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Information on EC 1.11.1.7 - peroxidase and Organism(s) Bos taurus and UniProt Accession P80025

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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:
Bos taurus
UNIPROT: P80025
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The taxonomic range for the selected organisms is: Bos taurus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide
2
phenolic donor
+
H2O2
=
2
phenoxyl radical of the donor
+
2
H2O
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
lactoperoxidase
-
eosinophil peroxidase
-
-
-
-
extensin peroxidase
-
-
-
-
guaiacol peroxidase
-
-
-
-
heme peroxidase
horseradish peroxidase (HRP)
-
-
-
-
Japanese radish peroxidase
-
-
-
-
lactoperoxidase
LPS
-
-
MPO
-
-
-
-
myeloperoxidase
-
-
-
-
oxyperoxidase
-
-
-
-
protoheme peroxidase
-
-
-
-
pyrocatechol peroxidase
-
-
-
-
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
benzohydroxamic acid + H2O2
?
show the reaction diagram
the estimated rate constant is approximately one-tenth of that of o-dianisidine
-
-
?
mitoxanthrone + H2O2
?
show the reaction diagram
-
-
-
?
o-anisidine + H2O2
?
show the reaction diagram
the peroxidase specific activities determined under comparable conditions (pH 8 and 5°C) reveal that of o-anisidine to be one-tenth of that of o-dianisidine
-
-
?
o-dianisidine + H2O2
?
show the reaction diagram
best electron donor
-
-
?
reduced 2,2'-azino-bis-(3-ethylbenzthiazole-6-sulfonic acid) + H2O2
oxidized 2,2'-azino-bis-(3-ethylbenzthiazole-6-sulfonic acid) + H2O
show the reaction diagram
thiocyanate + H2O2
hypothiocyanate + H2O
show the reaction diagram
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline)-sulfonic acid + H2O2
?
show the reaction diagram
-
-
-
-
?
2,2-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)diammonium salt + H2O2
?
show the reaction diagram
-
-
-
-
?
2,2-azino-bis-(3-ethylbenz-thiazoline-6-sulfonic acid) + H2O2
? + H2O
show the reaction diagram
-
-
-
-
?
acrylonitrile + H2O2
cyanide + H2O
show the reaction diagram
-
-
-
-
?
Br- + H2O2
?
show the reaction diagram
-
-
-
-
?
catechol + H2O2
?
show the reaction diagram
-
-
-
-
?
Cl- + H2O2
HClO + H2O
show the reaction diagram
-
-
-
-
?
electron donor + H2O2
oxidized electron donor + H2O
show the reaction diagram
estradiol + H2O2
?
show the reaction diagram
-
-
-
-
?
estriol + H2O
?
show the reaction diagram
-
-
-
-
?
estrone + H2O2
?
show the reaction diagram
-
-
-
-
?
ethynylestradiol + H2O2
?
show the reaction diagram
-
-
-
-
?
guaiacol + H2O2
tetraguaiacol + H2O
show the reaction diagram
-
-
-
-
?
I- + H2O2
?
show the reaction diagram
-
-
-
-
?
reduced 2,2'-azino-bis-(3-ethylbenzthiazole-6-sulfonic acid) + H2O2
oxidized 2,2'-azino-bis-(3-ethylbenzthiazole-6-sulfonic acid) + H2O
show the reaction diagram
-
-
-
-
?
SCN- + H2O2
OSCN- + H2O
show the reaction diagram
-
preferred substrate
-
-
?
additional information
?
-
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
electron donor + H2O2
oxidized electron donor + H2O
show the reaction diagram
-
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
enzyme contains Ca2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
hypothiocyanate
-
4-aminobenzenesulfanilamide
-
competitive inhibition
5-methyl-2-thiouracil
-
-
5-n-propyl-2-thiouracil
-
-
amitrole
-
-
benzohydroxyamic acid
-
-
captopril
-
-
genistein
-
-
I3-
-
-
indomethacin
-
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
melamine
-
-
Melatonin
-
-
menadione sodium bisulfate
-
-
Methimazole
-
-
propofol
quercetin
-
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
resorcinol
salicylhydroxyamic acid
-
-
Sodium azide
-
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
trolox C
-
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
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-penicillamine
-
D-penicillamine achieves 128.3% of the rate of cyanide production of the control in the LPO/H2O2/acetonitrile system
glutathione
-
glutathione achieves 138.8% of the rate of cyanide production of the control in the LPO/H2O2/acetonitrile system
L-cysteine
-
L-cysteine is associated with the highest boost in the rate of cyanide formation in the LPO/H2O2/acetonitrile system, achieving 156.7% of the rate of cyanide production of the control
N-acetylcysteine
-
N-acetylcysteine achieves 123.4% of the rate of cyanide production of the control in the LPO/H2O2/acetonitrile system
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000358
2,2'-azino-bis(3-ethylbenzthiazoline)-sulfonic acid
-
at 25°C, pH 6.0
0.107
estradiol
-
-
0.207
estriol
-
-
0.167
estrone
-
-
0.092
ethynylestradiol
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0357
4-aminobenzenesulfanilamide
-
at pH 6.0 and 22°C
0.00372
propofol
-
at 25°C, pH 6.0
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.848
4-aminobenzenesulfanilamide
Bos taurus
-
at pH 6.0 and 22°C
0.00576
5-methyl-2-thiouracil
Bos taurus
-
-
0.00885
5-n-propyl-2-thiouracil
Bos taurus
-
-
0.00951
captopril
Bos taurus
-
-
0.00274
Methimazole
Bos taurus
-
-
0.01597
propofol
Bos taurus
-
at 25°C, pH 6.0
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.1
-
crude enzyme, at pH 6.0 and 22°C
2.3
-
crude enzyme, using 2,2'-azino-bis(3-ethylbenzthiazoline)-sulfonic acid as substrate, at 25°C, pH 6.0
20.7
-
-
34
-
after 14.7fold purification, using 2,2'-azino-bis(3-ethylbenzthiazoline)-sulfonic acid as substrate, at 25°C, pH 6.0
40.9
-
after 409fold purification, at pH 6.0 and 22°C
additional information
-
the maximal rate of cyanide generation observed at pH 5.0 and 37°C is 139.7 pmol/ml/min on average
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
the highest rate of cyanide formation is recorded at pH 5.0
6
-
alginate film-immobilized enzyme
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
the highest rate of cyanide formation is recorded at a temperature of 37°C
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15 - 60
-
LPO enzyme activity is retained between 15°C and 60°C
16 - 30
-
in the 16-30°C range, the temperature change has almost no effect on LPS activity of alginate films
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
rennet whey
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PERL_BOVIN
712
0
80642
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
78000
-
native enzyme, SDS-PAGE
85000
90000
-
recombinant enzyme, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
lactoperoxidase complexes with acetylsalicylic acid, salicylhydroxamic acid, and benzylhydroxamic acid, hanging drop vapour diffusion method, using 0.2 M ammonium iodide and 20% (w/v) PEG-3350
lactoperoxidase containing thiocyanate and hypothiocyanate ions, hanging drop vapour diffusion method, using 0.2 M ammonium nitrate and 20% (w/v) PEG-3350
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8
the specific activity of the enzyme is 600times higher at pH 5.0 than at pH 8.0
696298
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the LPO activity is about 1.5 times higher on gold surfaces carrying a small amount of preadsorbed human mucin (MUC5B) in comparison to LPO directly adsorbed on bare gold
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18°C, and lyophilized by using dextran as supporting material, 2 months, 30% loss of activity
-
-18°C, and lyophilized by using dextran as supporting material, 5 months, 40% loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Amberlite CG-50 resin column chromatography, CM-Sephadex C-50 column chromatography, and Sephadex G-100 gel filtration
-
reverse micellar extraction with sodium di(2-ethylhexyl)sulfosuccinate 0.1-0.3 M dissolved in iso-octane
-
Sepharose 4B-L-tyrosine affinity column chromatography
-
Toyopearl-SP column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in recombinant vaccinia virus and RK-13 cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
food industry
-
preservation of raw milk, yoghurt, and cheese
medicine
-
the enzyme shows high antibacterial activity in 100 mM thiocyanate, 100 mM H2O2 medium for some pathogenic bacteria, such as Aeromonas hydrophila ATCC 79666, Micrococcus luteus LA 2971, Mycobacterium smegmatis RUT, Bacillus subtilis IMG22, Pseudomonas pyocyanea, Bacillus subtilis var. niger ATCC 10, Pseudomonas aeruginosa ATCC 27853, Enterococcus faecalis ATCC 15753, Bacillus brevis FMC3, Klebsiella pneumoniae FMC5, Corynebacterium xerosis UC9165, Bacillus cereus EÜ, Bacillus megaterium NRS, Yersinia enterocolitica, Listeria monocytogenes scoot A, Bacillus megaterium EÜ, Bacillus megaterium DSM32, Klebsiella oxytoca, Staphylococcus aerogenes, Streptococcus faecalis, Mycobacterium smegmatis CCM 2067. The lactoperoxidase(100 mM)/thiocyanate(100 mM)/H2O2 system is purposed as an effective agent against many of the diseases causing organisms in human and animals
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dumentet, C.; Rousset, B.
Identification, purification, and characterization of a non-heme lactoperoxidase in bovine milk
J. Biol. Chem.
258
14166-14172
1983
Bos taurus
Manually annotated by BRENDA team
Paul, K.G.
Peroxidases
The Enzymes, 2nd Ed (Boyer, P. D. , Lardy, H. , Myrbck, K. , eds. )
8
227-274
1963
Armoracia sp., Bos taurus
-
Manually annotated by BRENDA team
Jantschko, W.; Furtmuller, P.G.; Zederbauer, M.; Neugschwandtner, K.; Jakopitsch, C.; Obinger, C.
Reaction of ferrous lactoperoxidase with hydrogen peroxide and dioxygen: an anaerobic stopped-flow study
Arch. Biochem. Biophys.
434
51-59
2005
Bos taurus
Manually annotated by BRENDA team
Uguz, M.T.; Ozdemir, H.
Purification of bovine milk lactoperoxidase and investigation of antibacterial properties at different thiocyanate mediated
Prikl. Biokhim. Mikrobiol.
41
397-401
2005
Bos taurus
Manually annotated by BRENDA team
Lovstad, R.A.
A kinetic study on the lactoperoxidase catalyzed oxidation of estrogens
Biometals
19
587-592
2006
Bos taurus
Manually annotated by BRENDA team
Mecitoglu, C.; Yemenicioglu, A.
Partial purification and preparation of bovine lactoperoxidase and characterization of kinetic properties of its immobilized form incorporated into cross-linked alginate films
Food Chem.
104
726-733
2007
Bos taurus
Manually annotated by BRENDA team
Fielding, A.J.; Singh, R.; Boscolo, B.; Loewen, P.C.; Ghibaudi, E.M.; Ivancich, A.
Intramolecular electron transfer versus substrate oxidation in lactoperoxidase: investigation of radical intermediates by stopped-flow absorption spectrophotometry and (9-285 GHz) electron paramagnetic resonance spectroscopy
Biochemistry
47
9781-9792
2008
Bos taurus (P80025)
Manually annotated by BRENDA team
Singh, A.K.; Singh, N.; Sharma, S.; Shin, K.; Takase, M.; Kaur, P.; Srinivasan, A.; Singh, T.P.
Inhibition of lactoperoxidase by its own catalytic product: crystal structure of the hypothiocyanate-inhibited bovine lactoperoxidase at 2.3-A resolution
Biophys. J.
96
646-654
2009
Bos taurus (P80025), Bos taurus
Manually annotated by BRENDA team
Tanaka, T.; Xuan, X.; Kojima, A.; Igarashi, I.; Fujisaki, K.; Shimazaki, K.
Expression and characterization of bovine lactoperoxidase by recombinant vaccinia virus
Cytotechnology
58
127-133
2008
Bos taurus
Manually annotated by BRENDA team
Bhuyan, B.J.; Mugesh, G.
Heme peroxidase-catalyzed iodination of human angiotensins and the effect of iodination on angiotensin converting enzyme activity
Inorg. Chem.
47
6569-6571
2008
Bos taurus
Manually annotated by BRENDA team
Singh, A.K.; Singh, N.; Sinha, M.; Bhushan, A.; Kaur, P.; Srinivasan, A.; Sharma, S.; Singh, T.P.
Binding modes of aromatic ligands to mammalian heme peroxidases with associated functional implications: crystal structures of lactoperoxidase complexes with acetylsalicylic acid, salicylhydroxamic acid, and benzylhydroxamic acid
J. Biol. Chem.
284
20311-20318
2009
Bos taurus (P80025), Bos taurus
Manually annotated by BRENDA team
Haberska, K.; Svensson, O.; Shleev, S.; Lindh, L.; Arnebrant, T.; Ruzgas, T.
Activity of lactoperoxidase when adsorbed on protein layers
Talanta
76
1159-1164
2008
Bos taurus
Manually annotated by BRENDA team
Nasralla, S.N.; Ghoneim, A.I.; Khalifa, A.E.; Gad, M.Z.; Abdel-Naim, A.B.
Lactoperoxidase catalyzes in vitro activation of acrylonitrile to cyanide
Toxicol. Lett.
191
347-352
2009
Bos taurus
Manually annotated by BRENDA team
Nandini, K.E.; Rastogi, N.K.
Single step purification of lactoperoxidase from whey involving reverse micelles-assisted extraction and its comparison with reverse micellar extraction
Biotechnol. Prog.
26
763-771
2010
Bos taurus
Manually annotated by BRENDA team
Sisecioglu, M.; Cankaya, M.; Guelcin, I.; Ozdemir, H.
The inhibitory effect of propofol on bovine lactoperoxidase
Protein Pept. Lett.
16
46-49
2009
Bos taurus
Manually annotated by BRENDA team
Atasever, A.; Ozdemir, H.; Gulcin, I.; Irfan Kufrevioglu, O.
One-step purification of lactoperoxidase from bovine milk by affinity chromatography
Food Chem.
136
864-870
2013
Bos taurus
Manually annotated by BRENDA team
Sharma, S.; Singh, A.K.; Kaushik, S.; Sinha, M.; Singh, R.P.; Sharma, P.; Sirohi, H.; Kaur, P.; Singh, T.P.
Lactoperoxidase: structural insights into the function,ligand binding and inhibition
Int. J. Biochem. Mol. Biol.
4
108-128
2013
Bos taurus
Manually annotated by BRENDA team