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Information on EC 1.11.1.7 - peroxidase and Organism(s) Escherichia coli and UniProt Accession P0A862

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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:
Escherichia coli
UNIPROT: P0A862
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Word Map
The taxonomic range for the selected organisms is: Escherichia coli
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
thiol peroxidase
-
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 hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
hydroxylation
-
-
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
reduced thioredoxin 1 + cumene hydroperoxide
oxidized thioredoxin 1 + cumene hydroxide
show the reaction diagram
-
-
-
?
reduced thioredoxin 1 + H2O2
oxidized thioredoxin 1 + H2O
show the reaction diagram
-
-
-
?
3-methyltyrosine + H2O2
3-hydroxy-5-methyltyrosine + H2O
show the reaction diagram
-
-
-
-
?
L-tyrosine + H2O2
?
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3-methyltyrosine + H2O2
3-hydroxy-5-methyltyrosine + H2O
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.009
cumene hydroperoxide
25°C, pH 7.0
1.7
H2O2
25°C, pH 7.0
0.023
thioredoxin 1
25°C, pH 7.0
0.64
3-methyltyrosine
-
in 100 mM Tris-HCl, pH 9.0, at 25°C
1
L-tyrosine
-
in 100 mM Tris-HCl, pH 9.0, at 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
70.1
cumene hydroperoxide
25°C, pH 7.0
76
H2O2
25°C, pH 7.0
17.8
3-methyltyrosine
-
in 100 mM Tris-HCl, pH 9.0, at 25°C
12.3
L-tyrosine
-
in 100 mM Tris-HCl, pH 9.0, at 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
27.8
3-methyltyrosine
-
in 100 mM Tris-HCl, pH 9.0, at 25°C
12.2
L-tyrosine
-
in 100 mM Tris-HCl, pH 9.0, at 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
the enzyme is involved in the biosynthesis of saframycin A
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
17700
2 * 17700, ESI-mass spectrometry, dimer in solution
29500
sedimentation equilibrium, oxidized enzyme
32000
sedimentation equilibrium, reduced enzyme
39800
-
x * 39800, SDS-PAGE
39855
-
x * 39855, LC-MS analysis and calculated from amino acid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 17700, ESI-mass spectrometry, dimer in solution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C61S
no activity
C82S
72% of wild-type activity
C82S/C95S
10% of wild-type activity
C95S
20% of wild-type activity
C317A
-
the heme content of the mutant is very low and the mutant loses the ability to hydroxylate 3-methyltyrosine
H191A
-
the mutant loses the ability to hydroxylate 3-methyltyrosine
H274A
-
the mutant loses the ability to hydroxylate 3-methyltyrosine
H313A
-
the heme content of the mutant is very low and the mutant loses the ability to hydroxylate 3-methyltyrosine
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, Phenyl-Sepharodse, Q-Sepharose
Ni-NTA affinity column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Baker, L.M.S.; Poole, L.B.
Catalytic mechanism of thiol peroxidase from Escherichia coli: Sulfenic acid formation and overoxidation of essential Cys61
J. Biol. Chem.
278
9203-9211
2003
Escherichia coli (P0A862), Escherichia coli
Manually annotated by BRENDA team
Tang, M.C.; Fu, C.Y.; Tang, G.L.
Characterization of SfmD as a heme peroxidase that catalyzes the regioselective hydroxylation of 3-methyltyrosine to 3-hydroxy-5-methyltyrosine in saframycin A biosynthesis
J. Biol. Chem.
287
5112-5121
2012
Escherichia coli
Manually annotated by BRENDA team