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Search results 201 to 240 out of 240 for Lpo

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0.037s

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Type Details Score
Publication
16355390 | J:107087
First Author: Samarth RM
Year: 2006
Journal: Environ Mol Mutagen
Title: Modulatory effects of Mentha piperita on lung tumor incidence, genotoxicity, and oxidative stress in benzo[a]pyrene-treated Swiss albino mice.
Volume: 47
Issue: 3
Pages: 192-8
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Publication
27414401 | J:253091
First Author: Sati J
Year: 2016
Journal: PLoS One
Title: Pro-Oxidant Role of Silibinin in DMBA/TPA Induced Skin Cancer: 1H NMR Metabolomic and Biochemical Study.
Volume: 11
Issue: 7
Pages: e0158955
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Publication
35649726 | J:346228
First Author: Miracca G
Year: 2022
Journal: J Neurosci
Title: NMDA Receptors in the Lateral Preoptic Hypothalamus Are Essential for Sustaining NREM and REM Sleep.
Volume: 42
Issue: 27
Pages: 5389-5409
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Protein
F8WGZ9
Organism: Mus musculus/domesticus
Length: 99  
Fragment?: true
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Protein Domain
IPR019791 | Haem_peroxidase_animal
Type: Family
Description: Peroxidases are haem-containing enzymes that use hydrogen peroxide as the electron acceptor to catalyse a number of oxidative reactions.Peroxidases are found in bacteria, fungi, plants and animals. On the basis of sequence similarity, a number of animal haem peroxidases can be categorised as members of a superfamily: myeloperoxidase (MPO); eosinophil peroxidase (EPO); lactoperoxidase (LPO); thyroid peroxidase (TPO); prostaglandin H synthase (PGHS); and peroxidasin [, , ]. MPO plays a major role in the oxygen-dependent microbicidal system of neutrophils. EPO from eosinophilic granulocytes participates in immunological reactions, and potentiates tumor necrosis factor (TNF) production and hydrogen peroxide release by human monocyte-derived macrophages [, ]. In the main, MPO (and possibly EPO) utilises Cl-ions and H2O2to form hypochlorous acid (HOCl), which can effectively kill bacteria or parasites. In secreted fluids, LPO catalyses the oxidation of thiocyanate ions (SCN-) by H2O2, producing the weak oxidising agent hypothiocyanite (OSCN-), which has bacteriostatic activity []. TPO uses I-ions and H2O2to generate iodine, and plays a central role in the biosynthesis of thyroid hormones T(3) and T(4). To date, the 3D structures of MPO and PGHS have been reported. MPO is a homodimer: each monomer consists of a light (A or B) and a heavy (C or D) chain resulting from post-translational excision of 6 residues from the common precursor. Monomers are linked by a single inter-chain disulphide. Each monomer includes a bound calcium ion []. PGHS exists as a symmetric dimer, each monomer of which consists of 3 domains: an N-terminal epidermal growth factor (EGF) like module; a membrane-binding domain; and a large C-terminal catalytic domain containing the cyclooxygenase and the peroxidase active sites. The catalytic domain shows striking structural similarity to MPO. The cyclooxygenase active site, which catalyses the formation of prostaglandin G2 (PGG2) from arachidonic acid, resides at the apex of a long hydrophobic channel, extending from the membrane-binding domain to the centre of the molecule. The peroxidase active site, which catalyses the reduction of PGG2 to PGH2, is located on the other side of the molecule, at the haem binding site []. Both MPO and the catalytic domain of PGHS are mainly α-helical, 19 helices being identified as topologically and spatially equivalent; PGHS contains 5 additional N-terminal helices that have no equivalent in MPO. In both proteins, three Asn residues in each monomer are glycosylated.
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Protein Domain
IPR037120 | Haem_peroxidase_sf_animal
Type: Homologous_superfamily
Description: Peroxidases are haem-containing enzymes that use hydrogen peroxide as the electron acceptor to catalyse a number of oxidative reactions.Peroxidases are found in bacteria, fungi, plants and animals. On the basis of sequence similarity, a number of animal haem peroxidases can be categorised as members of a superfamily: myeloperoxidase (MPO); eosinophil peroxidase (EPO); lactoperoxidase (LPO); thyroid peroxidase (TPO); prostaglandin H synthase (PGHS); and peroxidasin [, , ]. MPO plays a major role in the oxygen-dependent microbicidal system of neutrophils. EPO from eosinophilic granulocytes participates in immunological reactions, and potentiates tumor necrosis factor (TNF) production and hydrogen peroxide release by human monocyte-derived macrophages [, ]. In the main, MPO (and possibly EPO) utilises Cl-ions and H2O2to form hypochlorous acid (HOCl), which can effectively kill bacteria or parasites. In secreted fluids, LPO catalyses the oxidation of thiocyanate ions (SCN-) by H2O2, producing the weak oxidising agent hypothiocyanite (OSCN-), which has bacteriostatic activity []. TPO uses I-ions and H2O2to generate iodine, and plays a central role in the biosynthesis of thyroid hormones T(3) and T(4). To date, the 3D structures of MPO and PGHS have been reported. MPO is a homodimer: each monomer consists of a light (A or B) and a heavy (C or D) chain resulting from post-translational excision of 6 residues from the common precursor. Monomers are linked by a single inter-chain disulphide. Each monomer includes a bound calcium ion []. PGHS exists as a symmetric dimer, each monomer of which consists of 3 domains: an N-terminal epidermal growth factor (EGF) like module; a membrane-binding domain; and a large C-terminal catalytic domain containing the cyclooxygenase and the peroxidase active sites. The catalytic domain shows striking structural similarity to MPO. The cyclooxygenase active site, which catalyses the formation of prostaglandin G2 (PGG2) from arachidonic acid, resides at the apex of a long hydrophobic channel, extending from the membrane-binding domain to the centre of the molecule. The peroxidase active site, which catalyses the reduction of PGG2 to PGH2, is located on the other side of the molecule, at the haem binding site []. Both MPO and the catalytic domain of PGHS are mainly α-helical, 19 helices being identified as topologically and spatially equivalent; PGHS contains 5 additional N-terminal helices that have no equivalent in MPO. In both proteins, three Asn residues in each monomer are glycosylated.
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Protein
P11247
Organism: Mus musculus/domesticus
Length: 718  
Fragment?: false
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Protein
Q6RFG4
Organism: Mus musculus/domesticus
Length: 718  
Fragment?: false
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Protein
A0A0A0MQL9
Organism: Mus musculus/domesticus
Length: 166  
Fragment?: true
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Protein
Q7TMS4
Organism: Mus musculus/domesticus
Length: 718  
Fragment?: false
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Protein
Q571G0
Organism: Mus musculus/domesticus
Length: 718  
Fragment?: true
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Protein
F7DC05
Organism: Mus musculus/domesticus
Length: 138  
Fragment?: true
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Publication
2548579 | -
First Author: Kimura S
Year: 1989
Journal: Biochemistry
Title: Structure of the human thyroid peroxidase gene: comparison and relationship to the human myeloperoxidase gene.
Volume: 28
Issue: 10
Pages: 4481-9
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Publication
6295491 | -
First Author: Wever R
Year: 1982
Journal: Biochim Biophys Acta
Title: The peroxidation of thiocyanate catalysed by myeloperoxidase and lactoperoxidase.
Volume: 709
Issue: 2
Pages: 212-9
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Publication
7774640 | -
First Author: Spessotto P
Year: 1995
Journal: Eur J Immunol
Title: Human eosinophil peroxidase enhances tumor necrosis factor and hydrogen peroxide release by human monocyte-derived macrophages.
Volume: 25
Issue: 5
Pages: 1366-73
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Publication
1320128 | -
First Author: Zeng J
Year: 1992
Journal: J Mol Biol
Title: X-ray crystal structure of canine myeloperoxidase at 3 A resolution.
Volume: 226
Issue: 1
Pages: 185-207
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Publication
8121489 | -
First Author: Picot D
Year: 1994
Journal: Nature
Title: The X-ray crystal structure of the membrane protein prostaglandin H2 synthase-1.
Volume: 367
Issue: 6460
Pages: 243-9
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Publication
2840655 | -
First Author: Kimura S
Year: 1988
Journal: Proteins
Title: Human myeloperoxidase and thyroid peroxidase, two enzymes with separate and distinct physiological functions, are evolutionarily related members of the same gene family.
Volume: 3
Issue: 2
Pages: 113-20
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Protein
A0A087WPT2
Organism: Mus musculus/domesticus
Length: 62  
Fragment?: true
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Protein
P49290
Organism: Mus musculus/domesticus
Length: 716  
Fragment?: false
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Protein
P22437
Organism: Mus musculus/domesticus
Length: 602  
Fragment?: false
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Protein
Q05769
Organism: Mus musculus/domesticus
Length: 604  
Fragment?: false
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Protein
Q3UMR6
Organism: Mus musculus/domesticus
Length: 604  
Fragment?: false
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Protein
Q3V1J3
Organism: Mus musculus/domesticus
Length: 403  
Fragment?: false
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Protein
Q7TMV2
Organism: Mus musculus/domesticus
Length: 561  
Fragment?: false
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Protein
Q3TJN9
Organism: Mus musculus/domesticus
Length: 488  
Fragment?: false
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Protein
Q3UZ23
Organism: Mus musculus/domesticus
Length: 602  
Fragment?: false
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Protein
Q543T1
Organism: Mus musculus/domesticus
Length: 602  
Fragment?: false
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Protein
P35419
Organism: Mus musculus/domesticus
Length: 914  
Fragment?: false
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Protein
B7ZWM4
Organism: Mus musculus/domesticus
Length: 1545  
Fragment?: false
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Protein
Q8BZ02
Organism: Mus musculus/domesticus
Length: 1058  
Fragment?: true
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Protein
A2AQ92
Organism: Mus musculus/domesticus
Length: 1551  
Fragment?: false
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Protein
A0A494BAW1
Organism: Mus musculus/domesticus
Length: 1545  
Fragment?: false
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Protein
A2AQ99
Organism: Mus musculus/domesticus
Length: 1517  
Fragment?: false
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Publication
8062820 | -
First Author: Nelson RE
Year: 1994
Journal: EMBO J
Title: Peroxidasin: a novel enzyme-matrix protein of Drosophila development.
Volume: 13
Issue: 15
Pages: 3438-47
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Protein
Q3UQ28
Organism: Mus musculus/domesticus
Length: 1475  
Fragment?: false
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Protein
A0A1W2P6L9
Organism: Mus musculus/domesticus
Length: 1295  
Fragment?: false
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Protein
B2RX13
Organism: Mus musculus/domesticus
Length: 1475  
Fragment?: false
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Protein
Q80U60
Organism: Mus musculus/domesticus
Length: 1431  
Fragment?: true
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Publication
7922023 | -
First Author: Li H
Year: 1994
Journal: Structure
Title: Structural variation in heme enzymes: a comparative analysis of peroxidase and P450 crystal structures.
Volume: 2
Issue: 6
Pages: 461-4
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