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Information on EC 1.11.1.12 - phospholipid-hydroperoxide glutathione peroxidase and Organism(s) Homo sapiens and UniProt Accession P36969

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IUBMB Comments
A protein containing a selenocysteine residue. The products of action of EC 1.13.11.12 lipoxygenase on phospholipids can act as acceptors; H2O2 can also act, but much more slowly (cf. EC 1.11.1.9 glutathione peroxidase).
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This record set is specific for:
Homo sapiens
UNIPROT: P36969
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
selenoprotein p, phgpx, glutathione peroxidase 4, phospholipid hydroperoxide glutathione peroxidase, gpx-4, glutathione peroxidase-4, npgpx, selenoperoxidase, gpx4b, gpx4a, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glutathione peroxidase 4
-
phospholipid hydroperoxide glutathione peroxidase-4
-
glutathione peroxidase-4
-
-
hydroperoxide glutathione peroxidase
-
-
-
-
non-selenocysteine PHGPx
-
-
NPGPx
-
-
peroxidation-inhibiting protein
-
-
-
-
peroxidation-inhibiting protein: peroxidase, glutathione (phospholipid hydroperoxide-reducing)
-
-
-
-
PHGPX
phospholipid hydroperoxide glutathione peroxidase
selenium-dependent glutathione peroxidase type-4
-
-
selenoperoxidase
-
-
selenoprotein P
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 glutathione + a hydroperoxy-fatty-acyl-[lipid] = glutathione disulfide + a hydroxy-fatty-acyl-[lipid] + H2O
show the reaction diagram
tert-uni ping-pong mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
reduction
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
glutathione:lipid-hydroperoxide oxidoreductase
A protein containing a selenocysteine residue. The products of action of EC 1.13.11.12 lipoxygenase on phospholipids can act as acceptors; H2O2 can also act, but much more slowly (cf. EC 1.11.1.9 glutathione peroxidase).
CAS REGISTRY NUMBER
COMMENTARY hide
97089-70-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 glutathione + a hydroperoxy-fatty-acyl-[lipid]
glutathione disulfide + a hydroxy-fatty-acyl-[lipid] + H2O
show the reaction diagram
-
-
-
?
2 glutathione + H2O2
glutathione disulfide + 2 H2O
show the reaction diagram
-
-
-
?
2 glutathione + phosphatidylcholine hydroperoxide
glutathione disulfide + ? + H2O
show the reaction diagram
-
-
-
?
2 glutathione + tert-butyl hydroperoxide
glutathione disulfide + 2-methylpropan-2-ol + H2O
show the reaction diagram
-
-
-
?
glutathione + (beta-(13-hydroperoxy-cis-9,trans-11-octadecadienoyl)-gamma-palmitoyl)-L-alpha-phosphatidylcholine
?
show the reaction diagram
-
-
-
-
?
glutathione + 1-palmitoyl-2-(13-hydroperoxy-cis-9,trans-11-octadecadienoyl)-3-phosphatidylcholine
?
show the reaction diagram
-
-
-
-
?
glutathione + a lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
-
-
-
?
glutathione + cholesterol hydroperoxide
?
show the reaction diagram
-
-
-
-
?
glutathione + cumene hydroperoxide
?
show the reaction diagram
-
-
-
-
?
glutathione + dilinoleoyl phosphatidylcholine hydroperoxide
?
show the reaction diagram
-
-
-
-
?
glutathione + H2O2
?
show the reaction diagram
glutathione + L-alpha-phosphatidylcholine hydroperoxide
?
show the reaction diagram
-
-
-
-
?
glutathione + linoleic acid hydroperoxide
?
show the reaction diagram
-
-
-
-
?
glutathione + lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
glutathione + phosphatidylcholine hydroperoxide
?
show the reaction diagram
-
activity assay
-
-
?
glutathione + tert-butyl hydroperoxide
?
show the reaction diagram
-
no activity
-
-
?
glutathione + tert-butylhydroperoxide
?
show the reaction diagram
-
-
-
-
?
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
2 glutathione + a hydroperoxy-fatty-acyl-[lipid]
glutathione disulfide + a hydroxy-fatty-acyl-[lipid] + H2O
show the reaction diagram
-
-
-
?
glutathione + a lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
-
-
-
?
glutathione + lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
glutathione
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
selenium
about 50% selenium incorporation, recombinant protein
selenium
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-chloro-N-(3-chloro-4-methoxyphenyl)-N-[(1S)-2-(phenylethylethylamino)-2-oxo-1-(thiophen-2-yl)ethyl]acetamide
i.e. ML162
-
deoxycholate
-
in reaction with cumene hydroperoxide and linoleic acid hydroperoxide
iodoacetate
-
2 mM, complete inhibition
Mercaptosuccinate
-
0.1 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9-hydroperoxy-10E,12Z-octadecadienoic acid
9-HpODE, induces a dose-dependent intracellular increase in GSH oxidation that is independent of intracellular H2O2 production and is mediated by glutathione peroxidase 4 (GPx4) in BEAS-2B cells. Glucose deprivation potentiates the oxidative effect of 9-HpODE on GSH and inhibits its recovery
-
deoxycholate
-
activity is slightly enhanced, but is enhanced by 50% together with Triton X-100
selenoprotein P
-
2 nM, 3fold stimulation of activity after 24h
-
Sodium selenite
-
100 nM, 3fold stimulation of activity after 24h
Triton X-100
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
20.6
H2O2
pH 7.4, 37°C
9.2
phosphatidylcholine hydroperoxide
pH 7.4, 37°C
5.1
tert-butyl hydroperoxide
pH 7.4, 37°C
91
(beta-(13-hydroperoxy-cis-9,trans-11-octadecadienoyl)-gamma-palmitoyl)-L-alpha-phosphatidylcholine
-
-
additional information
additional information
-
mutant compared to wild-type enzyme
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
14
substrate tert-butyl hydroperoxide, pH 7.4, 37°C
25
substrate phosphatidylcholine hydroperoxide, pH 7.4, 37°C
56
substrate H2O2, pH 7.4, 37°C
0.0038
-
crude platelet homogenate
0.0048
-
cytosolic fraction
0.006
-
mitochondrial fraction
0.009
-
-
0.0096
-
membrane fraction
160
-
purified enzyme, substrate linoleic acid hydroperoxide
190
-
purified enzyme, substrate cumene hydroperoxide
2.03
-
addition of Triton X-100 and deoxycholate
210
-
purified enzyme, substrate H2O2
30.6
pH 7.4, 37°C
336
-
purified enzyme, substrate (beta-(13-hydroperoxy-cis-9,trans-11-octadecadienoyl)-gamma-palmitoyl)-L-alpha-phosphatidylcholine
additional information
-
mutant compared to wild-type enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9
mutant C2S/C10S/C37S/C66S/C75S/C107S/C148S
7.6
-
assay at
8
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
mutant C2S/C10S/C37S/C66S/C75S/C107S/C148S
37
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
less than 10% of maximum activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
subclone s6, SV40 large T antigen-transformed human airway epithelial cells
Manually annotated by BRENDA team
-
knockdown of GPx-4 by small interfering RNA technique in a human ovarian cancer cell line significantly enhances the cytotoxic effect of docosahexaenoic acid in a time- and concentration-dependent manner. This cytotoxic effect of docosahexaenoic acid is reversed by pretreatment with vitamin E, suggesting that the enhanced toxicity ofGPx-4 knockdown is due to changes in the ability of the cells to handle oxidative stress
Manually annotated by BRENDA team
-
transgenic mouse
Manually annotated by BRENDA team
-
resting blood platelet
Manually annotated by BRENDA team
-
PHGPx expression levels are downregulated in poorly differentiated (grade 3) breast invasive ductal carcinoma. PHGPx expression levels decrease gradually with tumor grade from grade 1 to grade 3. Downregulation of PHGPx in cases that showed p53 accumulation compared with cases without p53 immunostaining is observed. PHGPx is downregulated in cases without progesterone receptors immunostaining compared with cases with PR immunostaining
Manually annotated by BRENDA team
-
treatment with docosahexaenoic acid results in 95% decrease in GPx-4 level
Manually annotated by BRENDA team
-
treatment with docosahexaenoic acid results in 90% decrease in GPx-4 level
Manually annotated by BRENDA team
-
expression level may vary during mammary gland development
Manually annotated by BRENDA team
-
treatment with docosahexaenoic acid results in 90% decrease in GPx-4 level
Manually annotated by BRENDA team
-
treatment with docosahexaenoic acid results in 60% decrease in GPx-4 level
Manually annotated by BRENDA team
-
treatment with docosahexaenoic acid results in 21% decrease in GPx-4 level
Manually annotated by BRENDA team
-
treatment with docosahexaenoic acid results in 95% decrease in GPx-4 level
Manually annotated by BRENDA team
-
extracellular localisation
Manually annotated by BRENDA team
-
treatment with docosahexaenoic acid results in 85% decrease in GPx-4 level
Manually annotated by BRENDA team
-
enzyme is transformed to an oxidatively inactivated protein in mature sperm, where it is a major constituent of the mitochondrial capsule in the midpiece
Manually annotated by BRENDA team
-
enzyme is expressed as active peroxidase
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
extracellular localisation
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
glutathione (GSH) is the most abundant intracellular antioxidant, with millimolar concentrations present in the cytosol of most cell types. The ratio of oxidized (GSSG) to reduced glutathione, which defines the glutathione redox potential (EGSH) in the Nernst equation, is an important indicator of overall cellular oxidative state. Under homeostatic conditions, the EGSH reflects a ratio of GSH:GSSG of 100:1. roGFP is a genetically encoded fluorogenic sensor that has been used in a variety of cell types for real-time assessments of the EGSH. roGFP has been shown to equilibrate with EGSH through a redox relay that is initiated by hydrogen peroxide (H2O2) and involves the participation of the enzymes GPx, glutaredoxin (Grx), and glutathione reductase (GR)
physiological function
linoleic acid is present in the surfactant lining the airway epithelium, where it is a target of lipid peroxidation by oxidizing air pollutants such as ozone. 9-hydroperoxy-10E,12Z-octadecadienoic acid (9-HpODE) is a product of linoleic acid peroxidation that can be generated enzymatically or via radical or non-radical mediated oxidation. Exposure of human airway epithelial cells (HAEC) to 9-HpODE results in an alteration of intracellular EGSH. Enzyme glutathione peroxidase 4, GPx4, is involved in the initiation of GSH oxidation in human aortic endothelial cells (HAEC) by 9-hydroperoxy-10E,12Z-octadecadienoic acid (9-HpODE), but not in GSH oxidation induction by H2O2 or the low molecular weight alkyl tert-butyl hydroperoxide (TBH). 9-Hydroperoxy-10E,12Z-octadecadienoic acid (9-HpODE) is a product of linoleic acid peroxidation that can be generated enzymatically or via radical or non-radical mediated oxidation. Long chain lipid hydroperoxides can directly alter cytosolic EGSH independent of secondary lipid oxidation products or H2O2 production. NADPH has a protective role against 9-HpODE induced EGSH changes. GPx4 is involved specifically in the reduction of long-chain lipid hydroperoxides, leading to GSH oxidation. The same concentration of 9-hydroxy-10E,12Z-octadecadienoic acid (9-HODE), the reduced product of 9-HpODE, does not result in GSH oxidation, as reported by roGFP, over the same period. Exposure to 9-HpODE causes a dose-dependent increase in GSH oxidation in HAEC that is independent of intracellular or extracellular H2O2 production and is exacerbated by NADPH depletion
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GPX4_HUMAN
197
0
22175
Swiss-Prot
Secretory Pathway (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
16100
-
gel filtration
20000
-
1 * 20000, non-mitochondrial S-form of the enzyme
21000
23000
-
1 * 23000, mitochondrial L-form of the enzyme
66000
-
1 * 66000, SDS-PAGE
69000
-
native PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 21000, SDS-PAGE
monomer
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
molecular modeling of mutant C2S/C10S/C37S/C66S/C75S/C107S/C148S. The catalytic tetrad consists of residues Sec46, Gln81, Trp136, and Asn137
sparse matrix crystallization method, crystal structure of the catalytically active U46C mutant of human GPx4 to 1.55 A resolution
structure of recombinant protein, at 1.3 A resolution. Data indicate a monomeric protein, which contains the catalytic selenium at the redox level of the seleninic acid. The presumed catalytic triad consists of residues Sec(Cys)46, Gln81 and Trp136. The triad is localized at a flat impression of the protein surface
structure of the wild-type form of GPX4 at 1.0 A resolution and in complex with inhibitor 2-chloro-N-(3-chloro-4-methoxyphenyl)-N-[(1S)-2-(phenylethylethylamino)-2-oxo-1-(thiophen-2-yl)ethyl]acetamide. Active site residue is Sec46
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C2S/C10S/C37S/C66S/C75S/C107S/C148S
substitution of all Cys residues by Ser. The mutant exhibits a Ping-Pong mechanism and structure similar to that of native GPx4, the activity is similar to wild-type
C66S
mutation of the second reactive Cys residue, crystallization data
Q81A
no residual activity
Q81E
no residual activity
Q81L
no residual activity
U46A
no residual activity
U46C
less than 1 % of residual activity
U46S
no residual activity
W136A
almost complete loss of activity
W136F
almost complete loss of activity
SeC46C
-
expression of mutant in Escherichia coli as His-tagged fusion protein and in baculovirus/insect cell system, site directed mutagenesis to avoid recognition problems of selenocysteine encoded by TGA stop codon in the expression systems, mutant has reduced specific acitvity
additional information
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-40°C, about 30% loss of activity during 1 freeze-thaw-cycle
-
4°C, loss of 10% activity in 1 week
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme partially from HEK-293T cells by ultrafiltration
large-scale, wild-type and mutant SeC46C from baculovirus/insect cell expression system and mutant SeC46C from expression in Escherichia coli as His-tagged fusion protein
-
recombinant protein
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in a cysteine-auxotrophic Escherichia coli strain
expression in Escherichia coli
expression in HEK293-6E cell
expression of mutant enzyme U46C in Escherichia coli
recombinant enzyme expression in HEK-293T cells
expressed in MIA PaCa-2 and AsPC-1 human pancreatic cancer cells
-
expressed in tumor cell transfectant clone 7G4
-
expression of wild-type enzyme and SeC46C mutant in baculovirus/insect cell system and expression of mutant SeC46C as His-tagged fusion protein in Escherichia coli
-
expresssion in HEK-293T cell
transgenic mice overexpressing human GPx4 are generated
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
because the content of enzyme, irrespective of the cause of alteration, is correlated with fertility-related parameters, PHGPx can be considered a predictive measure for fertilization capacity
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Saito, Y.; Hayashi, T.; Tanaka, A.; Watanabe, Y.; Suzuki, M.; Saito, E.; Takahashi, K.
Selenoprotein P in human plasma as an extracellular phospholipid hydroperoxide glutathione peroxidase. Isolation and enzymatic characterization of human selenoprotein P
J. Biol. Chem.
274
2866-2871
1999
Homo sapiens
Manually annotated by BRENDA team
Chambers, S.J.; Lambert, N.; Williamson, G.
Purification of a cytosolic enzyme from human liver with phospholipid hydroperoxide glutathione peroxidase activity
Int. J. Biochem.
26
1279-1286
1994
Homo sapiens
Manually annotated by BRENDA team
Schnurr, K.; Borchert, A.; Gerth, C.; Anton, M.; Kuhn, H.
Bacterial and nonbacterial expression of wild-type and mutant human phospholipid hydroperoxide glutathione peroxidase and purification of the mutant enzyme in the milligram scale
Protein Expr. Purif.
19
403-410
2000
Homo sapiens
Manually annotated by BRENDA team
Foresta, C.; Flohe, L.; Garolla, A.; Roveri, A.; Ursini, F.; Maiorino, M.
Male fertility is linked to the selenoprotein phospholipid hydroperoxide glutathione peroxidase
Biol. Reprod.
67
967-971
2002
Homo sapiens
Manually annotated by BRENDA team
Tramer, F.; Caponecchia, L.; Sgro, P.; Martinelli, M.; Sandri, G.; Panfili, E.; Lenzi, A.; Gandini, L.
Native specific activity of glutathione peroxidase (GPx-1), phospholipid hydroperoxide glutathione peroxidase (PHGPx) and glutathione reductase (GR)does not differ between normo- and hypomotile human sperm samples
Int. J. Androl.
27
88-93
2004
Homo sapiens
Manually annotated by BRENDA team
Utomo, A.; Jiang, X.; Furuta, S.; Yun, J.; Levin, D.S.; Wang, Y.C.; Desai, K.V.; Green, J.E.; Chen, P.L.; Lee, W.H.
Identification of a novel putative non-selenocysteine containing phospholipid hydroperoxide glutathione peroxidase (NPGPx) essential for alleviating oxidative stress generated from polyunsaturated fatty acids in breast cancer cells
J. Biol. Chem.
279
43522-43529
2004
Homo sapiens
Manually annotated by BRENDA team
Diaconu, M.; Tangat, Y.; Boehm, D.; Kuehn, H.; Michelmann, H.W.; Schreiber, G.; Haidl, G.; Glander, H.J.; Engel, W.; Nayernia, K.
Failure of phospholipid hydroperoxide glutathione peroxidase expression in oligoasthenozoospermia and mutations in the PHGPx gene
Andrologia
38
152-157
2006
Homo sapiens
Manually annotated by BRENDA team
Hattori, H.; Imai, H.; Furuhama, K.; Sato, O.; Nakagawa, Y.
Induction of phospholipid hydroperoxide glutathione peroxidase in human polymorphonuclear neutrophils and HL60 cells stimulated with TNF-alpha
Biochem. Biophys. Res. Commun.
337
464-473
2005
Homo sapiens
Manually annotated by BRENDA team
Januel, C.; El Hentati, F.; Carreras, M.; Arthur, J.R.; Calzada, C.; Lagarde, M.; Vericel, E.
Phospholipid-hydroperoxide glutathione peroxidase (GPx-4) localization in resting platelets, and compartmental change during platelet activation
Biochim. Biophys. Acta
1761
1228-1234
2006
Homo sapiens
Manually annotated by BRENDA team
Steinbrenner, H.; Bilgic, E.; Alili, L.; Sies, H.; Brenneisen, P.
Selenoprotein P protects endothelial cells from oxidative damage by stimulation of glutathione peroxidase expression and activity
Free Radic. Res.
40
936-943
2006
Homo sapiens
Manually annotated by BRENDA team
Liu, J.; Du, J.; Zhang, Y.; Sun, W.; Smith, B.J.; Oberley, L.W.; Cullen, J.J.
Suppression of the malignant phenotype in pancreatic cancer by overexpression of phospholipid hydroperoxide glutathione peroxidase
Hum. Gene Ther.
17
105-116
2006
Homo sapiens
Manually annotated by BRENDA team
Kriska, T.; Girotti, A.W.
A thin layer chromatographic method for determining the enzymatic activity of peroxidases catalyzing the two-electron reduction of lipid hydroperoxides
J. Chromatogr. B
827
58-64
2005
Homo sapiens
Manually annotated by BRENDA team
Scheerer, P.; Borchert, A.; Krauss, N.; Wessner, H.; Gerth, C.; Hoehne, W.; Kuhn, H.
Structural basis for catalytic activity and enzyme polymerization of phospholipid hydroperoxide glutathione peroxidase-4 (GPx4)
Biochemistry
46
9041-9049
2007
Homo sapiens (P36969), Homo sapiens
Manually annotated by BRENDA team
Conrad, M.; Schneider, M.; Seiler, A.; Bornkamm, G.W.
Physiological role of phospholipid hydroperoxide glutathione peroxidase in mammals
Biol. Chem.
388
1019-1025
2007
Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Cejas, P.; Garcia-Cabezas, M.A.; Casado, E.; Belda-Iniesta, C.; De Castro, J.; Fresno, J.A.; Sereno, M.; Barriuso, J.; Espinosa, E.; Zamora, P.; Feliu, J.; Redondo, A.; Hardisson, D.A.; Renart, J.; Gonzalez-Baron, M.
Phospholipid hydroperoxide glutathione peroxidase (PHGPx) expression is downregulated in poorly differentiated breast invasive ductal carcinoma
Free Radic. Res.
41
681-687
2007
Homo sapiens
Manually annotated by BRENDA team
Ding, W.Q.; Lind, S.E.
Phospholipid hydroperoxide glutathione peroxidase plays a role in protecting cancer cells from docosahexaenoic acid-induced cytotoxicity
Mol. Cancer Ther.
6
1467-1474
2007
Homo sapiens
Manually annotated by BRENDA team
Guo, Z.; Ran, Q.; Roberts, L.J.; Zhou, L.; Richardson, A.; Sharan, C.; Wu, D.; Yang, H.
Suppression of atherogenesis by overexpression of glutathione peroxidase-4 in apolipoprotein E-deficient mice
Free Radic. Biol. Med.
44
343-352
2008
Homo sapiens
Manually annotated by BRENDA team
Han, X.; Fan, Z.; Yu, Y.; Liu, S.; Hao, Y.; Huo, R.; Wei, J.
Expression and characterization of recombinant human phospholipid hydroperoxide glutathione peroxidase
IUBMB Life
65
951-956
2013
Homo sapiens (D6W5Y2), Homo sapiens
Manually annotated by BRENDA team
Yu, Y.; Song, J.; Guo, X.; Wang, S.; Yang, X.; Chen, L.; Wei, J.
Characterization and structural analysis of human selenium-dependent glutathione peroxidase 4 mutant expressed in Escherichia coli
Free Radic. Biol. Med.
71
332-338
2014
Homo sapiens (P36969), Homo sapiens
Manually annotated by BRENDA team
Moosmayer, D.; Hilpmann, A.; Hoffmann, J.; Schnirch, L.; Zimmermann, K.; Badock, V.; Furst, L.; Eaton, J.; Viswanathan, V.; Schreiber, S.; Gradl, S.; Hillig, R.
Crystal structures of the selenoprotein glutathione peroxidase 4 in its apo form and in complex with the covalently bound inhibitor ML162
Acta Crystallogr. D Struct. Biol.
77
237-248
2021
Homo sapiens (P36969), Homo sapiens
Manually annotated by BRENDA team
Corteselli, E.M.; Gibbs-Flournoy, E.; Simmons, S.O.; Bromberg, P.; Gold, A.; Samet, J.M.
Long chain lipid hydroperoxides increase the glutathione redox potential through glutathione peroxidase 4
Biochim. Biophys. Acta
1863
950-959
2019
Homo sapiens (P36969)
Manually annotated by BRENDA team
Borchert, A.; Kalms, J.; Roth, S.; Rademacher, M.; Schmidt, A.; Holzhutter, H.; Kuhn, H.; Scheerer, P.
Crystal structure and functional characterization of selenocysteine-containing glutathione peroxidase 4 suggests an alternative mechanism of peroxide reduction
Biochim. Biophys. Acta Mol. Cell Biol. Lipids
1863
1095-1107
2018
Homo sapiens (P36969), Homo sapiens
Manually annotated by BRENDA team