We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
eosinophil peroxidase
-
-
-
-
extensin peroxidase
-
-
-
-
guaiacol peroxidase
-
-
-
-
horseradish peroxidase (HRP)
-
-
-
-
Japanese radish peroxidase
-
-
-
-
protoheme peroxidase
-
-
-
-
pyrocatechol peroxidase
-
-
-
-
scopoletin peroxidase
-
-
-
-
thiocyanate peroxidase
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
reduced thioredoxin 1 + cumene hydroperoxide
oxidized thioredoxin 1 + cumene hydroxide
-
-
-
?
reduced thioredoxin 1 + H2O2
oxidized thioredoxin 1 + H2O
-
-
-
?
3-methyltyrosine + H2O2
3-hydroxy-5-methyltyrosine + H2O
-
-
-
-
?
L-tyrosine + H2O2
?
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3-methyltyrosine + H2O2
3-hydroxy-5-methyltyrosine + H2O
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.009
cumene hydroperoxide
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
70.1
cumene hydroperoxide
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
Uniprot
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
metabolism
-
the enzyme is involved in the biosynthesis of saframycin A
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
dimer
2 * 17700, ESI-mass spectrometry, dimer in solution
?
-
x * 39800, SDS-PAGE
?
-
x * 39855, LC-MS analysis and calculated from amino acid sequence
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ammonium sulfate, Phenyl-Sepharodse, Q-Sepharose
Ni-NTA affinity column chromatography
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
overexpression in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
brenda
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
brenda
Transporter Classification Database (TCDB):
9.A.61.3.1