effect of abscisic acid and EGTA on APX activity, 4 days, under normal temperature; effect of abscisic acid on APX activity, 7 days, under normal temperature; effect of LaCl3 on APX activity, 7 days, under normal temperature696567
0.32-Stylosanthes guianensis-effect of abscisic acid and LaCl3 on APX activity, 1 day following chilling stress; effect of EGTA on APX activity, 1 day following chilling stress; effect of LaCl3 on APX activity, 4 days following chilling stress; in water, 1 day following chilling stress696567
0.33-Stylosanthes guianensis-effect of abscisic acid and LaCl3 on APX activity, 4 days, under normal temperature; effect of abscisic acid and LaCl3 on APX activity, 7 days, under normal temperature; effect of EGTA on APX activity, 4 days, under normal temperature; effect of EGTA on APX activity, 7 days, under normal temperature; in water, 7 days, under normal temperature696567
0.35-Stylosanthes guianensis-in water, 4 days, under normal temperature696567
0.36-Stylosanthes guianensis-effect of abscisic acid on APX activity, 4 days following chilling stress; effect of LaCl3 on APX activity, 1 day following chilling stress696567
0.366-Arachis hypogaea-crude extract of root nodules439855
0.37-Stylosanthes guianensis-effect of LaCl3 on APX activity, 4 days, under normal temperature696567
0.4-Stylosanthes guianensis-effect of abscisic acid on APX activity, 1 day following chilling stress696567
0.45-Stylosanthes guianensis-effect of abscisic acid on APX activity, 4 days, under normal temperature696567
0.7684-Euglena gracilis-crude extract439857
1.3-Chlamydomonas sp.Q9SXL5recombinant enzyme, soluble fraction, addition of 3% NaCl439874
1.6-Pallavicinia lyellii-crude extract, in 50 mM potassium phosphate (pH 7.0), at 22°C713299
2.8-Euglena gracilis-purified enzyme, electron donor: glutathione, electron acceptor: H2O2439858
34Glycine max-affinity purified preparation439864
3.3-Chlorella vulgaris-cell extract439871
4-Arabidopsis thaliana-control698848
4.32-Alnus rubra-crude extract of root nodules, activity is only detected when soluble polyvinylpolypyrrolidone is included in the buffer and O2 is excluded by through degassing of buffers and performing all extraction steps under a vigorous stream of N2 gas439855
5.8-Euglena gracilis-purified enzyme, electron donor: iodide, electron acceptor: H2O2439858
7.1-Helicoverpa zea-substrate: cumene hydroperoxide439867
9.4-Glycine max-recombinant enzyme 1, after DEAE-column chromatography439869
18-Euglena gracilis-purified enzyme, electron donor: reductic acid, electron acceptor: H2O2439858
18-Arabidopsis thaliana-stress factor heat698848
19.2-Helicoverpa zea-substrate: tert-butyl hydroperoxide439867
20.3-Euglena gracilis-purified enzyme, electron donor: guaiacol, electron acceptor: H2O2439858
20.9-Helicoverpa zea-substrate: H2O2439867
31.7-Glycine max-purified recombinant enzyme439864
32-Glycine max-recombinant enzyme439872
34-Glycine max-wild-type enzyme439872
34.2-Glycine max-purified enzyme439855
36-Solanum tuberosum-purified enzyme439875
37-Arabidopsis thaliana-stress factor drought698848
46.7-Helicoverpa zea-partially purified enzyme439867
53-Arabidopsis thaliana-stress factors drought and heat698848
56-Brassica rapa-purified enzyme439865
63.6-Glycine max-recombinant enzyme 2, after chromatofocusing439869
100-Camellia sinensis-cytosolic enzyme, in the presence and absence of salicylic acid439870
117-Pisum sativum-purified recombinant enzyme439862
132.2-Euglena gracilis-purified enzyme, electron donor: L-ascorbic acid, electron acceptor: cumene hydroperoxide439858
142.1-Euglena gracilis-purified enzyme, electron donor: D-araboascorbic acid, electron acceptor: H2O2439858
172.8-Euglena gracilis-purified enzyme, electron donor: L-ascorbic acid, electron acceptor: tert-butyl hydroperoxide439858
185.5-Euglena gracilis-purified enzyme, electron donor: pyrogallol, electron acceptor: H2O2439858
254-Euglena gracilis-purified enzyme, electron donor: L-ascorbic acid, electron acceptor: H2O2439858
378-Ricinus communis-pH 7.5, 25°C654378
456-Pallavicinia lyellii-after 285fold purification, in 50 mM potassium phosphate (pH 7.0), at 22°C713299
561.1-Raphanus sativus-purified enzyme439868
580-Chlamydomonas sp.Q9SXL5purified recombinant enzyme439874
636-Chlamydomonas sp.Q9SXL5purified native enzyme439874
1307-Chlorella vulgaris-purified enzyme439871
1500-Camellia sinensis-chloroplastic enzyme, in the presence and absence of salicylic acid439870
additional information-Glycine max-effects of media amendments439864

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
4.5-Camellia sinensis-assay at, thylakoid-bound chloroplastic isoenzyme439870
56Zea mays--439861
5.2-Pisum sativum-enzyme form B439856
5.97Glycine max--439864
6-Raphanus sativus--439868
6-Pallavicinia lyellii-cytosolic APX713299
6.1-Chlorella vulgaris--439871
6.2-Pisum sativum-enzyme form C439856
6.2-Euglena gracilis--439857, 439858
6.3-Brassica rapa-assay at439865
6.4-Cenchrus americanusA4ZYP9in gel activity assay699802
6.57Populus tomentosa--688913
6.5-Brassica rapa--439865
6.5-Oryza sativa-APX 1657113
6.5-Gossypium hirsutumA7KIX5oxidation of ascorbate689240
6.6-Glycine max-recombinant enzyme 2439869
6.6-Cenchrus americanusA4ZYP9activity 75 units mg-1 protein min-1699802
6.8-Chlamydomonas sp.Q9SXL5-439874
7-Pisum sativum-assay at439862
7-Nicotiana tabacum-assay at439863
7-Glycine max-assay at439864
7-Helicoverpa zea-assay at439867
7-Glycine max-assay at; recombinant enzyme 1439869
7-Camellia sinensis-chloroplastic stromal and cytosolic enzyme, assay at439870
7-Nicotiana tabacum--439870
7-Chlorella vulgaris-assay at439871
7-Glycine max-assay at439872
7-Chlamydomonas sp.Q9SXL5assay at439874
7-Solanum tuberosum--439875
7-Oryza sativa-APX 2657113
7-Riccia fluitans-assay at694642
7-Stylosanthes guianensis-activity assay696567
7-Hordeum vulgare-activity assay697013
7-Arabidopsis thaliana, Cyanidioschyzon merolae-activity assay700728
7.4-Arabidopsis thaliana-activity assay698848
7.8-Populus tomentosa-activity assay700703
8-Crocus sativus--654139
8-Pallavicinia lyellii-chloroplast APX713299

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
57.5Gossypium hirsutumA7KIX5pH 5: about 50% of maximal activity, pH 7.5: about 50% of maximal activity689240
57.8Cenchrus americanusA4ZYP9activity 35 units mg-1 protein min-1 at pH 5.0 and pH 7.8699802
58Pisum sativum-both forms of the enzyme439856
58Pallavicinia lyellii-the activity of APX decreases rapidly at pH above 8.0713299
59Populus tomentosa-pH 5.0: 68% of maximal activity, pH 9.0: 23% of maximal activity688913
67.9Euglena gracilis-maximum activity maintained439858

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
7.5-Saccharomyces cerevisiae-activity assay696216
23-Cenchrus americanusA4ZYP9in gel activity assay at room temperature699802
25-Riccia fluitans-assay at694642
25-Arabidopsis thaliana-activity assay698848
30-Leishmania major-peroxidase assay698047
3234Euglena gracilis--439858
32-Euglena gracilis--439857
32-Euglena gracilis-assay at439858
36.4-Chlorella vulgaris--439871
38-Brassica rapa--439865
40-Pallavicinia lyellii--713299
42-Chlamydomonas sp.Q9SXL5-439874
45-Populus tomentosa--688913

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
2055Populus tomentosa-20°C: about 65% of maximal activity, 55°C: about 40% of maximal activity688913

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
5.62-Cenchrus americanusA4ZYP9estimated isoelectric point699802

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
coleoptileZea mays--439861Manually annotated by BRENDA team
cotton fibreGossypium hirsutumA7KIX5GhAPX1 is highly expressed in wild-type 5-day postanthesis fibres with much lower transcript levels in the fuzzless-lintless mutant ovules. GhAPX1 expression is upregulated in response to an increase in cellular H2O2 and ethylene689240Manually annotated by BRENDA team
embryoHordeum vulgareO23983, Q945R5; 713234Manually annotated by BRENDA team
fat bodyHelicoverpa zea-55.6% relative activity to salivary gland439867Manually annotated by BRENDA team
flowerBrassica napusC5IUM6-710788Manually annotated by BRENDA team
fruitSolanum lycopersicumQ09Y74, Q09Y76, Q09Y77, Q09Y78, Q3I5C3, Q3I5C4, Q3SC88-700220Manually annotated by BRENDA team
fruitSolanum pennellii--700220Manually annotated by BRENDA team
hypocotylGlycine max-presence of two major non-plastid isozymes439869Manually annotated by BRENDA team
leafTriticum aestivum--439859Manually annotated by BRENDA team
leafSpinacia oleracea--439859, 439860Manually annotated by BRENDA team
leafZea mays-young leaves contain low amounts of enzyme, in mature green leaves, small amounts of the enzyme are distributed in vascular systems, in particular in companion cells439861Manually annotated by BRENDA team
leafBrassica rapa--439865Manually annotated by BRENDA team
leafGlycine max-presence of two major non-plastid isozymes439869Manually annotated by BRENDA team
leafCamellia sinensis--439870Manually annotated by BRENDA team
leafNicotiana tabacum--439863, 439870Manually annotated by BRENDA team
leafZea mays--439879Manually annotated by BRENDA team
leafOryza sativa--657113Manually annotated by BRENDA team
leafArabidopsis thalianaQ42592, Q42593; 685002Manually annotated by BRENDA team
leafPopulus tomentosa--688913Manually annotated by BRENDA team
leafSaccharum officinarum-total APX activity, on a fresh weight basis, is stimulated only at 2 mM methyl viologen at 24 h, but dropps at higher doses689350Manually annotated by BRENDA team
leafAvicennia marinaA7LIY1salt stressed leaves689652Manually annotated by BRENDA team
leafStylosanthes guianensis--696567Manually annotated by BRENDA team
leafCenchrus americanusA4ZYP9-699802Manually annotated by BRENDA team
leafSolanum lycopersicumQ09Y74, Q09Y76, Q09Y77, Q09Y78, Q3I5C3, Q3I5C4, Q3SC88-700220Manually annotated by BRENDA team
leafSolanum pennellii--700220Manually annotated by BRENDA team
leafArabidopsis thaliana, Cyanidioschyzon merolae, Cyanidioschyzon merolae CMA035C--700728Manually annotated by BRENDA team
leafPopulus simonii x Populus pyramidalis--710779Manually annotated by BRENDA team
malpighian tubuleHelicoverpa zea-31.1% relative activity to salivary gland439867Manually annotated by BRENDA team
mesocotylZea mays--439861Manually annotated by BRENDA team
petalSolanum pennellii--700220Manually annotated by BRENDA team
rootAlnus rubra, Arachis hypogaea, Lupinus albus, Medicago sativa, Pisum sativum, Trifolium subterraneum, Vicia faba, Vicia sativa, Vigna unguiculata-nodules439855Manually annotated by BRENDA team
rootZea mays--439861Manually annotated by BRENDA team
rootRaphanus sativus--439868Manually annotated by BRENDA team
rootGlycine max-nodules; presence of two major non-plastid isozymes439869Manually annotated by BRENDA team
rootGlycine max-nodules439855, 439864, 439872Manually annotated by BRENDA team
rootOryza sativaP0C0L0, P0C0L1, Q0JEQ2, Q10N21, Q69SV0, Q6ZJJ1, Q7XJ02, Q9FE01of seedlings. NaCl-enhanced expression of OsAPx8 in rice roots is mediated through an accumulation of abscisic acid. Na+ but not Cl- is required for enhancing OsAPx8 expression. H2O2 is not involved in the regulation of NaCl-induced OsAPx8 expression in rice roots; of seedlings. No significant increase due to NaCl can be detected in the expression of OsAPx1; of seedlings. No significant increase due to NaCl can be detected in the expression of OsAPx2; of seedlings. No significant increase due to NaCl can be detected in the expression of OsAPx3; of seedlings. No significant increase due to NaCl can be detected in the expression of OsAPx4; of seedlings. No significant increase due to NaCl can be detected in the expression of OsAPx5; of seedlings. No significant increase due to NaCl can be detected in the expression of OsAPx6; of seedlings. The expression of OsAPx7 is not affected by 150 mM and 200 mM NaCl, but is 40% decreased by 300 mM NaCl688083Manually annotated by BRENDA team
rootPopulus tomentosa--688913Manually annotated by BRENDA team
rootSolanum lycopersicumQ09Y74, Q09Y76, Q09Y77, Q09Y78, Q3I5C3, Q3I5C4, Q3SC88-700220Manually annotated by BRENDA team
rootSolanum pennellii--700220Manually annotated by BRENDA team
rootOryza sativa--700843Manually annotated by BRENDA team
salivary glandHelicoverpa zea-highest activity439867Manually annotated by BRENDA team
seedZea mays--439861Manually annotated by BRENDA team
seedRicinus communis-germinating654378Manually annotated by BRENDA team
seedlingOryza sativa-root of seedling, increase in enzyme activity after treatment with NaCl or H2O2, inhibition of enzyme accumulation by diphenyleneiodinium chloride or imidazole, but not by dimethylthiourea656625Manually annotated by BRENDA team
seedlingOryza sativaP0C0L0, P0C0L1, Q0JEQ2, Q10N21, Q69SV0, Q6ZJJ1, Q7XJ02, Q9FE01root. NaCl-enhanced expression of OsAPx8 in rice roots is mediated through an accumulation of abscisic acid. Na+ but not Cl- is required for enhancing OsAPx8 expression. H2O2 is not involved in the regulation of NaCl-induced OsAPx8 expression in rice roots; root. No significant increase due to NaCl can be detected in the expression of OsAPx1; root. No significant increase due to NaCl can be detected in the expression of OsAPx2; root. No significant increase due to NaCl can be detected in the expression of OsAPx3; root. No significant increase due to NaCl can be detected in the expression of OsAPx4; root. No significant increase due to NaCl can be detected in the expression of OsAPx5; root. No significant increase due to NaCl can be detected in the expression of OsAPx6; root. The expression of OsAPx7 is not affected by 150 mM and 200 mM NaCl, but is 40% decreased by 300 mM NaCl688083Manually annotated by BRENDA team
seedlingGlycine maxQ76LA8cAPX 2 is involved in flooding stress responses in young soybean seedlings689427Manually annotated by BRENDA team
seedlingArabidopsis thaliana--698848Manually annotated by BRENDA team
seedlingCenchrus americanusA4ZYP9-699802Manually annotated by BRENDA team
seedlingOryza sativa--700843Manually annotated by BRENDA team
seedlingHordeum vulgareO23983, Q945R5; 713234Manually annotated by BRENDA team
shootPisum sativum--439856, 439859, 439866Manually annotated by BRENDA team
stamenSolanum pennellii--700220Manually annotated by BRENDA team
stemPopulus tomentosa--688913Manually annotated by BRENDA team
stemSolanum lycopersicumQ09Y74, Q09Y76, Q09Y77, Q09Y78, Q3I5C3, Q3I5C4, Q3SC88-700220Manually annotated by BRENDA team
thallusRiccia fluitans--694642Manually annotated by BRENDA team
thallusPallavicinia lyellii--713299Manually annotated by BRENDA team
tuberSolanum tuberosum--439875Manually annotated by BRENDA team
midgutHelicoverpa zea-20% relative activity to salivary gland439867Manually annotated by BRENDA team
additional informationHordeum vulgareO23983, Q945R5ascorbate peroxidase is not detected in dry mature seed; ascorbate peroxidase is not detected in dry mature seed713234Manually annotated by BRENDA team

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
chloroplastSpinacia oleracea--9507439860Manually annotated by BRENDA team
chloroplastCamellia sinensis, Camellia sinensis O. Kuntze-thylakoid-bound9507439870Manually annotated by BRENDA team
chloroplastPisum sativum-significant increase of stromal activity and decrease of thylakoidal activity in response to 0.07-0.11 mM NaCl with concommittant increase in H2O2 content of chloroplasts and reduction of ascorbate level9507656405Manually annotated by BRENDA team
chloroplastArabidopsis thalianaQ42592, Q42593stromal ascorbate peroxidase is particularly important for photoprotection during the early greening process. In mature leaves, thylakoid-bound enzyme and stromal enzyme are functionally redundant, and crucial upon sudden onset of oxidative stress. The chloroplast ascorbate peroxidases contribute to chloroplast retrograde signalling pathways upon slight fluctuations in the accumulation of H2O2 in chloroplasts; stromal enzyme is particularly important for photoprotection during the early greening process. In mature leaves, thylakoid-bound enzyme and stromal enzyme are functionally redundant, and crucial upon sudden onset of oxidative stress. The chloroplast ascorbate peroxidases contribute to chloroplast retrograde signalling pathways upon slight fluctuations in the accumulation of H2O2 in chloroplasts9507685002Manually annotated by BRENDA team
chloroplastArabidopsis sp.--9507685676Manually annotated by BRENDA team
chloroplastChlamydomonas sp. W80Q9SXL5-9507685676Manually annotated by BRENDA team
chloroplastNicotiana tabacum-stroma9507684930, 686710Manually annotated by BRENDA team
chloroplastSolanum lycopersicum-two APX isoforms, one thylakoid-bound and one stromal. APXs in the chloroplast is a highly sensitive site of antioxidant systems under Cd stress, and the inactivation of APX could be mainly responsible for oxidative modification to Rubisco and subsequent decrease in its activity9507688200Manually annotated by BRENDA team
chloroplastSolanum lycopersicumQ09Y74, Q09Y76, Q09Y77, Q09Y78, Q3I5C3, Q3I5C4, Q3SC88stromal; thylakoidal9507700220Manually annotated by BRENDA team
chloroplastSolanum pennellii-APX6, APX79507700220Manually annotated by BRENDA team
chloroplastEmbryophyta--9507700626Manually annotated by BRENDA team
chloroplastArabidopsis thaliana, Cyanidioschyzon merolae, Cyanidioschyzon merolae CMA035C--9507700728Manually annotated by BRENDA team
chloroplastPallavicinia lyellii-approximately 46% of the APX activity is associated with intact chloroplasts9507713299Manually annotated by BRENDA team
chloroplast stromaBrassica rapa--9570439865Manually annotated by BRENDA team
chloroplast stromaCamellia sinensis, Camellia sinensis O. Kuntze--9570439870Manually annotated by BRENDA team
chloroplast stromaChlamydomonas sp.Q9SXL5-9570439874Manually annotated by BRENDA team
chloroplast stromaNicotiana tabacum--9570655921Manually annotated by BRENDA team
chloroplast stromaGossypium hirsutumA7KIX5, C6ZDA9, C6ZDB0, Q39780-9570700842Manually annotated by BRENDA team
cytoplasmZea mays--5737439861Manually annotated by BRENDA team
cytosolAlnus rubra, Arachis hypogaea, Lupinus albus, Medicago sativa, Trifolium subterraneum, Vicia faba, Vicia sativa, Vigna unguiculata--5829439855Manually annotated by BRENDA team
cytosolEuglena gracilis--5829439857Manually annotated by BRENDA team
cytosolBrassica rapa--5829439865Manually annotated by BRENDA team
cytosolRaphanus sativus--5829439868Manually annotated by BRENDA team
cytosolGlycine max-presence of two major non-plastid isozymes5829439869Manually annotated by BRENDA team
cytosolCamellia sinensis, Camellia sinensis O. Kuntze--5829439870Manually annotated by BRENDA team
cytosolPisum sativum--5829439855, 439866, 439877, 655435, 655789Manually annotated by BRENDA team
cytosolGaldieria partita, Galdieria sulphuraria--5829685676Manually annotated by BRENDA team
cytosolGossypium hirsutumA7KIX5-5829689240Manually annotated by BRENDA team
cytosolOryza sativaQ10N21, Q9FE01; 5829689513Manually annotated by BRENDA team
cytosolGlycine max--5829439855, 439864, 656853, 685131, 685177, 689427, 696257Manually annotated by BRENDA team
cytosolArabidopsis thaliana--5829698848Manually annotated by BRENDA team
cytosolCenchrus americanusA4ZYP9-5829699802Manually annotated by BRENDA team
cytosolSolanum lycopersicumQ09Y74, Q09Y76, Q09Y77, Q09Y78, Q3I5C3, Q3I5C4, Q3SC88-5829700220Manually annotated by BRENDA team
cytosolSolanum pennellii-APX1, APX2, APX35829700220Manually annotated by BRENDA team
cytosolGossypium hirsutumA7KIX5, C6ZDA9, C6ZDB0, Q39780; 5829700842Manually annotated by BRENDA team
cytosolEuglena gracilis-APX becomes mature in the cytosol after processing of the precursor5829711139Manually annotated by BRENDA team
cytosolPallavicinia lyellii-54% of the total APX activity is presumed to be cytosolic APX5829713299Manually annotated by BRENDA team
endoplasmic reticulumLeishmania majorQ4Q3K2-5783685676Manually annotated by BRENDA team
endoplasmic reticulumTrypanosoma cruziQ8I1N3-5783439880, 685676Manually annotated by BRENDA team
glyoxysomeRicinus communis--9514654378Manually annotated by BRENDA team
glyoxysomeGossypium hirsutumA7KIX5, C6ZDA9, C6ZDB0, Q39780-9514700842Manually annotated by BRENDA team
mitochondrial intermembrane spaceLeishmania major--5758697682, 698047Manually annotated by BRENDA team
mitochondrionSolanum tuberosum-inside, either bound to the inner membrane or in the matrix5739439875Manually annotated by BRENDA team
peroxisomeAvicennia marinaA7LIY1-5777689652Manually annotated by BRENDA team
peroxisomeHordeum vulgare--5777697013Manually annotated by BRENDA team
peroxisomeSolanum lycopersicumQ09Y74, Q09Y76, Q09Y77, Q09Y78, Q3I5C3, Q3I5C4, Q3SC88; 5777700220Manually annotated by BRENDA team
peroxisomeSolanum pennellii-APX4, APX55777700220Manually annotated by BRENDA team
peroxisomePopulus tomentosa--5777700703Manually annotated by BRENDA team
mitochondrionLeishmania major--5739697682, 698047Manually annotated by BRENDA team
additional informationEuglena gracilis-not in mitochondria, chloroplasts, microsomes-439857Manually annotated by BRENDA team
additional informationGlycine max-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-439869Manually annotated by BRENDA team
additional informationEuglena gracilis-not localized in plastids-711139Manually annotated by BRENDA team

PDBSCOPCATHORGANISM
1oaf, downloadSCOP (1oaf)CATH (1oaf)Glycine max
1oag, downloadSCOP (1oag)CATH (1oag)Glycine max
1v0h, downloadSCOP (1v0h)CATH (1v0h)Glycine max
2cl4, downloadSCOP (2cl4)CATH (2cl4)Glycine max
2ggn, downloadSCOP (2ggn)CATH (2ggn)Glycine max
2ghc, downloadSCOP (2ghc)CATH (2ghc)Glycine max
2ghd, downloadSCOP (2ghd)CATH (2ghd)Glycine max
2ghe, downloadSCOP (2ghe)CATH (2ghe)Glycine max
2ghh, downloadSCOP (2ghh)CATH (2ghh)Glycine max
2ghk, downloadSCOP (2ghk)CATH (2ghk)Glycine max
2vcf, downloadSCOP (2vcf)CATH (2vcf)Glycine max
2vcn, downloadSCOP (2vcn)CATH (2vcn)Glycine max
2vcs, downloadSCOP (2vcs)CATH (2vcs)Glycine max
2wd4, downloadSCOP (2wd4)CATH (2wd4)Glycine max
2xi6, downloadSCOP (2xi6)CATH (2xi6)Glycine max
2xif, downloadSCOP (2xif)CATH (2xif)Glycine max
2xih, downloadSCOP (2xih)CATH (2xih)Glycine max
2xj6, downloadSCOP (2xj6)CATH (2xj6)Glycine max
2y6a, downloadSCOP (2y6a)CATH (2y6a)Glycine max
2y6b, downloadSCOP (2y6b)CATH (2y6b)Glycine max
3zcg, downloadSCOP (3zcg)CATH (3zcg)Glycine max
3zch, downloadSCOP (3zch)CATH (3zch)Glycine max
3zcy, downloadSCOP (3zcy)CATH (3zcy)Glycine max
3riv, downloadSCOP (3riv)CATH (3riv)Leishmania major
3riw, downloadSCOP (3riw)CATH (3riw)Leishmania major
4ged, downloadSCOP (4ged)CATH (4ged)Leishmania major
1iyn, downloadSCOP (1iyn)CATH (1iyn)Nicotiana tabacum
1apx, downloadSCOP (1apx)CATH (1apx)Pisum sativum

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
10000-Helicoverpa zea-partially purified enzyme, molecular weight cut-off centrifugation439867
27000-Glycine max-recombinant enzyme 1 and 2, calculated from sequence of cDNA439869
27000-Cenchrus americanusA4ZYP9determined by SDS-PAGE699802
27500-Cenchrus americanusA4ZYP9apparent molecular weight699802
28000-Zea mays-gel filtration439861
28000-Brassica rapa-gel filtration439865
28000-Raphanus sativus-native PAGE439868
28000-Galdieria partita-both enzymes A and B439876
28000-Pallavicinia lyellii-gel filtration713299
30000-Spinacia oleracea--439860
30000-Leishmania major-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 gene698047
30000-Arabidopsis thaliana, Cyanidioschyzon merolae CMA035C, Cyanidioschyzon merolae-determined by SDS-PAGE and Western Blot analysis700728
30030-Chlamydomonas sp.Q9SXL5calculated from the cDNA clone encoding a mature protein of 282 amino acids439874
31000-Chlamydomonas sp.Q9SXL5gel filtration, native and recombinant enzyme439874
32000-Chlorella vulgaris-gel filtration439871
46000-Glycine max-recombinant enzyme 2, column chromatography in the absence of denaturant439869
47000-Alnus rubra, Arachis hypogaea--439855
47000-Glycine max-gel filtration439855
47000-Lupinus albus, Medicago sativa, Pisum sativum, Trifolium subterraneum, Vicia faba, Vicia sativa, Vigna unguiculata--439855
48000-Glycine max-recombinant enzyme 1, column chromatography in the absence of denaturant439869
57000-Pisum sativum-crude pea shoot extract, gel filtration, co-elution of two forms of the enzyme, B and C, which can be separated by cation-exchange chromatography439856
58000-Euglena gracilis-mature full length APX, gel filtration711139
60080-Euglena gracilis-mature full length APX, calculated from amino acid sequence711139
64200-Gossypium hirsutumA7KIX5gel filtration689240
74000-Populus tomentosa-gel filtration688913
76000-Euglena gracilis-gel filtration439858

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
?Glycine max-x * 30000, SDS-PAGE439864
?Glycine max-x * 28000, SDS-PAGE, recombinant enzyme 2; x * 30000, SDS-PAGE, recombinant enzyme 1439869
?Solanum tuberosum-x * 31000, SDS-PAGE439875
?Ricinus communis-x * 34000, SDS-PAGE654378
?Oryza sativa-x * 28500, APX 1, x * 34000, APX 2, SDS-PAGE657113
dimerPopulus tomentosa-2 * 31580, calculated from sequence; 2 * 37370, SDS-PAGE688913
dimerGossypium hirsutumA7KIX52 * 28000, calculated from sequence; 2 * 31500, His-tag fused enzyme, SDS-PAGE689240
homodimerEuglena gracilis-2 * 30000, SDS-PAGE711139
monomerGlycine max-1 * 30000, SDS-PAGE, discrepancy to value from gel filtration probably due to enzyme conformation439855
monomerSpinacia oleracea--439860
monomerZea mays-1 * 28000, SDS-PAGE439861
monomerBrassica rapa-1 * 28000, SDS-PAGE439865
monomerHelicoverpa zea-1 * 10000, SDS-PAGE, partially purified enzyme439867
monomerRaphanus sativus-1 * 28000, SDS-PAGE439868
monomerChlorella vulgaris-1 * 32000, SDS-PAGE439871
monomerChlamydomonas sp.Q9SXL51 * 31000, SDS-PAGE, native and recombinant enzyme439874
monomerGaldieria partita-1 * 28000, both enzymes A and B439876
monomerPallavicinia lyellii-1 * 28000, SDS-PAGE713299

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
additional informationNicotiana tabacum-contains protoporphyrin IX heme655921
additional informationRicinus communis-hemoprotein654378

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
in complex with ascorbate; in complex with salicylhydroxamic acidGlycine maxQ43758656853
-Nicotiana tabacum-655921
crystals of Cys32Ser-mutant and DTNB-modified enzyme grown using the hanging drop, vapor diffusion method. The 2.0 A X-ray crystal structure of DTNB-modified enzyme shows clear electron density for the TNB group covalently attached to Cys32 in all four molecules of the asymmetric unit, indicating complete and specific modificationPisum sativum-439873
of the recombinant enzyme, using the hanging drop, vapor diffusion method, the recombinant enzyme forms monoclinic crystals in space group C2 with a: 132.80 A, b: 53.26 A, c: 171.96 A and beta: 106.93°Pisum sativum-439862
the crystal structures of the CCP2APX and CCP2APX/F191 mutants are solvedSaccharomyces cerevisiae-696216

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
58Pallavicinia lyellii-the enzyme is not stable below pH 5.0 and above 8.0 for 24 h at 4°C, 68% of the activity is retained between pH 5.0 and 8.0 for 24 h at 4°C713299
6.57.5Brassica rapa--439865

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
4-Alnus rubra, Arachis hypogaea, Glycine max, Lupinus albus, Medicago sativa, Pisum sativum, Trifolium subterraneum, Vicia faba, Vicia sativa, Vigna unguiculata-half-life 10 h439855
37-Euglena gracilis-maximum activity maintained up to439858
40-Euglena gracilis-inactivated after 5 min; preincubated in 30% sucrose and 0.05 mM ferrous sulfate, retains 88.1% activity after 5 min439858
49-Glycine max-melting temperature of the ferric derivative, monitored by circular dichroism spectroscopy439872
50-Chlorella vulgaris-the enzyme retains full activity between pH 6 and pH 7.5439871
52-Euglena gracilis-complete inactivation439858
55-Brassica rapa-complete loss of activity439865
57-Glycine max-melting temperature of the ferric-cyanide derivative, monitored by circular dichroism spectroscopy439872
60-Chlorella vulgaris-complete loss of activity439871
60-Pallavicinia lyellii-the enzyme is relatively stable at 60°C, with 54% loss of activity713299
70-Pisum sativum-5 min, complete inactivation439856
100-Pisum sativum-10 min, loss of activity439856
100-Helicoverpa zea-complete loss of activity439867

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
the enzyme is very unstable in the absence of ascorbate and looses its activity within min particularly in the case of chloroplastic and mitochondrial isoformsCenchrus americanusA4ZYP9699802
the enzyme is relatively stable in ascorbate-depleted mediumChlamydomonas sp.Q9SXL5439874
the half-inactivation time is estimated to be 15 min, when the enzyme is diluted with ascorbate-depleted mediumChlorella vulgaris-439871
the recombinant enzyme-B remains active for at least 180 min after depletion of ascorbateGaldieria partita-439881
when the enzyme is diluted with the ascorbate-deleted medium, the half inactivation time is approximately 15 minPallavicinia lyellii-713299
loss of activity after incubation of crude extracts from pea shoots with either pronase or chymotrypsinPisum sativum-439856
dialysis of crude enzyme preparations for 24 h against a buffer depleted of ascorbate or sorbitol results in 90% and 20% loss in enzyme activity, respectively. In air saturated solutions, salting-out results in a significant loss in enzyme activity, therefore exchange to N2 gas is performed prior to salting-out of the root enzymeRaphanus sativus-439868
the enzyme is completely inactivated within 30 s in ascorbate-depleted medium under anaerobic conditionsSolanum tuberosum-439875

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
Ethylene glycolOryza sativa, Oryza sativa IAC 165, Oryza sativa Japonica, Oryza sativa L. Hitomebore, Oryza sativa M-101, Oryza sativa Nipponbare, Oryza sativa njavara-PEG 6000, 40% in assay medium, 50% inhibition of aPX 1, 65% inhibition of APX 2 with increase in enzyme Km values, incorporation of 1 M proline, glycine betaine or sucrose in presence of PEG in the assay medium restores657113

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
not stable under aerobic conditionsSpinacia oleracea-439860
stabilization by ascorbate and sorbitolSpinacia oleracea-439860
not stable under aerobic conditionsSpinacia oleracea Atlanta, Spinacia oleracea Melody, Spinacia oleracea Mn-SOD-439860

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-20°C or -80°C, crude extracts of root nodules, 50 mM potassium phosphate buffer, pH 7.0, several monthsGlycine max-439855
-80°C, intact soybean nodules, stable, 3 yearsGlycine max-439855
4°C, crude extracts of root nodules, in air, 25% loss of activity, 15 daysGlycine max-439855
4°C, crude extracts of root nodules, in air, stable, 6 daysGlycine max-439855

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
Escherichia coli recombinant stromal ascorbate peroxidase is purified with a HisTrap kit, proteins are used to immunize rabbits and ratsArabidopsis thaliana-700728
using column chromatography on DEAE-Sephacel, ammonium sulfate treatment and column chromatography on butyl-Toyopearl and TSK G3000SWBrassica rapa-439865
purified near homogeneity from clarified Escherichia coli lysate by passing through Ni-NTA agarose beadsCenchrus americanusA4ZYP9699802
of the native enzyme, using ammonium sulfate precipitation, column chromatography on Phenyl-Sepharose, second ammonium sulfate precipitation, and column chromatography on Superdex 200 and Q SepharoseChlamydomonas sp.Q9SXL5439874
using ultra centrifugation, column chromatography on DEAE-Sephacel, ammonium sulfate precipitation, column chromatography on phenyl Sepharose, ammonium sulfate precipitation and column chromatography on Superdex 200 and Phenyl SuperoseChlorella vulgaris-439871
Escherichia coli recombinant stromal ascorbate peroxidase is purified with a HisTrap kit, proteins are used to immunize rabbits and ratsCyanidioschyzon merolae, Cyanidioschyzon merolae CMA035C-700728
TALON metal affinity resin column chromatographyEuglena gracilis-711139
using ultracentrifugation, column chromatography on DEAE-cellulose, ammonium sulfate precipitation and column chromatography on Sephadex G-150, DEAE-cellulose and CM-celluloseEuglena gracilis-439858
using hydrophobic chromatography, separation of two isozymes: enzyme-A and enzyme-B, enzyme-B accounts for 85% of the total activity, purification of both enzymesGaldieria partita-439876
-Glycine max-685131
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-300Glycine max-439869
using ammonium sulfate precipitation, dialysis and column chromatography on DEAE, Sephacryl und hydroxyapatiteGlycine max-439855
using Ni2+-agarose affinity chromatography and gel filtration after reconstitution with heminGlycine max-439864
-Gossypium hirsutumA7KIX5689240
partial, from whole body homogenate, using ammonium sulfate fractionation, column chromatography on Sephadex G-75 and isoelectric focusing. Second isolation of the enzyme: from regurgitant of actively feeding fifth instar organism, using centrifugation, a concentrator and isoelectric focusingHelicoverpa zea-439867
Arabidopsis thaliana leaf extracts are preparedHordeum vulgare-697013
mitochondria are prepared and fractionatedLeishmania major-698047
wild-type and mutant enzyme W208F expressed in Escherichia coliLeishmania major-685400
both APX 1 and APX 2Oryza sativa-657113
ammonium sulfate precipitation, butyl-Toyopearl column chromatography, DEAE-cellulofine column chromatography, and Sephadex G-75 gel filtrationPallavicinia lyellii-713299
of the recombinant enzyme, using affinity chromatography on amylose colum, and column chromatography on hydroxylapatite and FFQ-SepharosePisum sativum-439862
using ammonium sulfate fractionation, column chromatography on DEAE-cellulose, and a second ammonium sulfate fractionationPisum sativum-439859
using Ca-phosphate gel treatment, ammonium sulfate fractionation, column chromatography on Sephadex G-100, ultrafiltration and column chromatography on DEAE-Sephadex and CM-Sephadex C-50, two forms of the enzyme, B and C, can be separated by the CM-Sephadex C-50 stepPisum sativum-439856
-Populus tomentosa-688913
using ammonium sulfate precipitation, dialysis and column chromatography on butyl-Toyopearl, DEAE-cellulofine and Sephadex G-75Raphanus sativus-439868
-Ricinus communis-654378
recombinant Escherichia coli mutants are purified by chromatography on a Sephadex G-75 column and a DEAE-Sephacel anione-exchange columnSaccharomyces cerevisiae-696216
using lysed mitochondria, and column chromatography on DEAE-Sephacel, Sephadex G-75, DE-52 and hydroxylapatiteSolanum tuberosum-439875
-Spinacia oleracea-439860
-Zea mays-439861

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
full length AtstAPX is cloned into the pPZP221 binary vector, introduced into Arabidopsis thaliana by the floral dip method using Agrobacterium tumefaciens strain GV3101, for the generation of antibodies into the vector pQE80L for expression in Escherichia coli cellsArabidopsis thaliana-700728
overexpression in Escherichia coliAvicennia marinaA7LIY1689652
the entire and truncated versions of APX (1-140, 1-250, 140-439, 250-439 and 140-250) are cloned into pGADT7 to fuse to the GAL4 activation domain and expressed in yeastBrassica napusC5IUM6710788
into the vector pET-28a+ for the expression in Escherichia coli BL21DE3 cells, the 5'-flanking region of the PgAPX1 gene is cloned into the Topo-TA vectorCenchrus americanusA4ZYP9699802
expression in Escherichia coli, the presence of 3% NaCl as well as beta-D-thiogalactopyranoside is needed for the expressionChlamydomonas sp.Q9SXL5439874
full length CmstAPX is cloned into the pPZP221 binary vector, introduced into Arabidopsis thaliana by the floral dip method using Agrobacterium tumefaciens strain GV3101, for the generation of antibodies into the vector pQE80L for expression in Escherichia coli cellsCyanidioschyzon merolae, Cyanidioschyzon merolae CMA035C-700728
expressed in Escherichia coli strain BL21 StarEuglena gracilis, Euglena gracilis 1224-5/25, Euglena gracilis 1224-5/9, Euglena gracilis mutant, Euglena gracilis SM-ZK, Euglena gracilis Z-711139
expression in Escherichia coliGaldieria partita-439881
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 yeastGlycine max-439878
expression in Escherichia coliGlycine max-439872
expression in Escherichia coli of two soybean ascorbate peroxidase cDNAsGlycine max-439869
expression in Escherichia coli, most of the enzyme produced is present in the apo-form, without hemeGlycine max-439864
GhAPX1 is expressed in Escherichia coliGossypium hirsutumA7KIX5689240
transgenic Arabidopsis thaliana constitutively overexpressing HvAPX1 under control of the CaMv 35S promoterHordeum vulgare-697013
into the vector pXG B2863 for transfection of Leishmania major cellsLeishmania major-697682
into the vector pXG-B2863 for transfection of Leishmania major cellsLeishmania major-698047
overexpression in Arabidopsis. Transgenic lines over-expressing OsAPXb showed higher salt tolerance than OsAPXa transgenic lines. Overproduction of OsAPXb enhances and maintains APX activity to a much higher degree than OsAPXa in transgenic Arabidopsis during treatment with different concentrations of NaCl, enhances the active oxygen scavenging system, and protects plants from salt stress by equilibrating H2O2 metabolism; overexpression in Arabidopsis. Transgenic lines over-expressing OsAPXb show higher salt tolerance than OsAPXa transgenic lines. Overproduction of OsAPXb enhances and maintains APX activity to a much higher degree than OsAPXa in transgenic Arabidopsis during treatment with different concentrations of NaCl, enhances the active oxygen scavenging system, and protects plants from salt stress by equilibrating H2O2 metabolismOryza sativaQ10N21, Q9FE01689513
expression as a fusion product with the Escherichia coli maltose-binding proteinPisum sativum-439862
recombinant enzymePisum sativum-439877
expression in Escherichia coliPopulus tomentosa-688913
into the pBI121 binary vector for a Agrobacterium tumefaciens-mediated tobacco leaf disc transformation, a CaMV 35S promoter and a rd29A promoter driven construct is usedPopulus tomentosa-700703
the vector pT-7 is used, cytochrome c peroxidase, CCP, is converted into an ascorbate peroxidase, APX, by engineering the ascorbate-binding loop and critical arginine into CCP to give the CCP2APX mutantSaccharomyces cerevisiae-696216
into the vector pGEM-T Easy for sequencing; into the vector pGEM-T Easy for sequencing; into the vector pGEM-T Easy for sequencing; into the vector pGEM-T Easy for sequencing; into the vector pGEM-T Easy for sequencing; into the vector pGEM-T Easy for sequencing; into the vector pGEM-T Easy for sequencingSolanum lycopersicumQ09Y74, Q09Y76, Q09Y77, Q09Y78, Q3I5C3, Q3I5C4, Q3SC88700220
into the vector pGEM-T Easy for sequencingSolanum pennellii-700220
expression of an epitope-tagged form of the enzyme in Trypanosoma cruziTrypanosoma cruzi-439880

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
cytosolic ascorbate peroxidase 1 protein and mRNA accumulates during drought and heat stressArabidopsis thaliana-698848
expression of PgAPX1 significantly increases under heat-stress conditions, transcript analysis suggests that the heat-shock element, HSE, motifs may be responsible for stress-specific expression of PgAPX1 by interacting with PgHSFCenchrus americanusA4ZYP9699802
there is an increase in APX (from strain IR-1) under 28°C/0.1 mM m-2 s-1 light an temperature conditionsDunaliella salina, Dunaliella salina IR-1 and Gh-U-713220
APX is easily inactivated by excess amounts of H2O2, chloroplastic APX looses its activity within 1 min in the absence of ascorbate when 20 mol equivalent of H2O2 is addedEmbryophyta-700626
transcript level and the total APX activity are highly induced in response to in vitro applied H2O2 or ethylene, up-regulated during fiber cell elongatingGossypium hirsutumA7KIX5, C6ZDA9, C6ZDB0, Q39780700842
HvAPX1-overexpressing transgenic plants have higher APX activity in leaves under zinc stressHordeum vulgare-697013
no ascorbate peroxidase activity is present in mature seeds but activity is detected after 24 h post imbibition and increases 14fold up to 144 h post imbibition; no ascorbate peroxidase activity is present in mature seeds but activity is detected after 24 h post imbibition and increases 14fold up to 144 h post imbibitionHordeum vulgareO23983, Q945R5713234
expression of LmAPX is increased when cells are treated with exogenous H2O2Leishmania major, Leishmania major 5ASKH, Leishmania major Friedlin, Leishmania major Friedlin V9, Leishmania major LV-39, Leishmania major LV39, Leishmania major MHOM/IL/80/Friedlin, Leishmania major MHOM/IL/81, Leishmania major MHOM/IL/81/Friedlin, Leishmania major MRHO/IR/75/ER, Leishmania major V1-697682, 698047
salt stress, Na+ induces expression of OsAPx8, , NaCl-enhanced expression of OsAPx8 in rice roots is mediated through an accumulation of the plant hormone ABAOryza sativa-700843
0.01 mM diphenylene iodonium chloride treatment leads to an obvious decrease in the activity of ascorbate peroxidase in Clostera anachoreta larvae-wounded leavesPopulus simonii x Populus pyramidalis-710779
activity of ascorbate peroxidase is enhanced in Clostera anachoreta larvae-wounded leaves (immediate and sharp increase at 0.5 h, followed by a sudden decrease at 2 h, and then a slight increase at 6 h after damage)Populus simonii x Populus pyramidalis-710779
APX activity in the 35S-PpAPX transgenic lines increases by 50% compared to the activity in the control lines, activity is 80% higher in the leaves in response to drought or salt stresses, the PpAPX transcript level is very low under normal growing conditions in rd29Ap-PpAPX plants, but clearly increased under drought stressPopulus tomentosa-700703
expression of gene decreases in response to NaCl stress; expression of gene decreases in response to NaCl stressSolanum lycopersicumQ09Y74, Q09Y76, Q09Y77, Q09Y78, Q3I5C3, Q3I5C4, Q3SC88700220
salt-induced up-regulation of ascorbate peroxidaseSolanum pennellii-700220
the application of either LaCl3 or EGTA reverses the effect of abscisic acid on chilling-treated plants, i.e. it leads to the decrease in ascorbate peroxidase activityStylosanthes guianensis-696567
abscisic acid induces ascorbate peroxidase activityStylosanthes guianensis-696567

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
C25SGaldieria partita-kcat/Km for L-ascorbate is 5.4fold lower than wild-type value. kcat/KM for H2O2 is 2.1fold lower than wild-type value. In contrast to wild-type enzyme, the mutant enzyme retains more than 90% of the initial activity after incubation for 10 min with the radical scavenger 2,2,6,6-tetramethylpiperidinyl-1-oxy and H2O2686710
C25S/C121SGaldieria partita-kcat/Km for L-ascorbate is 4.5fold lower than wild-type value. kcat/KM for H2O2 is 2.1fold lower than wild-type value. In contrast to wild-type enzyme, the mutant enzyme retains more than 90% of the initial activity after incubation for 10 min with the radical scavenger 2,2,6,6-tetramethylpiperidinyl-1-oxy and H2O2686710
W41AGlycine max-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 peroxide696257
W208FLeishmania major-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 oxidation685400
W208YLeishmania major-mutant shows low spin hem. The mutant does not react with H2O2685400
C126ANicotiana tabacumQ9TNL9kcat/KM for L-ascorbate is 1.4fold higher than wild-type enzyme. kcat/Km for H2O2 is 1.7fold lower than wild-type enzyme684930
C26SNicotiana tabacumQ9TNL9kcat/KM for L-ascorbate is 1.8fold lower than wild-type enzyme. kcat/Km for H2O2 is 3.1fold lower than wild-type enzyme684930
C26SNicotiana tabacum-kcat/Km for L-ascorbate is 1.8fold lower than wild-type value. kcat/KM for H2O2 is 3.1fold lower than wild-type value. In contrast to wild-type enzyme, the mutant enzyme retains 60% of the initial activity after incubation for 10 min with the radical scavenger 2,2,6,6-tetramethylpiperidinyl-1-oxy and H2O2686710
C26S/C126ANicotiana tabacumQ9TNL9kcat/KM for L-ascorbate is 1.3fold lower than wild-type enzyme. kcat/Km for H2O2 is 2.5fold lower than wild-type enzyme684930
C26S/W35F/C126ANicotiana tabacumQ9TNL9kcat/KM for L-ascorbate is 1.6fold than wild-type enzyme. kcat/Km for H2O2 is 3.4fold lower than wild-type enzyme. Mutant shows increased tolerance to H2O2 (retains 50% of the initial activity after H2O2 treatment for 3 min) compared to wild-type enzyme (half-time of inactivation is less than 10 sec)684930
W35FNicotiana tabacumQ9TNL9kcat/KM for L-ascorbate is 2.6fold higher than wild-type enzyme. kcat/Km for H2O2 is 2.3fold lower than wild-type enzyme684930
W35FNicotiana tabacum-mutation does not cause a significant change in the structure of tsAPX. Mutation increases H2O2 tolerance. 2.3fold decrease in KM-value for L-ascorbate. 4.3fold increase in Km-value for H2O2686657
C32SPisum sativum-the mutation leads to approximately 70% drop in ascorbate peroxidase activity with no effect on guaiacol peroxidase activity, these results indicate that uncharged aromatic substrates and the anionic ascorbate molecule interact with different sites on the enzyme439873
H42APisum sativum-inactive, partial recovery of activity by addition of exogenous imidazoles655435
H42EPisum sativum-decrease in kcat- and Km-value655435
S160MPisum sativum-expression of apo-protein in Escherichia coli, reconstitution with exogenous heme, gives kinetic properties similar to wild-type enzyme655789
W41APisum sativum-the mutation enables the efficient conversion of recombinant enzyme into a stereoselective oxidizing agent for sulfides439877
CCP2APXSaccharomyces cerevisiae-residues 30-42, LREDDEYDNYIGY, of wild-type CCP are replaced with residues 27-32, IAEKKC, of APX in order to introduce the ascorbate-binding loop, a N184R point mutation is added696216
CCP2APX/F191Saccharomyces cerevisiae-in order to enable CCP2APX to form a porphyrin pi-cation radical during catalysis, Trp191 is converted to Phe696216
additional informationTriticum aestivum, Triticum aestivum Tugela DN-mutant lacking activity of isozyme TaAPX-6B, reduction of total enzymic activity by 40%, mutants show significantly reduced photosynthetic activity and biomass accumulation when grown at high-light intensity photosystem II electron transfer, but no oxidative damage657053

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
the apo-recombinant protein is easily converted to the holo-recombinant form by in vitro reconstitution with heminGlycine max, Glycine max L., Glycine max Williams 82-439864

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
synthesisArabidopsis thaliana-overexpression of thylakoidal isozyme, increased resistance to the herbicide Paraquat but not to photoinhibitory treatments ot iron or copper overload. Sodium nitroprusside partially inhibits enzyme activity657008
agricultureHordeum vulgare-the results suggest that HvAPX1 plays an important role in zinc and cadmium tolerance, and might be a candidate gene for developing high-biomass tolerant plants for phytoremediation of zinc- and cadmium-polluted environments697013
analysisPisum sativum-the ascorbate peroxidase procedure may be applied to ascorbate estimation in sources as black-currant juice, parsley leaf, broccoli influorescence, potato tuber, mouse liver and human urine439859
agriculturePopulus tomentosa-the transgenic plants show enhanced tolerance to oxidative stress, salt and drought, PpAPX does not play a significant role under normal growing conditions, but do ameliorate oxidative injury under abiotic stress, the Ad29 promoter shoul be used as an inducible promoter in transgenic works700703

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISM (UNIPROT ACCESSION NO.)LINK TO PUBMEDSOURCE
439855Dalton, D.A.; Hanus, F.J.; Russell, S.A.; Evans, H.J.Purification, properties, and distribution of ascorbate peroxidase in legume root nodulesPlant Physiol.83789-7941987Alnus rubra, Arachis hypogaea, Glycine max, Lupinus albus, Medicago sativa, Pisum sativum, Trifolium subterraneum, Vicia faba, Vicia sativa, Vigna unguiculata PubMed
439856Gerbling, K.P.; Kelly, G.J.; Fischer, K.H.; Latzko, E.Partial purification and properties of soluble ascorbate peroxidases from pea leaves.J. Plant Physiol.11559-671984Pisum sativum PubMed
439857Shigeoka, S.; Nakano, Y.; Kitaoka, S.Metabolism of hydrogen peroxide in Euglena gracilis Z by L-ascorbic acid peroxidaseBiochem. J.186377-3801980Euglena gracilis PubMed
439858Shigeoka, S.; Nahana, Y.; Kitaoka, S.Purification and some properties of L-ascorbic-acid-specific peroxidase in Euglena gracilis ZArch. Biochem. Biophys.201121-1271980Euglena gracilis PubMed
439859Kelly, G.J.; Latzko, E.Soluble ascorbate peroxidaseNaturwissenschaften6667-681979Eremosphaera viridis, Pisum sativum, Spinacia oleracea, Triticum aestivum-
439860Nakano, Y.; Asada, K.Purification of ascorbate peroxidase in spinach chloroplasts; its inactivation in ascorbate-depleted medium and reactivation by monodehydroascorbate radicalPlant Cell Physiol.28131-1401987Spinacia oleracea-
439861Koshiba, T.Cytosolic ascorbate peroxidase in seedlings and leaves of maize (Zea mays)Plant Cell Physiol.34713-7211993Zea mays-
439862Patterson, W.R.; Poulos, T.L.Characterization and Crystallization of Recombinant Pea Cytosolic Ascorbate PeroxidaseJ. Biol. Chem.26917020-170241994Pisum sativum PubMed
439863Durner, J.; Klessig, D.F.Inhibition of ascorbate peroxidase by salicylic acid and 2,6-dichloroisonicotinic acid, two inducers of plant defense responsesProc. Natl. Acad. Sci. USA9211312-113161995Nicotiana tabacum PubMed
439864Dalton, D.A.; Diaz del Castillo, L.; Kahn, M.L.; Joyner, S.L.; Chatfield, J.M.Heterologous expression and characterization of soybean cytosolic ascorbate peroxidaseArch. Biochem. Biophys.3281-81996Glycine max PubMed
439865Ishikawa, T.; Takeda, T.; Shigeoka, S.Purification and characterization of cytosolic ascorbate peroxidase from komatsuna (Brassica rapa)Plant Sci.12011-181996Brassica rapa-
439866Marquez, L.A.; Quitoriano, M.; Zilinskas, B.A.; Dunford, H.B.Kinetic and spectral properties of pea cytosolic ascorbate peroxidaseFEBS Lett.389153-1561996Pisum sativum PubMed
439867Mathews, M.C.; Summers, C.B.; Felton, G.W.Ascorbate peroxidase: a novel antioxidant enzyme in insectsArch. Insect Biochem. Physiol.3457-681997Helicoverpa zea-
439868Ohya, T.; Morimura, Y.; Saji, H.; Mihara, T.; Ikawa, T.Purification and characterization of ascorbate peroxidase in roots of Japanese radishPlant Sci.125137-1451997Raphanus sativus-
439869Caldwell, 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. coliPlanta204120-1261998Glycine max PubMed
439870Kvaratskhelia, M.; George, S.J.; Thorneley, R.N.Salicylic acid is a reducing substrate and not an effective inhibitor of ascorbate peroxidaseJ. Biol. Chem.27220998-210011997Camellia sinensis, Nicotiana tabacum PubMed
439871Takeda, T.; Yoshimura, K.; Ishikawa, T.; Shigeoka, S.Purification and characterization of ascorbate peroxidase in Chlorella vulgarisBiochimie80295-3011998Chlorella vulgaris PubMed
439872Jones, D.K.; Dalton, D.A.; Rosell, F.I.; Raven, E.L.Class I heme peroxidases: characterization of soybean ascorbate peroxidaseArch. Biochem. Biophys.360173-1781998Glycine max PubMed
439873Mandelman, D.; Jamal, J.; Poulos, T.L.Identification of two electron-transfer sites in ascorbate peroxidase using chemical modification, enzyme kinetics, and crystallographyBiochemistry3717610-176171998Pisum sativum PubMed
439874Takeda, T.; Yoshimura, K.; Yoshii, M.; Kanahoshi, H.; Miyasaka, H.; Shigeoka, S.Molecular characterization and physiological role of ascorbate peroxidase from halotolerant Chlamydomonas sp. W80 strainArch. Biochem. Biophys.37682-902000Chlamydomonas sp. (Q9SXL5) PubMed
439875De Leonardis, S.; Dipierro, N.; Dipierro, S.Purification and characterization of an ascorbate peroxidase from potato tuber mitochondriaPlant Physiol. Biochem.38773-7792000Solanum tuberosum-
439876Sano, S.; Ueda, M.; Kitajima, S.; Takeda, T.; Shigeoka, S.; Kurano, N.; Miyachi, S.; Miyake, C.; Yokota, A.Characterization of ascorbate peroxidases from unicellular red alga Galdieria partitaPlant Cell Physiol.42433-4402001Galdieria partita PubMed
439877Lloyd Raven, E.; Celik, A.; Cullis, P.M.; Sangar, R.; Sutcliffe, M.J.Engineering the active site of ascorbate peroxidaseBiochem. Soc. Trans.29105-1112001Pisum sativum PubMed
439878Moon, 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 generationBiochem. Biophys. Res. Commun.290457-4622002Glycine max PubMed
439879Pandey, N.; Singh, A.K.; Pathak, G.C.; Sharma, C.P.Effect of zinc on antioxidant response in maize (Zea mays L.) leavesIndian J. Exp. Biol.40954-9562002Zea mays PubMed
439880Wilkinson, S.R.; Obado, S.O.; Mauricio, I.L.; Kelly, J.M.Trypanosoma cruzi expresses a plant-like ascorbate-dependent hemoperoxidase localized to the endoplasmic reticulumProc. Natl. Acad. Sci. USA9913453-134582002Trypanosoma cruzi, Trypanosoma cruzi (Q8I1N3) PubMed
439881Kitajima, S.; Ueda, M.; Sano, S.; Miyake, C.; Kohchi, T.; Tomizawa, K.; Shigeoka, S.; Yokota, A.Stable form of ascorbate peroxidase from the red alga Galdieria partita similar to both chloroplastic and cytosolic isoforms of higher plantsBiosci. Biotechnol. Biochem.662367-23752002Galdieria partita PubMed
654139Ghamsari, L.; Keyhani, E.The distinctive features of ascorbate peroxidase in dormant Crocus sativus L. cormActa Hort.650119-1252004Crocus sativus-
654378Karyotou, K.; Donaldson, R.P.Ascorbate peroxidase, a scavenger of hydrogen peroxide in glyoxysomal membranesArch. Biochem. Biophys.434248-2572005Ricinus communis PubMed
655435Lad, L.; Mewies, M.; Basran, J.; Scrutton, N.S.; Raven, E.L.Role of histidine 42 in ascorbate peroxidase. Kinetic analysis of the H42A and H42E variantsEur. J. Biochem.2693182-31922002Pisum sativum PubMed
655789Metcalfe, C.L.; Ott, M.; Patel, N.; Singh, K.; Mistry, S.C.; Goff, H.M.; Raven, E.L.Autocatalytic formation of green heme: evidence for H2O2-dependent formation of a covalent methionine-heme linkage in ascorbate peroxidaseJ. Am. Chem. Soc.12616242-162482004Pisum sativum PubMed
655921Wada, K.; Tada, T.; Nakamura, Y.; Ishikawa, T.; Yabuta, Y.; Yoshimura, K.; Shigeoka, S.; Nishimura, K.Crystal structure of chloroplastic ascorbate peroxidase from tobacco plants and structural insights into its instabilityJ. Biochem.134239-2442003Nicotiana tabacum PubMed
656405Gomez, J.M.; Jimenez, A.; Olmos, E.; Sevilla, F.Location and effects of long-term NaCl stress on superoxide dismutase and ascorbate peroxidase isoenzymes of pea (Pisum sativum cv. Puget) chloroplastsJ. Exp. Bot.55119-1302004Pisum sativum PubMed
656620Lokhande, S.D.; Ogawa, K.; Tanaka, A.; Hara, T.Effect of temperature on ascorbate peroxidase activity and flowering of Arabidopsis thaliana ecotypes under different light conditionsJ. Plant Physiol.16057-642003Arabidopsis thaliana PubMed
656625Tsai, Y.C.; Hong, C.Y.; Liu, L.F.; Kao, C.H.Expression of ascorbate peroxidase and glutathione reductase in roots of rice seedlings in response to NaCl and H2O2J. Plant Physiol.162291-2992005Oryza sativa, Oryza sativa (P48642) PubMed
656853Sharp, K.H.; Mewies, M.; Moody, P.C.; Raven, E.L.Crystal structure of the ascorbate peroxidase-ascorbate complexNat. Struct. Biol.10303-3072003Glycine max (Q43758) PubMed
657008Murgia, I.; Tarantino, D.; Vannini, C.; Bracale, M.; Carravieri, S.; Soave, C.Arabidopsis thaliana plants overexpressing thylakoidal ascorbate peroxidase show increased resistance to Paraquat-induced photooxidative stress and to nitric oxide-induced cell deathPlant J.38940-9532004Arabidopsis thaliana PubMed
657041Panchuk, II; Volkov, R.A.; Schoffl, F.Heat stress- and heat shock transcription factor-dependent expression and activity of ascorbate peroxidase in ArabidopsisPlant Physiol.129838-8532002Arabidopsis thaliana PubMed
657053Danna, C.H.; Bartoli, C.G.; Sacco, F.; Ingala, L.R.; Santa-Maria, G.E.; Guiamet, J.J.; Ugalde, R.A.Thylakoid-bound ascorbate peroxidase mutant exhibits impaired electron transport and photosynthetic activityPlant Physiol.1322116-21252003Triticum aestivum PubMed
657063Vacca, R.A.; de Pinto, M.C.; Valenti, D.; Passarella, S.; Marra, E.; De Gara, L.Production of reactive oxygen species, alteration of cytosolic ascorbate peroxidase, and impairment of mitochondrial metabolism are early events in heat shock-induced programmed cell death in tobacco Bright-Yellow 2 cellsPlant Physiol.1341100-11122004Nicotiana tabacum PubMed
657113Sharma, P.; Dubey, R.S.Ascorbate peroxidase from rice seedlings: properties of enzyme isoforms, effects of stresses and protective roles of osmolytesPlant Sci.167541-5502004Oryza sativa-
684930Kitajima, S.; Kitamura, M.; Koja, N.Triple mutation of Cys26, Trp35, and Cys126 in stromal ascorbate peroxidase confers H2O2 tolerance comparable to that of the cytosolic isoformBiochem. Biophys. Res. Commun.372918-9232008Nicotiana tabacum (Q9TNL9) PubMed
685002Kangasjaervi, S.; Lepistoe, A.; Haennikaeinen, K.; Piippo, M.; Luomala, E.M.; Aro, E.M.; Rintamaeki, E.Diverse roles for chloroplast stromal and thylakoid-bound ascorbate peroxidases in plant stress responsesBiochem. J.412275-2852008Arabidopsis thaliana (Q42592), Arabidopsis thaliana (Q42593), Arabidopsis thaliana PubMed
685131Pipirou, 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 peroxidaseBiochemistry462174-21802007Glycine max (Q43758) PubMed
685177Efimov, 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 peroxidaseBiochemistry468017-80232007Glycine max PubMed
685400Yadav, 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 enzymeBiochim. Biophys. Acta1784863-8712008Leishmania major PubMed
685676Ishikawa, T.; Shigeoka, S.Recent advances in ascorbate biosynthesis and the physiological significance of ascorbate peroxidase in photosynthesizing organismsBiosci. Biotechnol. Biochem.721143-11542008Arabidopsis sp., Chlamydomonas sp. W80 (Q9SXL5), Euglena gracilis (Q8LP26), Galdieria partita, Galdieria sulphuraria, Leishmania major (Q4Q3K2), Trypanosoma cruzi (Q8I1N3) PubMed
686657Kitajima, S.; Shimaoka, T.; Kurioka, M.; Yokota, A.Irreversible cross-linking of heme to the distal tryptophan of stromal ascorbate peroxidase in response to rapid inactivation by H2O2FEBS J.2743013-30202007Nicotiana tabacum (Q9TNL9) PubMed
686710Kitajima, S.; Kurioka, M.; Yoshimoto, T.; Shindo, M.; Kanaori, K.; Tajima, K.; Oda, K.A cysteine residue near the propionate side chain of heme is the radical site in ascorbate peroxidaseFEBS J.275470-4802008Galdieria partita, Nicotiana tabacum, Nicotiana tabacum (Q9TNL9) PubMed
688083Hong, C.Y.; Hsu, Y.T.; Tsai, Y.C.; Kao, C.H.Expression of ascorbate peroxidase 8 in roots of rice (Oryza sativa L.) seedlings in response to NaClJ. Exp. Bot.583273-32832007Oryza sativa, Oryza sativa (P0C0L0), Oryza sativa (P0C0L1), Oryza sativa (Q0JEQ2), Oryza sativa (Q10N21), Oryza sativa (Q69SV0), Oryza sativa (Q6ZJJ1), Oryza sativa (Q7XJ02), Oryza sativa (Q9FE01) PubMed
688200Liu, K.; Shen, L.; Wang, J.; Sheng, J.Rapid inactivation of chloroplastic ascorbate peroxidase is responsible for oxidative modification to Rubisco in tomato (Lycopersicon esculentum) under cadmium stressJ. Integr. Plant Biol.50415-4262008Solanum lycopersicum PubMed
688913Lu, H.; Han, R.L.; Jiang, X.N.Heterologous expression and characterization of a proxidomal ascorbate peroxidase from Populus tomentosaMol. Biol. Rep.3621-272007Populus tomentosa, Populus tomentosa (Q5S1V5) PubMed
689240Li, H.B.; Qin, Y.M.; Pang, Y.; Song, W.Q.; Mei, W.Q.; Zhu, Y.X.A cotton ascorbate peroxidase is involved in hydrogen peroxide homeostasis during fibre cell developmentNew Phytol.175462-4712007Gossypium hirsutum (A7KIX5), Gossypium hirsutum PubMed
689350Chagas, R.M.; Silveira, J.A.; Ribeiro, R.V.; Vitorello, V.A.; Carrer, H.Photochemical damage and comparative performance of superoxide dismutase and ascorbate peroxidase in sugarcane leaves exposed to paraquat-induced oxidative stressPestic. Biochem. Physiol.90181-1882008Saccharum officinarum-
689427Shi, 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 floodingPhytochemistry691295-13032008Glycine max, Glycine max (Q76LA8) PubMed
689513Lu, Z.; Liu, D.; Liu, S.Two rice cytosolic ascorbate peroxidases differentially improve salt tolerance in transgenic ArabidopsisPlant Cell Rep.261909-19172007Oryza sativa, Oryza sativa (Q10N21), Oryza sativa (Q9FE01) PubMed
689652Kavitha, K.; Venkataraman, G.; Parida, A.An oxidative and salinity stress induced peroxisomal ascorbate peroxidase from Avicennia marina: Molecular and functional characterizationPlant Physiol. Biochem.46794-8042008Avicennia marina (A7LIY1), Avicennia marina PubMed
694642Burritt, D.J.The polycyclic aromatic hydrocarbon phenanthrene causes oxidative stress and alters polyamine metabolism in the aquatic liverwort Riccia fluitans LPlant Cell Environ.311416-14312008Riccia fluitans PubMed
696216Meharenna, Y.T.; Oertel, P.; Bhaskar, B.; Poulos, T.L.Engineering ascorbate peroxidase activity into cytochrome c peroxidaseBiochemistry4710324-103322008Saccharomyces cerevisiae PubMed
696257Badyal, 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 peroxidaseBiochemistry474403-44092008Glycine max (Q43758) PubMed
696567Zhou, B.; Guo, Z.Calcium is involved in the abscisic acid-induced ascorbate peroxidase, superoxide dismutase and chilling resistance in Stylosanthes guianensisBiol. Plant.5363-682009Stylosanthes guianensis-
697013Xu, W.; Shi, W.; Liu, F.; Ueda, A.; Takabe, T.Enhanced zinc and cadmium tolerance and accumulation in transgenic Arabidopsis plants constitutively overexpressing a barley gene (HvAPX1) that encodes a peroxisomal ascorbate peroxidaseBotany86567-5752008Hordeum vulgare-
697682Dolai, 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 damageEukaryot. Cell81721-17312009Leishmania major PubMed
698047Dolai, S.; Yadav, R.K.; Pal, S.; Adak, S.Leishmania major ascorbate peroxidase overexpression protects cells against reactive oxygen species-mediated cardiolipin oxidationFree Radic. Biol. Med.451520-15292008Leishmania major, Leishmania major 5ASKH PubMed
698848Koussevitzky, S.; Suzuki, N.; Huntington, S.; Armijo, L.; Sha, W.; Cortes, D.; Shulaev, V.; Mittler, R.Ascorbate peroxidase 1 plays a key role in the response of Arabidopsis thaliana to stress combinationJ. Biol. Chem.28334197-342032008Arabidopsis thaliana PubMed
699802Reddy, R.A.; Kumar, B.; Reddy, P.S.; Mishra, R.N.; Mahanty, S.; Kaul, T.; Nair, S.; Sopory, S.K.; Reddy, M.K.Molecular cloning and characterization of genes encoding Pennisetum glaucum ascorbate peroxidase and heat-shock factor: interlinking oxidative and heat-stress responsesJ. Plant Physiol.1661646-16592009Cenchrus americanus (A4ZYP9), Cenchrus americanus PubMed
700220Najami, N.; Janda, T.; Barriah, W.; Kayam, G.; Tal, M.; Guy, M.; Volokita, M.Ascorbate peroxidase gene family in tomato: Its identification and characterizationMol. Genet. Genomics279171-1822008Solanum lycopersicum (Q09Y74), Solanum lycopersicum (Q09Y76), Solanum lycopersicum (Q09Y77), Solanum lycopersicum (Q09Y78), Solanum lycopersicum (Q3I5C3), Solanum lycopersicum (Q3I5C4), Solanum lycopersicum (Q3SC88), Solanum lycopersicum, Solanum pennellii PubMed
700626Kitajima, S.Hydrogen peroxide-mediated inactivation of two chloroplastic peroxidases, ascorbate peroxidase and 2-cys peroxiredoxinPhotochem. Photobiol.841404-14092008Embryophyta PubMed
700703Li, Y.; Hai, R.; Du, X.; Jiang, X.; Lu, H.Over-expression of a Populus peroxisomal ascorbate peroxidase (PpAPX) gene in tobacco plants enhances stress tolerancePlant Breed.128404-4102009Populus tomentosa (Q5S1V5)-
700728Hirooka, S.; Misumi, O.; Yoshida, M.; Mori, T.; Nishida, K.; Yagisawa, F.; Yoshida, Y.; Fujiwara, T.; Kuroiwa, H.; Kuroiwa, T.Expression of the Cyanidioschyzon merolae stromal ascorbate peroxidase in Arabidopsis thaliana enhances thermotolerancePlant Cell Rep.281881-18932009Arabidopsis thaliana, Cyanidioschyzon merolae PubMed
700842Qin, Y.M.; Hu, C.Y.; Zhu, Y.X.The ascorbate peroxidase regulated by H(2)O(2) and ethylene is involved in cotton fiber cell elongation by modulating ROS homeostasisPlant Signal. Behav.3194-1962008Gossypium hirsutum (A7KIX5), Gossypium hirsutum (C6ZDA9), Gossypium hirsutum (C6ZDB0), Gossypium hirsutum, Gossypium hirsutum (Q39780) PubMed
700843Hong, C.Y.; Kao, C.H.NaCl-induced expression of ascorbate peroxidase 8 in roots of rice (Oryza sativa L.) seedlings is not associated with osmotic componentPlant Signal. Behav.3199-2012008Oryza sativa PubMed
710779Hu, Z.; Shen, Y.; Shen, F.; Su, X.Effects of feeding Clostera anachoreta on hydrogen peroxide accumulation and activities of peroxidase, catalase, and ascorbate peroxidase in Populus simonii × P. pyramidalis Opera 8277 leavesActa Physiol. Plant.20091-82009Populus simonii x Populus pyramidalis-
710788Liu, Z.; Yue, Y.; Xiang, J.; Wang, J.; Wu, J.; Li, X.; Yang, Y.Isolation of an ascorbate peroxidase in Brassica napus and analysis of its specific interaction with ATP6Afr. J. Biotechnol.92050-20552010Brassica napus (C5IUM6)-
711139Ishikawa, T.; Tajima, N.; Nishikawa, H.; Gao, Y.; Rapolu, M.; Shibata, H.; Sawa, Y.; Shigeoka, S.Euglena gracilis ascorbate peroxidase forms an intramolecular dimeric structure: its unique molecular characterizationBiochem. J.426125-1342010Euglena gracilis PubMed
713220Haghjou, M.M.; Shariati, M.; Smirnoff, N.The effect of acute high light and low temperature stresses on the ascorbate-glutathione cycle and superoxide dismutase activity in two Dunaliella salina strainsPhysiol. Plant.135272-2802009Dunaliella salina, Dunaliella salina IR-1 and Gh-U PubMed
713234Bonsager, B.C.; Shahpiri, A.; Finnie, C.; Svensson, B.Proteomic and activity profiles of ascorbate-glutathione cycle enzymes in germinating barley embryoPhytochemistry711650-16562010Hordeum vulgare, Hordeum vulgare (O23983), Hordeum vulgare (Q945R5) PubMed
713299Sajitha Rajan, S.; Murugan, K.Purification and kinetic characterization of the liverwort Pallavicinia lyelli (Hook.) S. Gray. cytosolic ascorbate peroxidasePlant Physiol. Biochem.48758-7632010Pallavicinia lyellii PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 1.11.1.11)
ExplorEnz
ExPASy
KEGG
MetaCyc
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)