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Information on EC 1.11.1.7 - peroxidase and Organism(s) Pleurotus eryngii and UniProt Accession O94753
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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
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retrograde
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dorsal
- nerve
- nuclei
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medial
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afferent
- fiber
-
tracer
- spinal
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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
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dorsolateral
-
somata
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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: Pleurotus eryngii
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 (HRP)
-
-
-
-
Japanese radish peroxidase
-
-
-
-
lactoperoxidase
-
-
-
-
MPO
-
-
-
-
myeloperoxidase
-
-
-
-
oxyperoxidase
-
-
-
-
protoheme peroxidase
-
-
-
-
pyrocatechol peroxidase
-
-
-
-
scopoletin peroxidase
-
-
-
-
thiocyanate peroxidase
-
-
-
-
verdoperoxidase
-
-
-
-
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
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). PDB
SCOP
CATH
UNIPROT
ORGANISM
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method. Crystallographic analysis of peroxide-treated wild-type enzyme and W164S variant
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H232F
P76F
kcat/KM for veratryl alcohol is increased slightly. kcat/KM for Mn2+ as substrate is 2.3fold lower than the wild-type value
W164S
mutant enzyme is completely unable to oxidize both veratryl, alcohol and Reactive Black 5. kcat/KM for Mn2+ as substrate is 1.2fold higher than the wild-type value
W164S/P76H
mutant enzyme is completely unable to oxidize both veratryl, alcohol and Reactive Black 5. kcat/KM for Mn2+ as substrate is 1.1fold lower than the wild-type value
H232F
kcat/Km for Reactive Black 5 is decreased, kcat/KM for veratryl alcohol is increased slightly. kcat/KM for Mn2+ as substrate is 1.5fold lower than the wild-type value
H232F
mutant enzyme is completely unable to oxidize both veratryl, alcohol and Reactive Black 5. kcat/KM for Mn2+ as substrate is 1.6fold higher than the wild-type value
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Perez-Boada, M.; Ruiz-Duenas, F.J.; Pogni, R.; Basosi, R.; Choinowski, T.; Martinez, M.J.; Piontek, K.; Martinez, A.T.
Versatile peroxidase oxidation of high redox potential aromatic compounds: site-directed mutagenesis, spectroscopic and crystallographic investigation of three long-range electron transfer pathways
J. Mol. Biol.
354
385-402
2005
Pleurotus eryngii (O94753)
EXTERNAL LINKS (specific for EC-Number 1.11.1.7)
Transporter Classification Database (TCDB): 9.A.61.3.1
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