1.11.1.7: peroxidase
This is an abbreviated version!
For detailed information about peroxidase, go to the full flat file.
Word Map on EC 1.11.1.7
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1.11.1.7
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retrograde
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dorsal
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nerve
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nuclei
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medial
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afferent
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fiber
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tracer
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spinal
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ventral
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ipsilateral
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cord
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rostrally
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innervation
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contralateral
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dendrite
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caudal
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anterograde
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ganglion
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posterior
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electrode
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agglutinin
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reticular
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tracing
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erythropoietin
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peroxidases
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lamina
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motoneuron
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thalamic
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trigeminal
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geniculate
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topographic
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arbor
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colliculus
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dorsolateral
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somata
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ventrolateral
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boutons
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collateral
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ventromedial
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commissure
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vestibular
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pontine
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dorsomedial
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raphe
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send
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mesencephalic
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iontophoretic
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immunosensors
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tegmental
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analysis
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medicine
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nutrition
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degradation
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synthesis
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food industry
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agriculture
- 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
Reaction
2 phenolic donor
+
Synonyms
acidic peroxidase, acidic POD, ALSP, AnaPX, anionic isoperoxidase, anionic peroxidase A1, AOPTP, basic peroxidase, basic POD, BCcP, black radish peroxidase A, black radish peroxidase B, BRP-A, BRP-B, cationic peroxidase, cationic peroxidase Cs, class III plant peroxidase, CmMnP, constitutive peroxidase, CP, cPOD-I, CYP119, dehaloperoxidase A, dehaloperoxidase B, DHP A, donor: H2O2 oxidoreductase, donor: hydrogen peroxide oxidoreductase, donor:hydrogen peroxide oxidoreductase, DtpA, ECPOX, ECPOX 1, ECPOX 2, ECPOX 3, ELP, eosinophil peroxidase, EPO, extensin peroxidase, extracellular peroxidase, FP1, Fp2, FP3, GCP1, GCP2, guaiacol peroxidase, H2O2 oxidoreductase, Hb peroxidase, Hb1, heme peroxidase, hemoglobin 1, hemoglobin peroxidase, hexacoordinate (class 1) non-symbiotic hemoglobin, horseradisch peroxidase, horseradish peroxidase, horseradish peroxidase (HRP), horseradish peroxidase C, HP, HRP, HRP A2, HRP C1A, HRP-C, HRPC, HRPO, HRP_A2A, HRP_C1A, HRP_E5, HTHP, hydrogen donor oxidoreductase, Japanese radish peroxidase, lactoperoxidase, LPO, LPRX, LPS, MAP-2744c, MGP, MnP124076, MnP13, More, MPO, myeloperoxidase, neutral peroxidase, neutral POD, NGO_0994, nsHb-1, oxyperoxidase, p20, PA1, PerII, peroxidase, peroxidase isoenzyme E5, POC1, POD, POD1, POII, POX, POX I, POX II, POX2, protoheme peroxidase, Prx02, Prx03, Prx06, Prx07, Prx09, Prx1, Prx11, Prx114, Prx12, Prx13, Prx15, Prx17, Prx21, Prx22, Prx27, Prx28, Prx30, Prx31, Prx32, Prx33, Prx34, Prx36, Prx37, Prx39, Prx42, Prx43, Prx45, Prx49, Prx50, Prx51, Prx52, Prx53, Prx55, Prx56, Prx57, Prx58, Prx59, Prx60, Prx62, Prx64, Prx66, Prx67, Prx68, Prx69, Prx70, Prx71, Prx72, Prx73, pyrocatechol peroxidase, QPO, quinol peroxidase, rhEPO, rHRP1, rHRP2, royal palm tree peroxidase, rPOD-II, RPTP, rubrerythrin, SacD, Saci_2081, SBP, scavengase, scopoletin peroxidase, SfmD, short PMnP, SPC4, Ssp, stigma-specific peroxidase, thiocyanate peroxidase, thiol peroxidase, TOP, TP I, Tpx, tyrosine-coordinated heme protein, vacuolar class III peroxidase, vascular peroxidase 1, verdoperoxidase, versatile peroxidase, versatile peroxidase VPL2, VP, VPO1, VPO2, WPTP
ECTree
1.11.1.7 peroxidaseAdvanced search results
results (
results (Inhibitors
Inhibitors on EC 1.11.1.7 - peroxidase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
1-butyl-3-methylimidazolium tetrafluoroborate
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weak, non-competitive inhibitor
2,4,6-tribromophenol
substrate inhibition at high concentration due to the internal binding at the distal pocket of DHP; substrate inhibition at high concentration due to the internal binding at the distal pocket of DHP
2,4,6-Trichlorophenol
substrate inhibition at high concentration due to the internal binding at the distal pocket of DHP; substrate inhibition at high concentration due to the internal binding at the distal pocket of DHP
2,4-dinitroresorcinol
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competitive inhibition of 3,3',5,5'-tetramethylbenzidine oxidation
2-amino-4-nitrophenol
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competitive inhibition of 3,3',5,5'-tetramethylbenzidine oxidation
butyl-3-methylimidazolium tetrafluoroborate
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significantly weakens the binding affinity of guaiacol to HRP
gallic acid
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competetive inhibition of 3,3',5,5'-tetramethylbenzidine oxidation
Haptoglobin
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mixed type of inhibition, haptoglobin binds with hemoglobin and weakens hemoglobin peroxidase activity
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histidine
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0.18 mM, 43% inhibition of the activity with quercetin, 13% inhibition of the activity with o-dianisidine, isoenzyme POX II; 0.18 mM, 71% inhibition of the activity with quercetin, 95% inhibition of the activity with o-dianisidine, isoenzyme POX I
imidazole
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0.18 mM, 24% inhibition of the activity with quercetin, 81% inhibition of the activity with o-dianisidine, isoenzyme POX II; 0.18 mM, 72% inhibition of the activity with quercetin, 97% inhibition of the activity with o-dianisidine, isoenzyme POX I
indomethacin
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the presence of indomethacin in the LPO/H2O2/acetonitrile system leads to a modest, yet significant decline in the rate of cyanide formation of only 84.1% of the control
KI
30% inhibition at 1 mM; 30% inhibition at 1 mM; 36% inhibition at 1 mM; 36% inhibition at 1 mM
La3+
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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+
linoleic acid
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3.6 mM, 76% inhibition of the activity with quercetin, 48% inhibition of the activity with o-dianisidine, isoenzyme POX II; 3.6 mM, no inhibition of the activity with quercetin, 32% inhibition of the activity with o-dianisidine, isoenzyme POX I
linolenic acid
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3.6 mM, 16% inhibition of the activity with quercetin, 21% inhibition of the activity with o-dianisidine, isoenzyme POX I; 3.6 mM, 35% inhibition of the activity with quercetin, 37% inhibition of the activity with o-dianisidine, isoenzyme POX II
n-Hexanol
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the enzymatic activity of horseradish peroxidase decreases upon addition of n-hexanol
NH4+
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0.18 mM, 6% inhibition of the activity with quercetin; 0.18 mM, no inhibition of the activity with quercetin, 27% inhibition of the activity with o-dianisidine, isoenzyme POX I
oleic acid
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3.6 mM, isoenzyme POX I, 62% inhibition of the activity with quercetin, 19% inhibition of the activity with o-dianisidine, isoenzyme POX I; 3.6 mM, isoenzyme POX II, 72% inhibition of the activity with quercetin, 41% inhibition of the activity with o-dianisidine, isoenzyme POX II
PCMB
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4 mM, 78% without substrate, 75% inhibition in presence of substrate
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
quercetin
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incubation of the LPO/H2O2/acetonitrile system with 0.1 mM quercetin is associated with the highest rate of inhibition amounting to 40.2% of the control
Sodium metabisulfite
complete inhibition at 1 mM; complete inhibition at 1 mM; complete inhibition at 1 mM
Tb3+
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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
trolox C
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incubation of the LPO/H2O2/acetonitrile system with 0.1 mM trolox C is associated with the highest rate of inhibition amounting to 47.8% of the control
Tween 80
30% inhibition at 1 mM; 38% inhibition at 1 mM; 45% inhibition at 1 mM; 45% inhibition at 1 mM
acetonitrile
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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
ascorbate
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0.1 mM, complete inhibition of membrane-bound isoform, 0.2 mM, complete inhibition of soluble isoform
ascorbic acid
complete inhibition at 1 mM; complete inhibition at 1 mM; complete inhibition at 1 mM
beta-mercaptoethanol
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4 mM, 80% without substrate, 78% inhibition in presence of substrate
beta-mercaptoethanol
94% inhibition at 1 mM; 94% inhibition at 1 mM; 96% inhibition at 1 mM; 96% inhibition at 1 mM
Co2+
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10 mM, 17% loss of activity, isoenzyme FP2; 10 mM, 42% loss of activity, isoenzyme FP1; 10 mM, 53% loss of activity, isoenzyme FP3
Co2+
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5 mM, 79% inhibition of cationic peroxidase GCP1. 5 mM, 20% inhibition of anionic peroxidase GCP2
Cu2+
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10 mM, 67% loss of activity, isoenzyme FP3; 10 mM, complete loss of activity, isoenzyme FP1
Cu2+
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5 mM, 85% inhibition of cationic peroxidase GCP1. 5 mM, 26% inhibition of anionic peroxidase GCP2
cysteine
73% inhibition at 1 mM; 73% inhibition at 1 mM; 78% inhibition at 1 mM; 78% inhibition at 1 mM
D-fructose
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D-fructose at different concentrations, POD activities are measured at 25°C and pH 7.0 to determine inhibitor effects of sugars on enzymatic activities. POD activities from both cultivars show a decreasing pattern as sugar concentration in the assay medium increased, except in POD extract from Charentais, which maintained its activity in the presence of high D-glucose concentration (up to 5 M)
D-glucose
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D-glucose at different concentrations, POD activities are measured at 25°C and pH 7.0 to determine inhibitor effects of sugars on enzymatic activities. POD activities from both cultivars show a decreasing pattern as sugar concentration in the assay medium increased, except in POD extract from Charentais, which maintained its activity in the presence of high D-glucose concentration (up to 5 M)
diethyl dicarbonate
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4 mM, 50% without substrate, 21% inhibition in presence of substrate
dithiothreitol
98% inhibition at 1 mM; 98% inhibition at 1 mM; complete inhibition at 1 mM; complete inhibition at 1 mM
EDTA
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10 mM, 14% loss of activity, isoenzyme FP2; 10 mM, 36% loss of activity, isoenzyme FP1; 10 mM, 88% loss of activity, isoenzyme FP3
EDTA
24% inhibition at 1 mM; 28% inhibition at 1 mM; 28% inhibition at 1 mM; 28% inhibition at 1 mM
guanidine hydrochloride
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less than 10% activity at 1M guanidine hydrochloride
H2O2
inactivation by H2O2 is expressed by pseudofirst order kinetics and is an irreversible process
H2O2
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3 mM, suicide inactivation. Addition of SDS to the reaction mixture intensifies the inactivation process; 3 mM, suicide inactivation through a steady-state mechanism
H2O2
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peroxidase isozyme A1 activity is decreased by 30% already at 20 mM H2O2
H2O2
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enzyme retains more than 80% of its initial activity after 24 h incubation in 5000fold molar excess of H2O2
Hg2+
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10 mM, 54% loss of activity, isoenzyme FP2; 10 mM, 82% loss of activity, isoenzyme FP3; 10 mM, 91% loss of activity, isoenzyme FP1
Hg2+
41% relative activity at 1 mM; 50% inhibition at 1 mM; 50% relative activity at 1 mM; 59% inhibition at 1 mM
Hg2+
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5 mM, 93% inhibition of cationic peroxidase GCP1. 5 mM, 33% inhibition of anionic peroxidase GCP2
K+
26% inhibition at 1 mM; 27% inhibition at 1 mM; 74% relative activity at 1 mM; 77% relative activity at 1 mM
KCN
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very low sensitivity, causes only 9% and 14% inhibition of the activity at 1 and 10 mM, respectively
KCN
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isozyme ECPOX 1 shows 1% residual activity, isozyme ECPOX 2 shows complete inhibition, and isozyme ECPOX 3 shows 3% residual activity at 0.1 mM
L-cysteine
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0.15 mM, complete inhibition of membrane-bound isoform, 2 mM, complete inhibition of soluble isoform
Metabisulfite
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3 mM, complete inhibition of membrane-bound isoform, 3.5 mM, complete inhibition of soluble isoform
Mn2+
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10 mM, 19% loss of activity, isoenzyme FP1; 10 mM, 2% loss of activity, isoenzyme FP2; 10 mM, 75% loss of activity, isoenzyme FP3
Mn2+
30% inhibition at 1 mM; 30% inhibition at 1 mM; 70% relative activity at 1 mM; 73% relative activity at 1 mM
Na+
44% inhibition at 1 mM; 49% inhibition at 1 mM; 49% inhibition at 1 mM
NaN3
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10 mM, 98% loss of activity, isoenzyme FP2; 10 mM, 99% loss of activity, isoenzyme FP1; 10 mM, complete loss of activity, isoenzyme FP3
NaN3
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isozyme ECPOX 1 shows 4% residual activity, isozyme ECPOX 2 shows complete inhibition, and isozyme ECPOX 3 shows 11% residual activity at 1 mM
Ni2+
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10 mM, 14% loss of activity, isoenzyme FP1; 10 mM, 27% loss of activity, isoenzyme FP2; 10 mM, 55% loss of activity, isoenzyme FP3
resorcinol
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competitive inhibition of 3,3',5,5'-tetramethylbenzidine oxidation
resorcinol
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incubation of the LPO/H2O2/acetonitrile system with resorcinol is associated with amoderate decline in the rate of cyanide production which is 64.8% of the control
Sodium azide
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incubation of the LPO/H2O2/acetonitrile system with sodium azide is associated with amoderate decline in the rate of cyanide production which is 61.6% of the control
Sodium azide
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0.187 mM, more than 75% inhibition, 0.5 mM, complete inhibition, heme-containing enzyme
Zn2+
38% relative activity at 1 mM; 46% relative activity at 1 mM; 54% inhibition at 1 mM; 62% inhibition at 1 mM
additional information
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no substrate inhibition by 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid); no substrate inhibition by 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)
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additional information
no substrate inhibition by 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid); no substrate inhibition by 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)
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additional information
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the enzyme is not sensitive to the prototypical catalase inhibitor 3-amino-1, 2, 4,-triazole in presence of ascorbic acid (1.0 mM)
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additional information
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HRP-DNA conjugates reveal a reduced peroxidase activity
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additional information
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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
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additional information
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no inhibition of enzyme activity when the concentrations of phenol and H2O2 are at or below 10 mM and 0.1 mM, respectively
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additional information
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enzyme does not exhibit any measurable substrate inhibition
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additional information
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the enzyme keeps its activity in the presence of high D-glucose concentrations (up to 5 M)
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additional information
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the enzyme keeps its activity in the presence of high D-glucose concentrations (up to 5 M)
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additional information
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inhibition is not observed with ethylmaleinimide and urea
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additional information
peroxidase activity is not inhibited by 3-amino-1,2,4-triazole concentrations up to 20 mM
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additional information
presence of Mg2+, Cu2+, Fe3+, Ni2+, citric acid, and urea has no effect on the peroxidase activity
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