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Information on EC 1.11.1.7 - peroxidase and Organism(s) Gossypium hirsutum and UniProt Accession Q8RVW0

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EC Tree
     1 Oxidoreductases
         1.11 Acting on a peroxide as acceptor
             1.11.1 Peroxidases
                1.11.1.7 peroxidase
IUBMB 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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This record set is specific for:
Gossypium hirsutum
UNIPROT: Q8RVW0
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Word Map
The taxonomic range for the selected organisms is: Gossypium hirsutum
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cPOD-I
eosinophil peroxidase
-
-
-
-
extensin peroxidase
-
-
-
-
guaiacol peroxidase
-
-
-
-
heme peroxidase
-
-
-
-
horseradish peroxidase (HRP)
-
-
-
-
Japanese radish peroxidase
-
-
-
-
lactoperoxidase
-
-
-
-
MPO
-
-
-
-
myeloperoxidase
-
-
-
-
oxyperoxidase
-
-
-
-
protoheme peroxidase
-
-
-
-
pyrocatechol peroxidase
-
-
-
-
rPOD-II
-
isozyme
scopoletin peroxidase
-
-
-
-
thiocyanate peroxidase
-
-
-
-
verdoperoxidase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -
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 hide
9003-99-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-methylcatechol + H2O2
?
show the reaction diagram
47% activity compared to guaiacol
-
-
?
benzoic acid + H2O2
?
show the reaction diagram
19% activity compared to guaiacol
-
-
?
catechin + H2O2
?
show the reaction diagram
10% activity compared to guaiacol
-
-
?
catechol + H2O2
?
show the reaction diagram
30% activity compared to guaiacol
-
-
?
chlorogenic acid + H2O2
?
show the reaction diagram
95% activity compared to guaiacol
-
-
?
guaiacol + H2O2
tetraguaiacol + H2O
show the reaction diagram
shows high efficiency of interaction with guaiacol at 25 mM
-
-
?
p-coumaric acid + H2O2
?
show the reaction diagram
15% activity compared to guaiacol
-
-
?
pyrogallol + H2O2
?
show the reaction diagram
84% activity compared to guaiacol
-
-
?
tetramethylbenzidine + H2O2
?
show the reaction diagram
206% activity compared to guaiacol
-
-
?
4-methylcatechol + H2O2
?
show the reaction diagram
benzoic acid + H2O2
?
show the reaction diagram
catechin + H2O2
?
show the reaction diagram
catechol + H2O2
?
show the reaction diagram
chlorogenic acid + H2O2
?
show the reaction diagram
guaiacol + H2O2
tetraguaiacol + H2O
show the reaction diagram
p-coumaric acid + H2O2
?
show the reaction diagram
pyrogallol + H2O2
?
show the reaction diagram
90% activity compared to guaiacol
-
-
?
pyrogallol + H2O2
purpurogallin + H2O
show the reaction diagram
tetramethylbenzidine + H2O2
?
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Al3+
108% increased activity at 1 mM
Ca2+
51% increased activity at 1 mM
Fe3+
205% increased activity at 1 mM
Ni2+
23% increased activity at 1 mM
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ascorbic acid
complete inhibition at 1 mM
beta-mercaptoethanol
94% inhibition at 1 mM
cysteine
78% inhibition at 1 mM
dithiothreitol
98% inhibition at 1 mM
EDTA
28% inhibition at 1 mM
Hg2+
50% inhibition at 1 mM
K+
26% inhibition at 1 mM
KI
30% inhibition at 1 mM
Mn2+
30% inhibition at 1 mM
Na+
49% inhibition at 1 mM
Sodium metabisulfite
complete inhibition at 1 mM
Tween 80
30% inhibition at 1 mM
Zn2+
54% inhibition at 1 mM
ascorbic acid
complete inhibition at 1 mM
beta-mercaptoethanol
cysteine
dithiothreitol
NaCl
44% inhibition at 1 mM
Sodium metabisulfite
complete inhibition at 1 mM
Tween 80
additional information
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cultivar R405-2000
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q8RVW0_GOSHI
327
1
35786
TrEMBL
Secretory Pathway (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 8
the enzyme retains more than 90% of its initial activity within the pH range 6.0-7.0, weakest activity at pH 8.0, enzymatic activity is lowest after incubation for 60 min at pH 4.0 and 8.0
695687
5 - 8
the enzyme retains more than 90% of its initial activity within the pH range 5.0-6.0, weakest activity at pH 8.0, enzymatic activity is lowest after incubation for 60 min at pH 7.0 and 8.0
695687
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 80
relatively stable between 20-30°C, activity decreases by 20% at 40°C, the time required for 50% inactivation of activity at 50°C, 60°C, and 70°C is about 5 min, a decrease in POD activity of 75%, 85%, and 90% occurs after 10 min at 50°C, 60°C, and 70°C, respectively, the enzyme activity at 50°C, 60°C, and 70-80°C is completely exhausted in 40, 25, and 10 min
20 - 70
relatively stable at 20-30°C, a decrease in POD activity of 75%, 85%, and 90% is found after 10 min at 50°C, 60°C, and 70°C, respectively. The enzyme activity at 50°C, 60°C, and 70-80°C is completely exhausted in 40, 25, and 10 min, respectively.
20 - 80
relatively stable between 20-30°C, activity decreases by 25% at 40°C, the time required for 50% inactivation of activity at 50°C, 60°C, and 70°C is about 5 min, a decrease in POD activity of 75%, 85%, and 90% occurs after 10 min at 50°C, 60°C, and 70°C, respectively, the enzyme activity at 50°C, 60°C, and 70-80°C is completely exhausted in 40, 25, and 10 min
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation and Sephadex G-200 gel filtration
ammonium sulfate precipitation and Sephadex G-200 gel filtration
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kouakou, T.H.; Due, E.A.; Kouadio, N.E.; Niamke, S.; Kouadio, Y.J.; Merillon, J.M.
Purification and characterization of cell suspensions peroxidase from cotton (Gossypium hirsutum L.)
Appl. Biochem. Biotechnol.
157
575-592
2008
Gossypium hirsutum, Gossypium hirsutum (Q8RVP6), Gossypium hirsutum (Q8RVW0)
Manually annotated by BRENDA team