Information on EC 1.11.1.12 - phospholipid-hydroperoxide glutathione peroxidase

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The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY hide
1.11.1.12
-
RECOMMENDED NAME
GeneOntology No.
phospholipid-hydroperoxide glutathione peroxidase
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
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Glutathione metabolism
-
-
glutathione-peroxide redox reactions
-
-
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
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
animal
invertebrate animals, the GPx genes are isolated from various platyhelminths via in silico screening
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
Shamouti orange, encoding gene csa
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
mitochondrial enzyme
TrEMBL
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
cattle tick
TrEMBL
Manually annotated by BRENDA team
American trypanosome
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
glutathione + 1-palmitoyl-2-(13-hydroperoxy-cis-9,trans-11-octadecadienoyl)-3-phosphatidylcholine
?
show the reaction diagram
-
-
-
-
?
glutathione + 1-palmitoyl-2-(13-hydroperoxy-cis-9,trans-11-octadecadienoyl)-L-3-phosphatidylcholine
?
show the reaction diagram
-
-
-
-
?
glutathione + 3beta-hydroxycholest-5-ene-7alpha-hydroperoxide
cholest-5-ene-3beta,7alpha-diol + ?
show the reaction diagram
-
-
-
-
?
glutathione + a lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
glutathione + cardiolipin
?
show the reaction diagram
glutathione + cholesterol hydroperoxide
?
show the reaction diagram
-
-
-
-
?
glutathione + cholesterol hydroperoxides
?
show the reaction diagram
glutathione + cumene hydroperoxide
?
show the reaction diagram
glutathione + dilinoleoyl phosphatidylcholine hydroperoxide
?
show the reaction diagram
glutathione + fatty acid hydroperoxides
?
show the reaction diagram
-
-
-
-
?
glutathione + H2O2
?
show the reaction diagram
glutathione + L-alpha-phosphatidylcholine hydroperoxide
?
show the reaction diagram
glutathione + LDL hydroperoxides
?
show the reaction diagram
-
-
-
-
?
glutathione + linoleic acid hydroperoxide
?
show the reaction diagram
glutathione + lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
glutathione + phosphatidic acid hydroperoxide
?
show the reaction diagram
-
-
-
-
?
glutathione + phosphatidylcholine hydroperoxide
?
show the reaction diagram
glutathione + phosphatidylethanolamine hydroperoxide
?
show the reaction diagram
-
-
-
-
?
glutathione + phosphatidylserine hydroperoxide
?
show the reaction diagram
-
-
-
-
?
glutathione + phospholipid hydroperoxides
?
show the reaction diagram
glutathione + QKSPCCPKSP
?
show the reaction diagram
-
-
-
?
glutathione + t-butyl hydroperoxide
?
show the reaction diagram
-
-
-
-
?
glutathione + tert-butyl hydroperoxide
?
show the reaction diagram
glutathione + tert-butyl-hydroperoxide
?
show the reaction diagram
glutathione + tert-butylhydroperoxide
?
show the reaction diagram
-
-
-
-
?
GSH + cumene hydroperoxide
GSSG + ?
show the reaction diagram
GSH + H2O2
GSSG + ?
show the reaction diagram
-
about 50% of the activity with cumene hydroperoxide
-
-
?
GSH + linoleic acid hydroperoxide
GSSG + ?
show the reaction diagram
-
-
-
-
?
GSH + phosphatidylcholine dilinoleoyl hydroperoxide
GSSG + ?
show the reaction diagram
-
-
-
-
?
GSH + tert-butyl hydroperoxide
GSSG + ?
show the reaction diagram
KKSQCCQQKT + H2O2
KKSQ-L-cystinyl-QQKT + 2 H2O
show the reaction diagram
-
-
-
?
KPPCCPPK + H2O2
KPP-L-cystinyl-PPK + 2 H2O
show the reaction diagram
-
-
-
?
PKPPCCPPKP + H2O2
PKPP-L-cystinyl-PPKP + 2 H2O
show the reaction diagram
-
-
-
?
PKSPCCPPKP + H2O2
PKSP-L-cystinyl-PPKP + 2 H2O
show the reaction diagram
-
-
-
?
PKSPCCPPKS + H2O2
PKSP-L-cystinyl-PPKS + 2 H2O
show the reaction diagram
-
-
-
?
PPCCPP + H2O2
PP-L-cystinyl-PP + 2 H2O
show the reaction diagram
-
-
-
?
PPKPCCPPKP + H2O2
PPKP-L-cystinyl-PKP + 2 H2O
show the reaction diagram
-
-
-
?
PPPPCCPPPP + H2O2
PPPP-L-cystinyl-PPPP + 2 H2O
show the reaction diagram
-
-
-
?
QKPPCCPKSP + H2O2
QKPP-L-cystinyl-PKSP + 2 H2O
show the reaction diagram
-
-
-
?
thioredoxin + 1-palmitoyl-2-(13-hydroperoxy-cis-9,trans-11-octadecadienoyl)-L-3-phosphatidylcholine
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
alpha-tocopherol
-
complete inhibition of glutathione oxidation
deoxycholate
iodoacetate
Mercaptosuccinate
-
0.1 mM
unsaturated fatty acids
-
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
17-beta-estradiol
causes increase in GPx-4 activity
deoxycholate
-
activity is slightly enhanced, but is enhanced by 50% together with Triton X-100
H2O2
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-
NaCl
-
-
selenoprotein P
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2 nM, 3fold stimulation of activity after 24h
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Sodium selenite
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100 nM, 3fold stimulation of activity after 24h
Triton X-100
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00014 - 0.0362
1-palmitoyl-2-(13-hydroperoxy-cis-9,trans-11-octadecadienoyl)-L-3-phosphatidylcholine
0.0017 - 608
cumene hydroperoxide
1.37
glutathione
-
-
0.0008656 - 0.799
H2O2
0.00074
L-alpha-phosphatidylcholine hydroperoxide
-
recombinant enzyme
-
0.00058 - 0.0827
linoleic acid hydroperoxide
0.0121 - 0.0249
phosphatidylcholine dilinoleoyl hydroperoxide
0.0002353 - 0.01113
phosphatidylcholine hydroperoxide
0.011
phospholipid hydroperoxide
-
-
-
0.0056 - 4.344
tert-butyl hydroperoxide
2.932
tert-butyl-hydroperoxide
apparent KM
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
91
(beta-(13-hydroperoxy-cis-9,trans-11-octadecadienoyl)-gamma-palmitoyl)-L-alpha-phosphatidylcholine
Homo sapiens
-
-
additional information
additional information
Homo sapiens
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mutant compared to wild-type enzyme
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.019
alpha-tocopherol
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-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0038
-
crude platelet homogenate
0.0048
-
cytosolic fraction
0.006
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mitochondrial fraction
0.009
-
-
0.0096
-
membrane fraction
0.04
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low-PHGPx group
0.051
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enzyme from tissue lysate, using L-alpha-phosphatidylcholine hydroperoxide as peroxide substrate, at 37°C
0.0539
-
low-PHGPx, Chianina
0.056
-
low-PHGPx, Marchigiana
0.0746
-
low-PHGPx, Romagnola
0.13
-
high-PHGPx group
0.2242
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high-PHGPx, Chianina
0.2447
-
high-PHGPx, Romagnola
0.2453
-
high-PHGPx, Marchigiana
0.3
in 0.1 M potassium phosphate, pH 7.8 with 1 mM EDTA, using 0.1 mM KKSQCCQQKT as substrate
0.4
in 0.1 M potassium phosphate, pH 7.8 with 1 mM EDTA, using 0.1 mM KPPCCPPK as substrate
0.9
-
substrate tert-butyl hydroperoxide
2.03
-
addition of Triton X-100 and deoxycholate
2.2
-
substrate phosphatidylcholine
3.8
-
substrate cumene hydroperoxide
7
-
purified enzyme
13.6
in 0.1 M potassium phosphate, pH 7.8 with 1 mM EDTA, using 0.1 mM PKSPCCPPKP as substrate
21.5
-
enzyme after 422fold purification, using L-alpha-phosphatidylcholine hydroperoxide as peroxide substrate, at 37°C
25.2
in 0.1 M potassium phosphate, pH 7.8 with 1 mM EDTA, using 0.1 mM PPKPCCPPKP as substrate
28.3
in 0.1 M potassium phosphate, pH 7.8 with 1 mM EDTA, using 0.1 mM PKPPCCPPKP as substrate
30.6
pH 7.4, 37°C
36
in 0.1 M potassium phosphate, pH 7.8 with 1 mM EDTA, using 0.1 mM QKSPCCPKSP as substrate
37.5
in 0.1 M potassium phosphate, pH 7.8 with 1 mM EDTA, using 0.1 mM QKPPCCPKSP as substrate
42
in 0.1 M potassium phosphate, pH 7.8 with 1 mM EDTA, using 0.1 mM PKSPCCPPKS as substrate
69
in 0.1 M potassium phosphate, pH 7.8 with 1 mM EDTA, using 0.1 mM PPPPCCPPPP as substrate
90
-
partially purified enzyme
107
-
purified enzyme
160
-
purified enzyme, substrate linoleic acid hydroperoxide
160.2
in 0.1 M potassium phosphate, pH 7.8 with 1 mM EDTA, using 0.1 mM PPCCPP as substrate
190
-
purified enzyme, substrate cumene hydroperoxide
195.1
-
purified enzyme
210
-
purified enzyme, substrate H2O2
310.1
-
purified enzyme
336
-
purified enzyme, substrate (beta-(13-hydroperoxy-cis-9,trans-11-octadecadienoyl)-gamma-palmitoyl)-L-alpha-phosphatidylcholine
109900
-
purified enzyme from cytosol
146300
-
purified enzyme from mitochondria
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 11
-
pH 8.0: about 40% of maximal activity, pH 11: about 80% of maximal activity
8 - 9.5
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-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
activity assay
40
activity assay
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 40
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10°C: 80% of maximal activity, 40°C: 60% of maximal activity
10 - 45
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-
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5
-
isoelectric focusing electrophoresis
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
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
-
smooth muscle cells
Manually annotated by BRENDA team
-
resting blood platelet
Manually annotated by BRENDA team
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-
Manually annotated by BRENDA team
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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
-
ovular callus, salt-sensitive and adapted salt-tolerant cell lines
Manually annotated by BRENDA team
extraction of genomic DNA
Manually annotated by BRENDA team
-
keratinized surface epithelium
Manually annotated by BRENDA team
-
treatment with docosahexaenoic acid results in 90% decrease in GPx-4 level
Manually annotated by BRENDA team
-
basophil leucemia cell line S1 wild-type cell line and (RBL)2H3 cell line overexpressing mitochondrial phospholipid hydroperoxide glutathione peroxidase
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
-
pituicytes
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
-
PHGPx-overexpressed cell
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
100 nM 8(S/R)-hydroxy-11(S),12S-trans-epoxyeicosa-5Z,9E,14Z-trienoic acid upregulates phospholipid hydroperoxide glutathione peroxidase (PHGPx) mRNA and protein expressions. Under persistent oxidative stress the formation of 8(S/R)-hydroxy-11(S),12S-trans-epoxyeicosa-5Z,9E,14Z-trienoic acid and the 8(S/R)-hydroxy-11(S),12S-trans-epoxyeicosa-5Z,9E,14Z-trienoic acid-induced upregulation of PHGPx constitute a compensatory defense response to protect the vitality and functionality of the cell
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
of arteries
Manually annotated by BRENDA team
-
enzyme is expressed as active peroxidase
Manually annotated by BRENDA team
PHGPx expression is tightly regulated in pachytene spermatocytes, with any spatial-temporal increase in PHGPx expression resulting in damage to spermatogenesis and eventual loss of haploid cells
Manually annotated by BRENDA team
cDNA library
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
high-salt extract from retina
-
Manually annotated by BRENDA team
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6000
-
below, retina enzyme, gel filtration
16100
-
gel filtration
18000
His6-tagged fusion protein, determined by SDS-PAGE
18300
-
recombinant enzyme, glutathione-S-transferase-tag cut off, SDS-PAGE
18500
-
cytosolic enzyme form, SDS-PAGE
19000
determined by SDS-PAGE
19400
-
determined by gel filtration
21000
-
20 to 22 kDa
21480
calculated from sequence of cDNA
21500
-
mitochondrial enzyme form, SDS-PAGE
22000
-
gel filtration
22500
His6-McPHGPx fusion protein, determined by SDS-PAGE
23000
-
gel filtration
34000
-
nucleic enzyme form, SDS-PAGE
69000
-
native PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
-
tyrosine phosphorylation generates multiple isoforms of the mitochondrial capsule protein during sperm capacitation
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sparse matrix crystallization method, crystal structure of the catalytically active U46C mutant of human GPx4 to 1.55 A resolution
the crystal structure is solved to a resolution of 2.0 A
-
the crystal structures of the Sec43Cys and Sec43Ser mutants are solved at resolutions of 1.0 A and 1.7 A, respectively
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
thermal stability shows that the activity is significantly decreased when the temperature is higher than 40°C
65
-
complete loss of activity after 5 min
additional information
-
heat stress at 37°C leads to increase in RNA transcript level in salt-sensitive cell line and slightly also in salt-tolerant cell line, exposure to 4°C had no effect
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
alpha-tocopherol stabilizes triple mutant against H2O2 and unsaturated linolenate
-
presence of thiol, e.g. 2-mercaptoethanol, during purification is necessary for stabilization
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
urea
-
with the increase of urea concentration, the residual activity of OsPHGPx decreases correspondingly. When the urea concentration is above 5.0 mol/l, there is no residual activity. The unfolding process comprises of three zones: the native base-line zone between 0 and 2. 5 mol/l urea, the transition zone between 2.5 and 5.5 mol/l urea, and the denatured base-line zone above 5.5 mol/l urea. The transition zone has a midpoint at about 4.0 mol/l urea
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 10% glycerol, stable for several months
-
-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
ammonium sulfate precipitation, DEAE-Sepharose column chromatography, Sephadex G-50 gel filtration, and HiTrap SP column chromatography
-
by Ni2+-nitrilotriacetic acid Sepharose
by nickel affinity chromatography
from cytosol and mitochondria
-
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
-
on a Ni-NTA column, further purified by gel filtration
-
partially
partially from testis and to homogenity from sperm as recombinant enzyme expressed in Escherichia coli and as wild-type enzyme
-
Percoll step gradient and nickel affinity chromatography
-
recombinant enzyme
-
recombinant enzyme from Escherichia coli
-
recombinant protein
Sec43Cys is purified on a GSH-Sepharose column, Sec43Ser is purified by ionic exchange chromatography, the GST-tags are cleaved with bovine thrombin
-
using a HisTrap column
wild-type and mutant proteins
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
-
expressed in MIA PaCa-2 and AsPC-1 human pancreatic cancer cells
-
expressed in tumor cell transfectant clone 7G4
-
expression in Escherichia coli
expression in Escherichia coli; expression in Escherichia coli; expression in Escherichia coli; expression in Escherichia coli
expression of mutant enzyme U46C in Escherichia coli
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
-
expression vector encoding mitochondrial enzyme for overexpression in (RBL)2H3 cell line
-
expresssion in HEK-293T cell
for sequencing
-
His-tagged protein termed TcGPX1, expression in Escherichia coli
-
into the vector pET-28a+ for expression in Escherichia coli BL21DE3 cells, into the vector YEpGAP112 for a functional complementation test in yeast
into the vector pYEX-S1 for transformation into Saccharomyces cerevisiae cells
production of a transgenic mouse line overexpressing mPHGPx in the testis during the prophase of the first meiotic division, when the endogenous mPHGPx level is markedly lower than in the postmeiotic phase. Such mPHGPx overexpression is associated with male germ apoptosis, seminiferous tubule disorganization and reduced fertility
spermatozoa enzyme, expression in Escherichia coli as glutathione-S-transferase fusion protein
-
the baculovirus expression vector system, using the Autographa californica nucleopolyhedrovirus and the Sf9 insect cell line, is used to produce recombinant Bi-PHGPx proteins, the cDNA fragment containing the full-length open reading frame is inserted into the transfer vector pBAC1
the codon optimized gene is cloned into the vector pGex4T-1 for expression in Escherichia coli BL21DE3 cells
-
the entire encoding region for Oryza sativa PHGPx is expressed in Escherichia coli M15
-
the open reading frame of Hyr1/YIR037W is cloned into a pET28a-derived vector for expression in Escherichia coli Rosetta DE3 cells
-
the triple deletion mutant gpx1delta/gpx2delta/gpx3delta is not growing with medium containing unsaturated linolenate; wild-type enzyme gpx1, gpx2, gpx3 and mutants, expression in Escherichia coli
-
transgenic mice overexpressing human GPx4 are generated
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
10 mg/l Cd2+ down-regulates gpx4b in liver and olfactory lobe tissues; in the liver of the carp exposed to 7°C temperature drop, the gpx4a gene is down-regulated as early as 1 h after cold shock to 75%
-
Bi-PHGPx transcripts are up-regulated by stresses, such as wounding, H2O2 exposure, external temperature shock, and starvation
expression in rice seedlings can be markedly induced by H2O2 and NaCl
-
in liver direct exposure to low temperature increases the transcription of gpx4b by 2.5fold
-
PHGPx expression is up-regulated in spermatozoa by unknown mechanisms
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
C82S
-
in the presence of thioredixin system, wild-type Hyr1 can consume H2O2 rapidly, while the C82S mutant totally abolish the activity, indicating the important role of Cys82 in Trx2 specifity
Sec43Cys
-
mutation of the selenium cysteine in the active site
Sec43Ser
-
mutation of the selenium cysteine in the active site
additional information
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
additional information