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Search results 201 to 237 out of 237 for Gpx5

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Type Details Score
Publication
1631065 | -
First Author: Cookson E
Year: 1992
Journal: Proc Natl Acad Sci U S A
Title: Identification of the major soluble cuticular glycoprotein of lymphatic filarial nematode parasites (gp29) as a secretory homolog of glutathione peroxidase.
Volume: 89
Issue: 13
Pages: 5837-41
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Publication
23567855 | -
First Author: Xia XF
Year: 2013
Journal: Fish Shellfish Immunol
Title: Cloning and functional analysis of glutathione peroxidase gene in red swamp crayfish Procambarus clarkii.
Volume: 34
Issue: 6
Pages: 1587-95
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Publication
8747457 | -
First Author: Moréra S
Year: 1995
Journal: Structure
Title: X-ray structure of human nucleoside diphosphate kinase B complexed with GDP at 2 A resolution.
Volume: 3
Issue: 12
Pages: 1307-14
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Publication
9742940 | -
First Author: Munier A
Year: 1998
Journal: FEBS Lett
Title: A new human nm23 homologue (nm23-H5) specifically expressed in testis germinal cells.
Volume: 434
Issue: 3
Pages: 289-94
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Publication
7669763 | -
First Author: Moréra S
Year: 1995
Journal: Biochemistry
Title: Mechanism of phosphate transfer by nucleoside diphosphate kinase: X-ray structures of the phosphohistidine intermediate of the enzymes from Drosophila and Dictyostelium.
Volume: 34
Issue: 35
Pages: 11062-70
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Protein Domain
IPR012410 | NDK_H5
Type: Family
Description: This family contains homologues of nucleoside diphosphate kinases (NDPKs). They are designated NDP kinase homologue 5 (NDK-H5), and differ from other NDPKs by having a C-terminal Dpy-30 motif. Despite considerable sequence similarity to other NDPKs, and conservation of seven out of nine known functionally important residues [, , ], human NDK-H5 (nm23-H5) seems to lack NDP kinase activity []. The nature of the sequence features specific to the NDK-H5 as compared to other NDPKs suggests that it may be unable to form hexamers and instead have a dimeric structure, which may affect its catalytic activity.NDK-H5 is thought to be involved in early stages of spermatogenesis []. Heterologous expression of murine NDK-H5 (nm23-M5) in yeast cells confers protection from cell death induced by Bax, which is due to the generation of reactive oxygen species, and over-expression of nm23-M5 in fibroblasts alters cellular levels of several antioxidant enzymes including Gpx5 []. Therefore, nm23-M5 may play a role in late spermatogenesis by increasing the ability of late-stage spermatids to eliminate reactive oxygen species [].
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Protein Domain
IPR000889 | Glutathione_peroxidase
Type: Family
Description: Glutathione peroxidase (GSHPx) () is an enzyme that catalyses the reduction of hydroperoxides by glutathione []. Its main function is to protect against the damaging effect of endogenously formed hydroperoxides. In higher vertebrates, several forms of GSHPx are known, including a ubiquitous cytosolic form (GSHPx-1), a gastrointestinal cytosolic form (GSHPx-GI), a plasma secreted form (GSHPx-P), and an epididymal secretory form (GSHPx-EP). In mammals there are eight GPx, divided in two clusters, the classical GPx (GPx1, GPx2, GPx3, GPx5 and GPx6) and phospholipid hydroperoxide GPx (GPx4, GPx7 and GPx8). The classical GPx is multimeric (commonly tetrameric) and soluble, while the phospholipid hydroperoxide (PHGPx) is monomeric and often membrane-associated []. In addition to these characterised forms, the sequence of a protein of unknown function []has been shown to be evolutionary related to those of GSHPx's.In filarial nematode parasites, the major soluble cuticular protein (gp29) is a secreted GSHPx, which may provide a mechanism of resistance to the immune reaction of the mammalian host by neutralising the products of the oxidative burst of leukocytes []. The structure of bovine seleno-glutathione peroxidase has been determined []. The protein belongs to the α-β class, with a three layer(aba) sandwich architecture. The catalytic site of GSHPx contains a conserved residue which is either a cysteine or, in many eukaryotic GSHPx, a selenocysteine [].
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Protein
Q8CC60
Organism: Mus musculus/domesticus
Length: 94  
Fragment?: true
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Publication
6852035 | -
First Author: Epp O
Year: 1983
Journal: Eur J Biochem
Title: The refined structure of the selenoenzyme glutathione peroxidase at 0.2-nm resolution.
Volume: 133
Issue: 1
Pages: 51-69
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Publication
2771650 | -
First Author: Dunn DK
Year: 1989
Journal: Nucleic Acids Res
Title: A human cDNA sequence for a novel glutathione peroxidase-related selenopeptide, GPRP.
Volume: 17
Issue: 15
Pages: 6390
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Protein
Q9D7B7
Organism: Mus musculus/domesticus
Length: 209  
Fragment?: false
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Protein
A0A0A6YY34
Organism: Mus musculus/domesticus
Length: 144  
Fragment?: false
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Protein
Q8K4U7
Organism: Mus musculus/domesticus
Length: 170  
Fragment?: false
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Protein
A0A0A6YVV2
Organism: Mus musculus/domesticus
Length: 145  
Fragment?: false
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Publication
7565867 | -
First Author: Barnett YA
Year: 1995
Journal: Mutat Res
Title: An investigation of antioxidant status, DNA repair capacity and mutation as a function of age in humans.
Volume: 338
Issue: 1-6
Pages: 115-28
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Protein
Q9JHC0
Organism: Mus musculus/domesticus
Length: 190  
Fragment?: false
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Protein
P11352
Organism: Mus musculus/domesticus
Length: 201  
Fragment?: false
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Protein
Q99MH5
Organism: Mus musculus/domesticus
Length: 211  
Fragment?: false
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Protein
P46412
Organism: Mus musculus/domesticus
Length: 226  
Fragment?: false
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Protein
O70325
Organism: Mus musculus/domesticus
Length: 197  
Fragment?: false
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Protein
P21765
Organism: Mus musculus/domesticus
Length: 221  
Fragment?: false
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Protein
Q91WR8
Organism: Mus musculus/domesticus
Length: 221  
Fragment?: false
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Protein
Q99LJ6
Organism: Mus musculus/domesticus
Length: 186  
Fragment?: false
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Protein
Q3TI34
Organism: Mus musculus/domesticus
Length: 170  
Fragment?: false
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Protein
Q496Q2
Organism: Mus musculus/domesticus
Length: 221  
Fragment?: false
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Protein
Q3V2L8
Organism: Mus musculus/domesticus
Length: 211  
Fragment?: false
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Protein
Q8CDQ5
Organism: Mus musculus/domesticus
Length: 221  
Fragment?: false
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Protein
Q3TNK3
Organism: Mus musculus/domesticus
Length: 186  
Fragment?: false
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Protein
A0A1C7ZMZ7
Organism: Mus musculus/domesticus
Length: 217  
Fragment?: true
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Protein
A0A1C7ZMZ5
Organism: Mus musculus/domesticus
Length: 199  
Fragment?: true
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Protein
Q5XJZ8
Organism: Mus musculus/domesticus
Length: 174  
Fragment?: true
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Protein
Q76LV0
Organism: Mus musculus/domesticus
Length: 253  
Fragment?: false
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Protein
S4R1E5
Organism: Mus musculus/domesticus
Length: 157  
Fragment?: false
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Protein
A0A0R4J111
Organism: Mus musculus/domesticus
Length: 190  
Fragment?: false
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Protein
Q3TIF2
Organism: Mus musculus/domesticus
Length: 182  
Fragment?: false
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Protein
Q9D111
Organism: Mus musculus/domesticus
Length: 147  
Fragment?: false
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Publication
2142875 | -
 
First Author: Stadtman TC
Year: 1990
Journal: Annu Rev Biochem
Title: Selenium biochemistry.
Volume: 59
Pages: 111-27
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