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Information on EC 1.11.1.7 - peroxidase and Organism(s) Armoracia rusticana and UniProt Accession K7ZW28
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1.11.1.7 peroxidaseIUBMB Comments
Heme proteins with histidine as proximal ligand. The iron in the resting enzyme is Fe(III). They also peroxidize non-phenolic substrates such as 3,3',5,5'-tetramethylbenzidine (TMB) and 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS). Certain peroxidases (e.g. lactoperoxidase, SBP) oxidize bromide, iodide and thiocyanate.
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Word Map
- 1.11.1.7
-
retrograde
-
dorsal
- nerve
- nuclei
-
medial
-
afferent
- fiber
-
tracer
- spinal
-
ventral
-
ipsilateral
- cord
-
rostrally
-
innervation
-
contralateral
- dendrite
-
caudal
-
anterograde
- ganglion
- posterior
-
electrode
- agglutinin
- reticular
-
tracing
- erythropoietin
- peroxidases
- lamina
- motoneuron
- thalamic
-
trigeminal
-
geniculate
-
topographic
-
arbor
- colliculus
-
dorsolateral
-
somata
-
ventrolateral
-
boutons
- collateral
-
ventromedial
- commissure
-
vestibular
- pontine
-
dorsomedial
-
raphe
-
send
-
mesencephalic
-
iontophoretic
-
immunosensors
- tegmental
- analysis
- medicine
- nutrition
- degradation
- synthesis
- food industry
- agriculture
The taxonomic range for the selected organisms is: Armoracia rusticana
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
2
phenolic donor
+
=
2
phenoxyl radical of the donor
+
2
Synonyms
horseradish peroxidase, horseradish peroxidase (hrp), rhepo, lactoperoxidase, eosinophil peroxidase, guaiacol peroxidase, heme peroxidase, rubrerythrin, cyp119, thiol peroxidase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
eosinophil peroxidase
-
-
-
-
extensin peroxidase
-
-
-
-
guaiacol peroxidase
-
-
-
-
heme peroxidase
-
-
-
-
horseradish peroxidase
horseradish peroxidase (HRP)
-
-
-
-
HRP
HRPC
Japanese radish peroxidase
-
-
-
-
lactoperoxidase
-
-
-
-
MPO
-
-
-
-
myeloperoxidase
-
-
-
-
oxyperoxidase
-
-
-
-
protoheme peroxidase
-
-
-
-
pyrocatechol peroxidase
-
-
-
-
rHRP1
-
apo-horseradish peroxidase constituted with the artificial prostethic group heminD1
rHRP2
-
apo-horseradish peroxidase constituted with the artificial prostethic group heminD2
scopoletin peroxidase
-
-
-
-
thiocyanate peroxidase
-
-
-
-
verdoperoxidase
-
-
-
-
horseradish peroxidase
-
-
HRP
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
phenolic donor:hydrogen-peroxide oxidoreductase
Heme proteins with histidine as proximal ligand. The iron in the resting enzyme is Fe(III). They also peroxidize non-phenolic substrates such as 3,3',5,5'-tetramethylbenzidine (TMB) and 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS). Certain peroxidases (e.g. lactoperoxidase, SBP) oxidize bromide, iodide and thiocyanate.
CAS REGISTRY NUMBER
COMMENTARY
9003-99-0
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
? + H2O
-
-
-
?
(2Z)-2-(4-aminophenyl)-3-(1H-indol-2-yl)prop-2-enenitrile + H2O2
?
-
-
-
-
?
(2Z)-2-(4-aminophenyl)-3-(4-hydroxyphenyl)prop-2-enenitrile + H2O2
?
-
-
-
-
?
(2Z)-2-(4-aminophenyl)-3-(9-ethyl-9H-carbazol-3-yl)prop-2-enenitrile + H2O2
?
-
-
-
-
?
(2Z)-2-(4-aminophenyl)-3-anthracen-9-ylprop-2-enenitrile + H2O2
?
-
-
-
-
?
(2Z)-2-(4-aminophenyl)-3-thiophen-2-ylprop-2-enenitrile + H2O2
?
-
-
-
-
?
(2Z)-3-(1H-indol-3-yl)-2-(4-nitrophenyl)prop-2-enenitrile + H2O2
?
-
-
-
-
?
(2Z)-3-(4-hydroxyphenyl)-2-(4-nitrophenyl)prop-2-enenitrile + H2O2
?
-
-
-
-
?
(2Z)-3-[4-(dimethylamino)phenyl]-2-(4-nitrophenyl)prop-2-enenitrile + H2O2
?
-
-
-
-
?
(2Z,4E)-2-(4-aminophenyl)-5-[4-(dimethylamino)phenyl]penta-2,4-dienenitrile + H2O2
?
-
-
-
-
?
1-(1,3-dioxolan-2-ylmethyl)-4-[(E)-2-[4-[4-(2-hydroxyethyl)piperazin-1-yl]phenyl]ethenyl]pyridinium bromide + H2O2
?
-
-
-
-
?
1-(1,3-dioxolan-2-ylmethyl)-4-[(E)-2-[4-[4-(2-hydroxyethyl)piperazin-1-yl]phenyl]ethenyl]pyridinium perchlorate + H2O2
?
-
-
-
-
?
1-butyl-4-[(E)-2-(1H-indol-3-yl)ethenyl]quinolinium perchlorate + H2O2
?
-
-
-
-
?
1-ethyl-4-[(E)-2-(1H-indol-3-yl)ethenyl]quinolinium iodide + H2O2
?
-
-
-
-
?
1-ethyl-4-[(E)-2-(1H-pyrrol-2-yl)ethenyl]quinolinium iodide + H2O2
?
-
-
-
-
?
1-ethyl-4-[(E)-2-thiophen-2-ylethenyl]quinolinium iodide + H2O2
?
-
-
-
-
?
1-methyl-4-[(E)-2-(1H-pyrrol-2-yl)ethenyl]pyridinium iodide + H2O2
?
-
-
-
-
?
1-methyl-4-[(E)-2-thiophen-2-ylethenyl]pyridinium iodide + H2O2
?
-
-
-
-
?
2 guaiacol + H2O2
3,3'-dimethoxy-4,4'-biphenylquinone + H2O
-
-
-
?
2,2'-azino-bis (3-ethylbenzthiazoline-6-sulphonic acid) + H2O2
? + H2O
-
-
-
?
2-(4-[4-[(E)-2-quinolin-2-ylethenyl]phenyl]piperazin-1-yl)ethanol perchlorate (salt) + H2O2
?
-
-
-
-
?
2-aminophenol + H2O2
2-amino-9,10a-dihydro-3H-phenoxazin-3-one
-
-
-
-
ir
2-chlorophenol + H2O2
?
-
optimal concentrations of 2-chlorophenol and H2O2 are 0.2 mM and 0.3 mM, respectively
-
-
r
2-[(1Z,3Z)-4-[4-(dimethylamino)phenyl]buta-1,3-dien-1-yl]-3-propyl-1,3-benzothiazol-3-ium iodide + H2O2
?
-
-
-
-
?
2-[(E)-2-[4-(diethylamino)phenyl]ethenyl]-3-propyl-1,3-benzothiazol-3-ium iodide + H2O2
?
-
-
-
-
?
2-[(E)-2-[4-(dimethylamino)naphthalen-1-yl]ethenyl]-3-ethyl-1,3-benzothiazol-3-ium iodide + H2O2
?
-
-
-
-
?
2-[(E)-2-[4-(dimethylamino)phenyl]ethenyl]-1-propylpyridinium iodide + H2O2
?
-
-
-
-
?
2-[(E)-2-[4-(dimethylamino)phenyl]ethenyl]-1-propylquinolinium iodide + H2O2
?
-
-
-
-
?
2-[(E)-2-[4-(dimethylamino)phenyl]ethenyl]-3-propyl-1,3-benzothiazol-3-ium iodide + H2O2
?
-
-
-
-
?
2-[(E)-2-[4-(diphenylamino)phenyl]ethenyl]-3-propyl-1,3-benzothiazol-3-ium iodide + H2O2
?
-
-
-
-
?
2-[(E)-2-[4-(diprop-2-en-1-ylamino)phenyl]ethenyl]-3-ethyl-1,3-benzothiazol-3-ium iodide + H2O2
?
-
-
-
-
?
2-[(E)-2-[4-[4-(2-hydroxyethyl)piperazin-1-yl]phenyl]ethenyl]-1-propylquinolinium iodide + H2O2
?
-
-
-
-
?
2-[(E)-2-[4-[4-(2-hydroxyethyl)piperazin-1-yl]phenyl]ethenyl]-3-propyl-1,3-benzothiazol-3-ium iodide + H2O2
?
-
-
-
-
?
2-[(E)-2-[4-[4-(2-hydroxyethyl)piperazin-1-yl]phenyl]ethenyl]-3-propyl-1,3-benzoxazol-3-ium iodide + H2O2
?
-
-
-
-
?
2-[(E)-2-[4-[bis(2-hydroxyethyl)amino]phenyl]ethenyl]-3-ethyl-1,3-benzothiazol-3-ium iodide + H2O2
?
-
-
-
-
?
2-[[4-(1,3-benzothiazol-2-yl)phenyl](ethyl)amino]ethanol + H2O2
?
-
-
-
-
?
3-(4-carboxybutyl)-2-[(E)-2-[4-(dimethylamino)phenyl]ethenyl]-1,3-benzothiazol-3-ium iodide + H2O2
?
-
-
-
-
?
3-(4-[(E)-2-[4-(dimethylamino)phenyl]ethenyl]quinolinium-1-yl)propanoate + H2O2
?
-
-
-
-
?
3-ethyl-2-[(E)-2-(9-ethyl-9H-carbazol-3-yl)ethenyl]-1,3-benzothiazol-3-ium iodide + H2O2
?
-
-
-
-
?
4-(4-[(E)-2-[4-(dimethylamino)phenyl]ethenyl]pyridinium-1-yl)butane-1-sulfonate + H2O2
?
-
-
-
-
?
4-[(1E,3E)-4-[4-(dimethylamino)phenyl]buta-1,3-dien-1-yl]-1-methylpyridinium iodide + H2O2
?
-
-
-
-
?
4-[(1E,3E)-4-[4-(dimethylamino)phenyl]buta-1,3-dien-1-yl]-1-pentylpyridinium iodide + H2O2
?
-
-
-
-
?
4-[(1Z)-3-[4-(dimethylamino)phenyl]prop-1-en-1-yl]-1-(2-propoxyethyl)quinolinium perchlorate + H2O2
?
-
-
-
-
?
4-[(1Z,3Z)-4-[4-(dimethylamino)phenyl]buta-1,3-dien-1-yl]-1-(2-propoxyethyl)quinolinium perchlorate + H2O2
?
-
-
-
-
?
4-[(1Z,3Z)-4-[4-(dimethylamino)phenyl]buta-1,3-dien-1-yl]-1-methylquinolinium iodide + H2O2
?
-
-
-
-
?
4-[(1Z,3Z)-4-[4-(dimethylamino)phenyl]buta-1,3-dien-1-yl]-1-propylquinolinium iodide + H2O2
?
-
-
-
-
?
4-[(1Z,3Z)-4-[4-(dimethylamino)phenyl]buta-1,3-dien-1-yl]-1-[2-(2-hydroxyethoxy)ethyl]quinolinium iodide + H2O2
?
-
-
-
-
?
4-[(E)-2-(1,3-benzothiazol-2-yl)ethenyl]-N,N-dimethylaniline + H2O2
?
-
-
-
-
?
4-[(E)-2-(1H-indol-3-yl)ethenyl]-1-methylquinolinium iodide + H2O2
?
-
-
-
-
?
4-[(E)-2-(9-ethyl-9H-carbazol-3-yl)ethenyl]-1-methylpyridinium iodide + H2O2
?
-
-
-
-
?
4-[(E)-2-benzo[g]quinolin-4-ylethenyl]-N,N-dimethylaniline + H2O2
?
-
-
-
-
?
4-[(E)-2-[4-(acetylamino)phenyl]ethenyl]-1-methylpyridinium iodide + H2O2
?
-
-
-
-
?
4-[(E)-2-[4-(acetylamino)phenyl]ethenyl]-1-methylquinolinium iodide + H2O2
?
-
-
-
-
?
4-[(E)-2-[4-(dimethylamino)naphthalen-1-yl]ethenyl]-1-methylpyridinium iodide + H2O2
?
-
-
-
-
?
4-[(E)-2-[4-(dimethylamino)phenyl]ethenyl]-1-(1,3-dioxolan-2-ylmethyl)pyridinium + H2O2
?
-
-
-
-
?
4-[(E)-2-[4-(dimethylamino)phenyl]ethenyl]-1-(1,3-dioxolan-2-ylmethyl)pyridinium bromide + H2O2
?
-
-
-
-
?
4-[(E)-2-[4-(dimethylamino)phenyl]ethenyl]-1-(2-ethoxyethyl)pyridinium bromide + H2O2
?
-
-
-
-
?
4-[(E)-2-[4-(dimethylamino)phenyl]ethenyl]-1-(2-hydroxyethyl)pyridinium bromide + H2O2
?
-
-
-
-
?
4-[(E)-2-[4-(dimethylamino)phenyl]ethenyl]-1-(2-hydroxyethyl)pyridinium iodide + H2O2
?
-
-
-
-
?
4-[(E)-2-[4-(dimethylamino)phenyl]ethenyl]-1-(3-methylbutyl)pyridinium bromide + H2O2
?
-
-
-
-
?
4-[(E)-2-[4-(dimethylamino)phenyl]ethenyl]-1-(5-ethoxy-5-oxopentyl)pyridinium perchlorate + H2O2
?
-
-
-
-
?
4-[(E)-2-[4-(dimethylamino)phenyl]ethenyl]-1-dodecylquinolinium bromide + H2O2
?
-
-
-
-
?
4-[(E)-2-[4-(dimethylamino)phenyl]ethenyl]-1-methylpyridinium iodide + H2O2
?
-
-
-
-
?
4-[(E)-2-[4-(dimethylamino)phenyl]ethenyl]-1-methylquinolinium iodide + H2O2
?
-
-
-
-
?
4-[(E)-2-[4-(dimethylamino)phenyl]ethenyl]-1-octylpyridinium bromide + H2O2
?
-
-
-
-
?
4-[(E)-2-[4-(dimethylamino)phenyl]ethenyl]-1-propylpyridinium iodide + H2O2
?
-
-
-
-
?
4-[(E)-2-[4-(dimethylamino)phenyl]ethenyl]-1-propylquinolinium iodide + H2O2
?
-
-
-
-
?
4-[(E)-2-[4-(diphenylamino)phenyl]ethenyl]-1-methylpyridinium iodide + H2O2
?
-
-
-
-
?
4-[(E)-2-[4-(diprop-2-en-1-ylamino)phenyl]ethenyl]-1-methylpyridinium iodide + H2O2
?
-
-
-
-
?
4-[(E)-2-[4-[4-(2-hydroxyethyl)piperazin-1-yl]phenyl]ethenyl]-1-propylpyridinium iodide + H2O2
?
-
-
-
-
?
4-[(E)-2-[4-[4-(2-hydroxyethyl)piperazin-1-yl]phenyl]ethenyl]-1-propylquinolinium iodide + H2O2
?
-
-
-
-
?
5-ethyl-6-phenyl-5,6-dihydrophenanthridine-3,8-diamine + H2O2
?
-
-
-
-
?
capsaicin + H2O2
5,5'-dicapsaicin + 4'-O-5-dicapsaicin ether + capsaicin polymers
-
-
-
-
?
chlorophyll a + H2O2
?
-
in the active centre of the enzyme the imidazole nitrogen of His-42plays a crucial role in the C-132 deprotonation of chlorophyll a, which results in the chlorophyll a enolate ion resonance hybrid. The chlorophyll enolate is then oxidized to the chlorophyll 132-radical
-
-
?
dihydrocapsaicin + H2O2
5,5-didihydrocapsaicin + 4'-O-5-didihydrocapsaicin ether + dihydrocapsaicin polymers
-
-
-
-
?
N,N-dimethyl-4-[(E)-2-quinolin-2-ylethenyl]aniline perchlorate + H2O2
?
-
-
-
-
?
p-hydroxyphenylacetamide + H2O2
? + H2O
-
a model compound of tyrosine residues in fibroins
-
-
?
p-phenylenediamine + H2O2
cyclohexa-2,5-diene-1,4-diimine + H2O
-
-
-
-
?
reduced 2,2'-azino-bis-(3-ethylbenzthiazole-6-sulfonic acid) + H2O2
oxidized 2,2'-azino-bis-(3-ethylbenzthiazole-6-sulfonic acid) + H2O
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
? + H2O
-
-
-
-
?
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
? + H2O
-
-
-
?
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
? + H2O
-
-
-
?
esculetin + H2O2
?
-
demonstration, that esculetin is no inhibitor, but a substrate of mushroom polyphenol oxidase (PPO) and horseradish peroxidase (POD)
-
-
?
guaiacol + H2O2
tetraguaiacol + H2O
-
-
-
-
?
guaiacol + H2O2
tetraguaiacol + H2O
-
optimal concentrations of guaiacol and H2O2 are 0.5 mM and 0.3 mM, respectively
-
-
r
phenol + H2O2
?
-
optimal concentrations of phenol and H2O2 are 0.2 mM and 0.3 mM, respectively
-
-
r
reduced 2,2'-azino-bis-(3-ethylbenzthiazole-6-sulfonic acid) + H2O2
oxidized 2,2'-azino-bis-(3-ethylbenzthiazole-6-sulfonic acid) + H2O
-
-
-
-
?
reduced 2,2'-azino-bis-(3-ethylbenzthiazole-6-sulfonic acid) + H2O2
oxidized 2,2'-azino-bis-(3-ethylbenzthiazole-6-sulfonic acid) + H2O
-
-
-
?
reduced 2,2'-azino-bis-(3-ethylbenzthiazole-6-sulfonic acid) + H2O2
oxidized 2,2'-azino-bis-(3-ethylbenzthiazole-6-sulfonic acid) + H2O
-
the catalytic activity of peroxidase in the oxidation process of reduced 2,2'-azino-bis-(3-ethylbenzthiazole-6-sulfonic acid) is found to depend on the nature and the amount of added salt. The influence of the salt on the buffer pH can be identified as one of the major reasons
-
-
?
additional information
?
-
-
direct electron transfer kinetics in horseradish peroxidase electrocatalysis
-
-
?
additional information
?
-
-
HRP in colloidal carbon microspheres/chitosan hybrid keeps its native bioactivity and has high affinity for H2O2
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
HRP in colloidal carbon microspheres/chitosan hybrid keeps its native bioactivity and has high affinity for H2O2
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
heme
-
-
heme
loss of a structural restraint in the proximal heme pocket of mutant enzyme T171S allows slippage of the proximal heme ligand, but only in the reduced state. This is a remarkably subtle and specific effect that appears to increase the flexibility of the reduced state of the mutant compared to that of the wild-type protein
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Tb3+
-
HRP bioactivity is slightly stimulated and reaches the maximum at 0.01 mM Tb3+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-butyl-3-methylimidazolium tetrafluoroborate
-
weak, non-competitive inhibitor
2,4-dinitroresorcinol
-
competitive inhibition of 3,3',5,5'-tetramethylbenzidine oxidation
2-amino-4-nitrophenol
-
competitive inhibition of 3,3',5,5'-tetramethylbenzidine oxidation
acetonitrile
-
about 98% activity is lost for native HRP after incubation in 50% (v/v) acetonitrile at 35°C for 3 h, native HRP only possess less than 20% activity in 30% (v/v) acetonitrile
butyl-3-methylimidazolium tetrafluoroborate
-
significantly weakens the binding affinity of guaiacol to HRP
gallic acid
-
competetive inhibition of 3,3',5,5'-tetramethylbenzidine oxidation
La3+
-
the formation of the La3+-HRP complex causes the destruction of the native structure of HRP molecule, leading to the decrease in the non-planarity of the porphyrin ring in the heme group of HRP molecule, and then in the exposure extent of active center, Fe(III) of the porphyrin ring of HRP molecule. Thus, the direct electrochemical and catalytic activities of HRP are decreased. When the molar ratio of La3+ and HRP is 10, the catalytic activity of HRP is decreased by 12% comparing with that of HRP in the absence of La3+
n-Hexanol
-
the enzymatic activity of horseradish peroxidase decreases upon addition of n-hexanol
phenoxy radical
phenylalanine residues are vulnerable to modification by phenoxyl radicals. Radical coupling does not change the secondary structure or the active site of HRP isoform C
resorcinol
-
competitive inhibition of 3,3',5,5'-tetramethylbenzidine oxidation
Tb3+
-
after treatment with 0.2 mM Tb3+, the HRP bioactivity in horseradish leaf is inhibited by 27.2% compared to the sample without Tb3+treatment
H2O2
-
3 mM, suicide inactivation. Addition of SDS to the reaction mixture intensifies the inactivation process
additional information
-
HRP-DNA conjugates reveal a reduced peroxidase activity
-
additional information
-
incorporation of an iron corrole into the apo-form of horseradish peroxidase leads to decreased catalytic activity as a result of the iron attaining the +4 oxidation state which causes poor binding and/or activation of H2O2 on the iron
-
additional information
-
enzyme does not exhibit any measurable substrate inhibition
-
additional information
-
no inhibition of enzyme activity when the concentrations of phenol and H2O2 are at or below 10 mM and 0.1 mM, respectively
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-aminothiazole
-
2 mM, 4fold, more than 2fold and 1.4fold activation of 3,3',5,5'-tetramethylbenzidine, o-phenylenediamine and 5-aminosalycylic acid oxidation, respectively
melamine
-
1 mM, approx. 2fold increase in kcat for oxidation of 3,3',5,5'-tetramethylbenzidine
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.95
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 6.5, 37°C
4.53
2,4,6-tribromophenol
-
pH 7.0, temperature not specified in the publication
5.1
2,4,6-Trichlorophenol
-
pH 7.0, temperature not specified in the publication
607
reduced 2,2'-azino-bis-(3-ethylbenzthiazole-6-sulfonic acid)
25°C, pH 5.0, mutant enzyme
additional information
additional information
-
Hofmeister specific-ion effects
-
0.99
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)
mutant N13D/N57S/N255D/N268D, pH 6.5, 30°C
1.01
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 6.5, 37°C
1.5
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)
wild-type, pH 6.5, 30°C
3.5
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 6.5, 37°C
5.4
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 7.0, temperature not specified in the publication
1.4
esculetin
-
KM as a kinetic constant of the POD/H2O2/ESC system at pH 7
2
esculetin
-
KM as a kinetic constant of the POD/H2O2/ESC system at pH 4.5
0.966
guaiacol
mutant F130A, pH 5, temperature not specified in the publication
0.966
guaiacol
wild-type isoform C, pH 5, temperature not specified in the publication
1.06
guaiacol
mutant F68A, pH 5, temperature not specified in the publication
1.72
guaiacol
mutant F143A, pH 5, temperature not specified in the publication
1.82
guaiacol
mutant F179A, pH 5, temperature not specified in the publication
2.04
guaiacol
mutant F142A, pH 5, temperature not specified in the publication
2.16
guaiacol
mutant F130A/F142A/ F143A/F179A, pH 5, temperature not specified in the publication
2.69
guaiacol
mutant F68A/F142A/ F143A/F179A, pH 5, temperature not specified in the publication
2.8
guaiacol
-
in the absence of 1-butyl-3-methylimidazolium tetrafluoroborate, in potassium phosphate buffer (20 mM, pH 7.0) at 25°C
2.8
guaiacol
-
in the absence of butyl-3-methylimidazolium tetrafluoroborate, at 25°C
4.1
guaiacol
-
in the presence of 5% (v/v) 1-butyl-3-methylimidazolium tetrafluoroborate, in potassium phosphate buffer (20 mM, pH 7.0) at 25°C
6.8
guaiacol
-
in the presence of 10% (v/v) 1-butyl-3-methylimidazolium tetrafluoroborate, in potassium phosphate buffer (20 mM, pH 7.0) at 25°C
7.8
guaiacol
-
in the presence of 15% (v/v) 1-butyl-3-methylimidazolium tetrafluoroborate, in potassium phosphate buffer (20 mM, pH 7.0) at 25°C
15.1
guaiacol
-
in the presence of 20% (v/v) 1-butyl-3-methylimidazolium tetrafluoroborate, in potassium phosphate buffer (20 mM, pH 7.0) at 25°C
22.5
guaiacol
-
in 25% (v/v) butyl-3-methylimidazolium tetrafluoroborate, at 25°C
22.5
guaiacol
-
in the presence of 25% (v/v) 1-butyl-3-methylimidazolium tetrafluoroborate, in potassium phosphate buffer (20 mM, pH 7.0) at 25°C
0.0052
H2O2
-
KM as a kinetic constant of the POD/H2O2/ESC system at pH 7
0.012
H2O2
-
2,4,6-trichlorophenol, pH 7.0, temperature not specified in the publication
0.05
H2O2
-
cosubstrate 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid), pH 7.0, temperature not specified in the publication
0.052
H2O2
-
KM as a kinetic constant of the POD/H2O2/ESC system at pH 4.5
0.093
H2O2
-
cosubstrate 2,4,6-tribromophenol, pH 7.0, temperature not specified in the publication
2.33
H2O2
-
HRP in colloidal carbon microspheres/chitosan hybrid, apparent Km value
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
571
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 7.0, temperature not specified in the publication
223
2,4,6-tribromophenol
-
pH 7.0, temperature not specified in the publication
52.5
2,4,6-Trichlorophenol
-
pH 7.0, temperature not specified in the publication
871
esculetin
-
kcat as a kinetic constant of the POD/H2O2/ESC system at pH 7
890
esculetin
-
kcat as a kinetic constant of the POD/H2O2/ESC system at pH 4.5
0.952
guaiacol
mutant F68A, pH 5, temperature not specified in the publication
1.24
guaiacol
mutant F142A, pH 5, temperature not specified in the publication
1.41
guaiacol
mutant F130A, pH 5, temperature not specified in the publication
1.44
guaiacol
wild-type isoform C, pH 5, temperature not specified in the publication
1.55
guaiacol
mutant F143A, pH 5, temperature not specified in the publication
1.83
guaiacol
mutant F179A, pH 5, temperature not specified in the publication
2.09
guaiacol
mutant F130A/F142A/ F143A/F179A, pH 5, temperature not specified in the publication
2.3
guaiacol
mutant F68A/F142A/ F143A/F179A, pH 5, temperature not specified in the publication
8.7
guaiacol
-
in the presence of 25% (v/v) 1-butyl-3-methylimidazolium tetrafluoroborate, in potassium phosphate buffer (20 mM, pH 7.0) at 25°C
9.3
guaiacol
-
in the presence of 20% (v/v) 1-butyl-3-methylimidazolium tetrafluoroborate, in potassium phosphate buffer (20 mM, pH 7.0) at 25°C
10.6
guaiacol
-
in the presence of 15% (v/v) 1-butyl-3-methylimidazolium tetrafluoroborate, in potassium phosphate buffer (20 mM, pH 7.0) at 25°C
10.9
guaiacol
-
in the presence of 10% (v/v) 1-butyl-3-methylimidazolium tetrafluoroborate, in potassium phosphate buffer (20 mM, pH 7.0) at 25°C
12.2
guaiacol
-
in the absence of 1-butyl-3-methylimidazolium tetrafluoroborate, in potassium phosphate buffer (20 mM, pH 7.0) at 25°C
12.4
guaiacol
-
in the presence of 5% (v/v) 1-butyl-3-methylimidazolium tetrafluoroborate, in potassium phosphate buffer (20 mM, pH 7.0) at 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.61
guaiacol
mutant F142A, pH 5, temperature not specified in the publication
0.86
guaiacol
mutant F68A/F142A/ F143A/F179A, pH 5, temperature not specified in the publication
0.89
guaiacol
mutant F143A, pH 5, temperature not specified in the publication
0.89
guaiacol
mutant F68A, pH 5, temperature not specified in the publication
1.01
guaiacol
mutant F179A, pH 5, temperature not specified in the publication
1.07
guaiacol
mutant F130A/F142A/ F143A/F179A, pH 5, temperature not specified in the publication
1.46
guaiacol
mutant F130A, pH 5, temperature not specified in the publication
1.49
guaiacol
wild-type isoform C, pH 5, temperature not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.65
-
crude enzyme, using guaiacol as substrate, in 50 mM phosphate buffer (pH 7.5), at 30°C
772.3
-
after 291fold purification, using guaiacol as substrate, in 50 mM phosphate buffer (pH 7.5), at 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5
7
-
the highest activity of the enzyme is observed in potassium dihydrogenphosphate/sodium hydroxide of pH 7.0
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 7.5
-
oxidation of 5-aminosalicylic acid, approx. 30% of maximal activity at pH 4.5 and pH 7.0, respectively
6 - 8
6 - 8
-
although peroxidase activity is comparable in the pH range of 6.0-7.5, significant decline in enzyme activity is observed when the pH is increased to above 8.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
42
-
thermal denaturation of isolated HRP occurs at temperatures above 42°C, and the enzyme activity decreases rapidly
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.8
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). K7ZW28_ARMRU
336
1
35029
TrEMBL
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
44000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 65000, SDS-PAGE, wild-type. x * 50000, SDS-PAGE, glycosylation mutant N13D/N57S/N255D/N268D
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F130A/F142A/ F143A/F179A
isoform HRP C, mutant shows marginal improvement in stability
F142A
isoform HRP C, mutation in a residue vulnerable to modification by phenoxyl radicals, mutant still exhibits rapid radical inactivation
F143A
isoform HRP C, mutation in a residue vulnerable to modification by phenoxyl radicals, mutant still exhibits rapid radical inactivation
F179A
isoform HRP C, mutation in a residue vulnerable to modification by phenoxyl radicals, mutant still exhibits rapid radical inactivation
F68A
isoform HRP C, mutation in a residue vulnerable to modification by phenoxyl radicals, mutant still exhibits rapid radical inactivation
F68A/F142A/F143A/F179A
isoform HRP C, dramatic enhancement of radical stability by retaining 41% of its initial activity in conditions when wild-type is completely inactivated
N13D/N57S/N255D/N268D
mutations introduced to reduce glycosylation during production in Pichia pastoris
T171S
loss of a structural restraint in the proximal heme pocket that allows slippage of the proximal heme ligand, but only in the reduced state. This is a remarkably subtle and specific effect that appears to increase the flexibility of the reduced state of the mutant compared to that of the wild-type protein. Significant change in the Fe2+/Fe3+ redox potential of the mutant T171S
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 9
-
the enzyme shows high stability between pH 4.0 and 9.0. At lower and higher pH values a significant reduction of the enzymatic activity is observed
726432
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
65 - 76.5
-
the melting temperature is at 70°C for the native enzyme and at 75.4°C for the cofactor-modified enzyme rHRP1 and at 76.5°C for the cofactor-modified enzyme rHRP2. the reconstituted HRPs with modified hemin show higher thermostability in aqueous buffer. After the exposure for 1.5 h at 65°C, native HRP retains only about 15% activity, the reconstituted HRPs, however, retained about 60% activity
60
half-life of wild-type 31.5 min, half-life of mutant N13D/N57S/N255D/N268D 173 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
cofactor modification(heminD1 in rHRP1 and heminD2 in rHRP2 instead of heme) increases the substrate affinity and catalytic efficiency both in aqueous buffer and some organic solvents, the catalytic efficiency for phenol oxidation is increased by about 55% for rHRP1 in aqueous buffer, and it is also increased by about 70% for rHRP1 in 10% (v/v) acetonitrile.
-
the optimal buffer for the assay of purified HRP is 50 mM phosphate buffer (pH 7.5)
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50 mM phosphate buffer (pH 7.5) containing 20% (v/v) glycerol, at least 6 months, less than 5% loss of activity
-
0-2°C, 50 mM phosphate buffer (pH 7.5), 48-72 h, 40-45% loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, ion-exchange chromatography and gel filtration
-
hydrophobic charge induction chromatography with 4-mercapto-ethyl-pyridine and Superdex 75 gel filtration
-
ultrasonication, ammonium sulfate salt precipitation, and phenyl Sepharose column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Pichia pastoris
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
expression of 19 individual HRP isoenzymes recombinantly in the yeast Pichia pastoris and optimization of a 2-step purification strategy
analysis
synthesis
analysis
-
application of molecular absorption properties of horseradish peroxidase for self-indicating enzymatic interactions and analytical methods. This method can be applied for glucose determination where there is a low concentration (or an absence) of proteins
analysis
-
use of nanoporous TiO2 electrodes as a substrate for enzyme immobilization in order to enhance the electron transport across the semiconductor electrode-electrolyte interface. The immobilized HRP enzyme is stable and the overall electron transfer process is predominantly controlled by a diffusion process. The application for H2O2 biosensors is demonstrated by monitoring its reduction process using cyclic voltammetry
synthesis
expression of 19 individual HRP isoenzymes recombinantly in the yeast Pichia pastoris and optimization of a 2-step purification strategy
synthesis
-
preparation of starch-g-poly(butyl acrylate) copolymers using horseradish peroxidase, in the presence of hydrogen peroxide and acetylacetone. Poly(butyl acrylate) is successfully grafted onto starch by HRP-mediated graft copolymerization, improving the thermal stability of starch
synthesis
protein engineering to obtain an active and stable HRP variant with reduced surface glycosylation during production in Pichia pastoris. Mutant N13D/N57S/N255D/N268D produced in the Pichia pastoris benchmark strain shows considerable catalytic activity and thermal stability and is less glycosylated
synthesis
-
self-crosslinking of fibroin molecules and p-hydroxyphenylacetamide, as a model compound of tyrosine residues in fibroins, using the hydrogen peroxide-horseradish peroxidase system. Incubation leads to p-hydroxyphenylacetamide polymerization, and the molecular weight of fibroin proteins is also noticeably increased by treatment. The mechanical properties and thermal behavior for the modified fibroin membrane are improved. The obtained membrane exhibits good biocompatibility
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Goodwin, D.C.; Hertwig, K.M.
Peroxidase-catalyzed oxidation of capsaicinoids: steady-state and transient-state kinetic studies
Arch. Biochem. Biophys.
417
18-26
2003
Armoracia rusticana
Karasyova, E.I.; Naumchik, I.V.; Metelitza, D.I.
Activation of peroxidase-catalyzed oxidation of aromatic amines with 2-aminothiazole and melamine
Biochemistry
68
54-62
2003
Armoracia rusticana
Gilabert, M.A.; Fenoll, L.G.; Garcia-Molina, F.; Tudela, J.; Garcia-Canovas, F.; Rodriguez-Lopez, J.N.
Kinetic characterization of phenol and aniline derivates as substrates of peroxidase
Biol. Chem.
385
795-800
2004
Armoracia rusticana
Kamal, J.K.; Behere, D.V.
Activity, stability and conformational flexibility of seed coat soybean peroxidase
J. Inorg. Biochem.
94
236-242
2003
Armoracia rusticana, Glycine max
Howes, B.D.; Brissett, N.C.; Doyle, W.A.; Smith, A.T.; Smulevich, G.
Spectroscopic and kinetic properties of the horseradish peroxidase mutant T171S. Evidence for selective effects on the reduced state of the enzyme
FEBS J.
272
5514-5521
2005
Armoracia rusticana (P00433), Armoracia rusticana
Sanz, V.; de Marcos, S.; Castillo, J.R.; Galban, J.
Application of molecular absorption properties of horseradish peroxidase for self-indicating enzymatic interactions and analytical methods
J. Am. Chem. Soc.
127
1038-1048
2005
Armoracia rusticana
Nazari, K.; Mahmoudi, A.; Shahrooz, M.; Khodafarin, R.; Moosavi-Movahedi, A.A.
Suicide-peroxide inactivation of horseradish peroxidase in the presence of sodium n-dodecyl sulphate: a study of the enzyme deactivation kinetics
J. Enzyme Inhib. Med. Chem.
20
285-292
2005
Armoracia rusticana
Bauduin, P.; Nohmie, F.; Touraud, D.; Neueder, R.; Kunz, W.; Ninham, B.W.
Hofmeister specific-ion effects on enzyme activity and buffer pH: Horseradish peroxidase in citrate buffer
J. Mol. Liq.
123
14-19
2005
Armoracia rusticana
-
Andreu, R.; Ferapontova, E.E.; Gorton, L.; Calvente, J.J.
Direct electron transfer kinetics in horseradish peroxidase electrocatalysis
J. Phys. Chem. B
111
469-477
2007
Armoracia rusticana
Ding, C.; Zhang, M.; Zhao, F.; Zhang, S.
Disposable biosensor and biocatalysis of horseradish peroxidase based on sodium alginate film and room temperature ionic liquid
Anal. Biochem.
378
32-37
2008
Armoracia rusticana
Kamal, J.K.; Behere, D.V.
Kinetic stabilities of soybean and horseradish peroxidases
Biochem. Eng. J.
38
110-114
2008
Glycine max (O22443), Armoracia rusticana (P00433)
-
Munoz-Munoz, J.L.; Garcia-Molina, F.; Varon, R.; Rodriguez-Lopez, J.N.; Garcia-Canovas, F.; Tudela, J.
Kinetic characterization of the oxidation of esculetin by polyphenol oxidase and peroxidase
Biosci. Biotechnol. Biochem.
71
390-396
2007
Armoracia rusticana
Hong, E.S.; Kwon, O.Y.; Ryu, K.
Strong substrate-stabilizing effect of a water-miscible ionic liquid [BMIM][BF(4)] in the catalysis of horseradish peroxidase
Biotechnol. Lett.
30
529-533
2008
Armoracia rusticana
Bhatti, H.N.; Akbar, M.N.; Zia, M.A.
Kinetics of irreversible thermal denaturation of horseradish peroxidase
J. Chem. Soc. Pak.
29
99-102
2007
Armoracia rusticana
-
Bhatnagar, P.K.; Das, D.; Suresh, M.R.
Sequential affinity purification of peroxidase tagged bispecific anti-SARS-CoV antibodies on phenylboronic acid agarose
J. Chromatogr. B
863
235-241
2008
Armoracia rusticana
Lee, Y.M.; Kwon, O.Y.; Yoo, I.K.; Ryu, K.G.
Effect of ionic liquid on the kinetics of peroxidase catalysis
J. Microbiol. Biotechnol.
17
600-603
2007
Armoracia rusticana
Krieg, R.; Eitner, A.; Guenther, W.; Schuerer, C.; Lindenau, J.; Halbhuber, K.J.
N,N-dialkylaminostyryl dyes: specific and highly fluorescent substrates of peroxidase and their application in histochemistry
J. Mol. Histol.
39
169-191
2008
Armoracia rusticana
Kamidate, T.; Maruya, M.; Tani, H.; Ishida, A.
Application of 4-iodophenol-enhanced luminol chemiluminescence to direct detection of horseradish peroxidase encapsulated in liposomes
Anal. Sci.
25
1163-1166
2009
Armoracia rusticana
Nagaraja, P.; Shivakumar, A.; Kumar Shrestha, A.
Development and evaluation of kinetic spectrophotometric assays for horseradish peroxidase by catalytic coupling of paraphenylenediamine and mequinol
Anal. Sci.
25
1243-1248
2009
Armoracia rusticana
Feng, J.Y.; Liu, J.Z.; Ji, L.N.
Thermostability, solvent tolerance, catalytic activity and conformation of cofactor modified horseradish peroxidase
Biochimie
90
1337-1346
2008
Armoracia rusticana
Glettenberg, M.; Niemeyer, C.M.
Tuning of peroxidase activity by covalently tethered DNA oligonucleotides
Bioconjug. Chem.
20
969-975
2009
Armoracia rusticana
Nagaraja, P.; Shivakumar, A.; Shrestha, A.K.
Peroxidase-catalyzed oxidative coupling of paraphenylenediamine with 3-dimethylaminobenzoic acid: application in crude plant extracts
J. Agric. Food Chem.
57
5173-5177
2009
Armoracia rusticana
Roth, J.P.; Cramer, C.J.
Direct examination of H2O2 activation by a heme peroxidase
J. Am. Chem. Soc.
130
7802-7803
2008
Armoracia rusticana
Matsuo, T.; Hayashi, A.; Abe, M.; Matsuda, T.; Hisaeda, Y.; Hayashi, T.
Meso-unsubstituted iron corrole in hemoproteins: Remarkable differences in effects on peroxidase activities between myoglobin and horseradish peroxidase
J. Am. Chem. Soc.
131
15124-15125
2009
Armoracia rusticana
Guo, S.; Cao, R.; Lu, A.; Zhou, Q.; Lu, T.; Ding, X.; Li, C.; Huang, X.
One of the possible mechanisms for the inhibition effect of Tb(III) on peroxidase activity in horseradish (Armoracia rusticana) treated with Tb(III)
J. Biol. Inorg. Chem.
13
587-597
2008
Armoracia rusticana
Biswas, R.; Das, A.R.; Pradhan, T.; Touraud, D.; Kunz, W.; Mahiuddin, S.
Spectroscopic studies of catanionic reverse microemulsion: correlation with the superactivity of horseradish peroxidase enzyme in a restricted environment
J. Phys. Chem. B
112
6620-6628
2008
Armoracia rusticana
Violante-Mota, F.; Tellechea, E.; Moran, J.F.; Sarath, G.; Arredondo-Peter, R.
Analysis of peroxidase activity of rice (Oryza sativa) recombinant hemoglobin 1: Implications for in vivo function of hexacoordinate non-symbiotic hemoglobins in plants
Phytochemistry
71
21-26
2010
Oryza sativa, Armoracia rusticana (P00433), Armoracia rusticana
Chen, X.; Li, C.; Liu, Y.; Du, Z.; Xu, S.; Li, L.; Zhang, M.; Wang, T.
Electrocatalytic activity of horseradish peroxidase/chitosan/carbon microsphere microbiocomposites to hydrogen peroxide
Talanta
77
37-41
2008
Armoracia rusticana
Koelsch, M.; Mallak, R.; Graham, G.G.; Kajer, T.; Milligan, M.K.; Nguyen, L.Q.; Newsham, D.W.; Keh, J.S.; Kettle, A.J.; Scott, K.F.; Ziegler, J.B.; Pattison, D.I.; Fu, S.; Hawkins, C.L.; Rees, M.D.; Davies, M.J.
Acetaminophen (paracetamol) inhibits myeloperoxidase-catalyzed oxidant production and biological damage at therapeutically achievable concentrations
Biochem. Pharmacol.
79
1156-1164
2010
Armoracia rusticana
Petacci, F.; Freitas, S.S.; Brunetti, I.L.; Khalil, N.M.
Inhibition of peroxidase activity and scavenging of reactive oxygen species by astilbin isolated from Dimorphandra mollis (Fabaceae, Caesalpinioideae)
Biol. Res.
43
63-74
2010
Armoracia rusticana
Lavery, C.B.; Macinnis, M.C.; Macdonald, M.J.; Williams, J.B.; Spencer, C.A.; Burke, A.A.; Irwin, D.J.; D'Cunha, G.B.
Purification of peroxidase from horseradish (Armoracia rusticana) roots
J. Agric. Food Chem.
58
8471-8476
2010
Armoracia rusticana
Guo, S.; Wang, L.; Lu, A.; Lu, T.; Ding, X.; Huang, X.
Inhibition mechanism of lanthanum ion on the activity of horseradish peroxidase in vitro
Spectrochim. Acta A. Mol. Biomol. Spectrosc.
75
936-940
2010
Armoracia rusticana
Gumiero, A.; Murphy, E.J.; Metcalfe, C.L.; Moody, P.C.; Raven, E.L.
An analysis of substrate binding interactions in the heme peroxidase enzymes: a structural perspective
Arch. Biochem. Biophys.
500
13-20
2010
Armoracia rusticana (P00433)
Zakharova, G.S.; Uporov, I.V.; Tishkov, V.I.
Horseradish peroxidase: modulation of properties by chemical modification of protein and heme
Biochemistry
76
1391-1401
2011
Armoracia rusticana
Hynninen, P.H.; Kaartinen, V.; Kolehmainen, E.
Horseradish peroxidase-catalyzed oxidation of chlorophyll a with hydrogen peroxide: characterization of the products and mechanism of the reaction
Biochim. Biophys. Acta
1797
531-542
2010
Armoracia rusticana
Spadiut, O.; Rossetti, L.; Dietzsch, C.; Herwig, C.
Purification of a recombinant plant peroxidase produced in Pichia pastoris by a simple 2-step strategy
Protein Expr. Purif.
86
89-97
2012
Armoracia rusticana
Deva Kumar, E.T.; Ganesh, V.
Immobilization of horseradish peroxidase enzyme on nanoporous titanium dioxide electrodes and its structural and electrochemical characterizations
Appl. Biochem. Biotechnol.
174
1043-1058
2014
Armoracia rusticana
Zhou, B.; Wang, P.; Cui, L.; Yu, Y.; Deng, C.; Wang, Q.; Fan, X.
Self-crosslinking of silk fibroin using H2O2-horseradish peroxidase system and the characteristics of the resulting fibroin membranes
Appl. Biochem. Biotechnol.
182
1548-1563
2017
Armoracia rusticana
Kim, S.J.; Joo, J.C.; Song, B.K.; Yoo, Y.J.; Kim, Y.H.
Engineering a horseradish peroxidase C stable to radical attacks by mutating multiple radical coupling sites
Biotechnol. Bioeng.
112
668-676
2015
Armoracia rusticana (P80679), Armoracia rusticana
Capone, S.; Corajevic, L.; Bonifert, G.; Murth, P.; Maresch, D.; Altmann, F.; Herwig, C.; Spadiut, O.
Combining protein and strain engineering for the production of glyco-engineered horseradish peroxidase C1A in Pichia pastoris
Int. J. Mol. Sci.
16
23127-23142
2015
Armoracia rusticana (P00433), Armoracia rusticana
Kong, M.; Zhang, Y.; Li, Q.; Dong, R.; Gao, H.
Kinetics of horseradish peroxidase-catalyzed nitration of phenol in a biphasic system
J. Microbiol. Biotechnol.
27
297-305
2017
Armoracia rusticana
Zhao, J.; Lu, C.; Franzen, S.
Distinct enzyme-substrate interactions revealed by two dimensional kinetic comparison between dehaloperoxidase-hemoglobin and horseradish peroxidase
J. Phys. Chem. B
119
12828-12837
2015
Armoracia rusticana, Amphitrite ornata, Amphitrite ornata (Q9NAV8)
Wang, S.; Xu, J.; Wang, Q.; Fan, X.; Yu, Y.; Wang, P.; Zhang, Y.; Yuan, J.; Cavaco-Paulo, A.
Preparation and rheological properties of starch-g-poly(butyl acrylate) catalyzed by horseradish peroxidase
Process Biochem.
59
104-110
2017
Armoracia rusticana
-
Krainer, F.; Pletzenauer, R.; Rossetti, L.; Herwig, C.; Glieder, A.; Spadiut, O.
Purification and basic biochemical characterization of 19 recombinant plant peroxidase isoenzymes produced in Pichia pastoris
Protein Expr. Purif.
95
104-112
2014
Armoracia rusticana (K7ZW28), Armoracia rusticana (K7ZW57), Armoracia rusticana (K7ZWW6), Armoracia rusticana
EXTERNAL LINKS (specific for EC-Number 1.11.1.7)
Transporter Classification Database (TCDB): 9.A.61.3.1
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Release 2023.1 (January 2023)
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