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
1.11.1.12
-
RECOMMENDED NAME
GeneOntology No.
phospholipid-hydroperoxide glutathione peroxidase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 glutathione + a hydroperoxy-fatty-acyl-[lipid] = glutathione disulfide + a hydroxy-fatty-acyl-[lipid] + H2O
show the reaction diagram
a protein containing a selenocysteine residue. The products of EC 1.13.11.12 on phospholipids can act as acceptor, H2O2 can also act, but much more slowly. The product of EC 1.13.11.12 lipoxygenase on phospholipids can act as acceptor; H2O2 can also act, but much more slowly (cf. EC1.11.1.9 glutathione peroxidase)
-
-
-
2 glutathione + a hydroperoxy-fatty-acyl-[lipid] = glutathione disulfide + a hydroxy-fatty-acyl-[lipid] + H2O
show the reaction diagram
tert-uni ping-pong mechanism
-
2 glutathione + a hydroperoxy-fatty-acyl-[lipid] = glutathione disulfide + a hydroxy-fatty-acyl-[lipid] + H2O
show the reaction diagram
ping-pong mechanism
-
2 glutathione + a hydroperoxy-fatty-acyl-[lipid] = glutathione disulfide + a hydroxy-fatty-acyl-[lipid] + H2O
show the reaction diagram
ping-pong mechanism with formation of ternary complexes
-
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
LITERATURE
oxidation
-
-
-
-
oxidation
-
-
oxidation
animal
-
-
oxidation
-
-
oxidation
-
-
oxidation
-
-
oxidation
-
-
oxidation
-
-
oxidation
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
reduction
-
GPx4 can catalyze the GSH-dependent two-electron reduction of various phospholipid-, cholesterol-, and cholesteryl ester-derived hydroperoxides in solubilized as well as membrane- or lipoprotein-bound form
reduction
-
GSH-dependent peroxidase activity with the largest affinity to and the highest catalytic efficiency on phosphatidylcholine hydroperoxide
reduction
-
-
reduction
animal
-
-
reduction
-
-
reduction
-
-
reduction
-
-
reduction
-
-
reduction
-
-
reduction
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
glutathione redox reactions I
-
-
Glutathione metabolism
-
-
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 acceptor; H2O2 can also act, but much more slowly (cf. EC 1.11.1.9 glutathione peroxidase).
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
class 4 GPx
-
-
glutathione peroxidase 4
-
-
glutathione peroxidase-4
-
-
glutathione-dependent phospholipid peroxidase
-
-
GPx-4
-
-
GPx4
-
-
GPx41
mitochondrial form
hydroperoxide glutathione peroxidase
-
-
-
-
Hyr1/YIR037W
-
-
non-selenocysteine PHGPx
-
-
NPGPx
-
-
nPHGPx
-
-
peroxidation-inhibiting protein
-
-
-
-
peroxidation-inhibiting protein: peroxidase, glutathione (phospholipid hydroperoxide-reducing)
-
-
-
-
PHGPX
-
-
-
-
PHGPX
animal
-
-
PHGPX
-
-
PHGPX
-
-
phospholipid glutathione peroxidase
-
-
phospholipid hydroperoxide glutathione peroxidase
-
-
-
-
phospholipid hydroperoxide glutathione peroxidase
animal
-
-
phospholipid hydroperoxide glutathione peroxidase
-
-
phospholipid hydroperoxide glutathione peroxidase
-
-
phospholipid hydroperoxide glutathione peroxidase
-
phospholipid hydroperoxide glutathione peroxidase
-
phospholipid hydroperoxide glutathione peroxidase
-
-
phospholipid hydroperoxide glutathione peroxidase
-
-
phospholipid hydroperoxide glutathione peroxidase
-
-
phospholipid hydroperoxide glutathione peroxidase
-
-
phospholipid hydroperoxide glutathione peroxidase
-
phospholipid hydroperoxide glutathione peroxidase
-
-
phospholipid hydroperoxide glutathione peroxidase
-
phospholipid hydroperoxide glutathione peroxidase A
-
-
phospholipid hydroperoxide glutathione peroxidase B
-
-
phospholipid hydroperoxide glutathione peroxidase-4
-
phospholipid-hydroperoxide glutathione peroxidase
-
phospholipid-hydroperoxide glutathione peroxidases
-
-
selenium-dependent glutathione peroxidase type-4
-
-
seleno GPx
-
-
selenoperoxidase
-
-
selenoprotein P
-
-
sperm nucleus-specific glutathione peroxidase
-
-
type-4 glutathione peroxidase
-
-
additional information
-
salt-sensitive cell line is inducible by abscisic acid and 10fold by NaCl 0.2 M, salt-tolerant cell line is not
CAS REGISTRY NUMBER
COMMENTARY
97089-70-8
-
ORGANISM
COMMENTARY
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
bull, three Italian beef breeds, Chianina, Marchigiana, Romagnola
-
-
Manually annotated by BRENDA team
Shamouti orange, encoding gene csa
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
mitochondrial enzyme
TrEMBL
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
male
-
-
Manually annotated by BRENDA team
transgenic mice in which PHGPx is overexpressed solely in the mitochondrion
SwissProt
Manually annotated by BRENDA team
genes GPX1, GPX2 and GPX3
-
-
Manually annotated by BRENDA team
blood fluke, parasite platyhelminth
-
-
Manually annotated by BRENDA team
American trypanosome
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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 + a lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
-
-
?
glutathione + a lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
-
-
?
glutathione + a lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
-
-
?
glutathione + a lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
-
-
?
glutathione + a lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
-
-
?
glutathione + a lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
animal
-
-
-
?
glutathione + a lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
-
?
glutathione + a lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
-
?
glutathione + cardiolipin
?
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 + cholesterol hydroperoxides
?
show the reaction diagram
-
-
-
-
?
glutathione + cholesterol hydroperoxides
?
show the reaction diagram
-
-
-
-
?
glutathione + cumene hydroperoxide
?
show the reaction diagram
-
-
-
-
?
glutathione + cumene hydroperoxide
?
show the reaction diagram
-
-
-
-
?
glutathione + cumene hydroperoxide
?
show the reaction diagram
-
-
-
-
?
glutathione + cumene hydroperoxide
?
show the reaction diagram
-
-
-
-
?
glutathione + cumene hydroperoxide
?
show the reaction diagram
-
-
-
-
?
glutathione + cumene hydroperoxide
?
show the reaction diagram
-
no activity
-
-
-
glutathione + dilinoleoyl phosphatidylcholine hydroperoxide
?
show the reaction diagram
-
-
-
-
?
glutathione + dilinoleoyl phosphatidylcholine hydroperoxide
?
show the reaction diagram
-
and derivatives of dilinoyl phosphatidylcholine hydroperoxide
-
-
?
glutathione + fatty acid hydroperoxides
?
show the reaction diagram
-
-
-
-
?
glutathione + H2O2
?
show the reaction diagram
-
-
-
-
?
glutathione + H2O2
?
show the reaction diagram
-
-
-
-
?
glutathione + H2O2
?
show the reaction diagram
-
-
-
-
?
glutathione + H2O2
?
show the reaction diagram
-
-
-
-
?
glutathione + H2O2
?
show the reaction diagram
-
-
-
-
?
glutathione + H2O2
?
show the reaction diagram
-
-
-
-
?
glutathione + H2O2
?
show the reaction diagram
-
-
-
-
?
glutathione + H2O2
?
show the reaction diagram
-
-
-
-
?
glutathione + H2O2
?
show the reaction diagram
-
-
-
?
glutathione + H2O2
?
show the reaction diagram
-
protein follows a ping–pong mechanism, which is similar to that of native cytosolic glutathione peroxidase, EC 1.11.1.9
-
?
glutathione + H2O2
?
show the reaction diagram
-
no activity
-
-
-
glutathione + H2O2
?
show the reaction diagram
-
no activity
-
-
-
glutathione + H2O2
?
show the reaction diagram
-
activity assay
-
-
?
glutathione + H2O2
?
show the reaction diagram
activity assay
-
-
?
glutathione + L-alpha-phosphatidylcholine hydroperoxide
?
show the reaction diagram
-
-
-
-
?
glutathione + L-alpha-phosphatidylcholine hydroperoxide
?
show the reaction diagram
-
-
-
-
?
glutathione + L-alpha-phosphatidylcholine hydroperoxide
?
show the reaction diagram
-
-
-
-
?
glutathione + L-alpha-phosphatidylcholine hydroperoxide
?
show the reaction diagram
-
-
-
?
glutathione + L-alpha-phosphatidylcholine hydroperoxide
?
show the reaction diagram
-
-
-
-
?
glutathione + L-alpha-phosphatidylcholine hydroperoxide
?
show the reaction diagram
-
-
-
-
?
glutathione + L-alpha-phosphatidylcholine hydroperoxide
?
show the reaction diagram
L-alpha-phosphatidylcholine hydroperoxide is a specific substrate of GPx4
-
-
?
glutathione + LDL hydroperoxides
?
show the reaction diagram
-
-
-
-
?
glutathione + linoleic acid hydroperoxide
?
show the reaction diagram
-
-
-
-
?
glutathione + linoleic acid 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 + lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
-
-
?
glutathione + lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
-
-
?
glutathione + lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
-
-
?
glutathione + lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
-
-
?
glutathione + lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
-
-
?
glutathione + lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
-
-
?
glutathione + lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
-
-
?
glutathione + lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
-
-
?
glutathione + lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
-
-
-
glutathione + lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
-
-
?
glutathione + lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
-
-
?
glutathione + lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
-
-
?
glutathione + lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
-
-
ir
glutathione + lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
-
-
?
glutathione + lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
-
-
?
glutathione + lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
-
-
?
glutathione + lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
-
-
?
glutathione + lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
-
-
?
glutathione + lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
-
-
?
glutathione + lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
-
-
?
glutathione + lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
-
?
glutathione + lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
dithiothreitol, 2-mercaptoethanol, cysteine and homocysteine also serve as reducing agents
-
?
glutathione + lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
reduces hydroperoxides of phosphatidylcholine and cholesteryllinolate alone or associated to oxidized LDL and oxidized HDL
-
?
glutathione + lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
wide specificity for lipid hydroperoxides
-
?
glutathione + lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
dithiothreitol and dithioerythritol are 3fold more active than glutathione, while 2-mercaptoethanol and L-cysteine show 50% and 20% of the activity with glutathione as reductants, respectively
-
?
glutathione + lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
the oxidized active site of the enzyme can also be reduced by mercaptoethanol
-
?
glutathione + lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
protection of biomembranes against oxidative damage
-
?
glutathione + lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
protection of biomembranes against oxidative damage
-
?
glutathione + lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
protection of biomembranes against oxidative damage
-
?
glutathione + lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
protection of biomembranes against oxidative damage
-
?
glutathione + lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
protection of biomembranes against oxidative damage
-
?
glutathione + lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
protection of biomembranes against oxidative damage
-
?
glutathione + lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
enzyme reduces amphiphilic peroxides, possibly at the water-lipid interface
-
?
glutathione + lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
role in cellular detoxification of a wide variety of lipid hydroperoxides in membranes and internalized lipoproteins
-
?
glutathione + phosphatidic acid hydroperoxide
?
show the reaction diagram
-
-
-
-
?
glutathione + phosphatidylcholine hydroperoxide
?
show the reaction diagram
-
-
-
-
?
glutathione + phosphatidylcholine hydroperoxide
?
show the reaction diagram
-
-
-
?
glutathione + phosphatidylcholine hydroperoxide
?
show the reaction diagram
-
activity assay
-
-
?
glutathione + phosphatidylcholine hydroperoxide
?
show the reaction diagram
-
activity assay
-
-
?
glutathione + phosphatidylcholine hydroperoxide
?
show the reaction diagram
activity assay
-
-
?
glutathione + phosphatidylethanolamine hydroperoxide
?
show the reaction diagram
-
-
-
-
?
glutathione + phosphatidylserine hydroperoxide
?
show the reaction diagram
-
-
-
-
?
glutathione + phospholipid hydroperoxides
?
show the reaction diagram
-
-
-
-
?
glutathione + phospholipid hydroperoxides
?
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-butyl hydroperoxide
?
show the reaction diagram
-
-
-
-
?
glutathione + tert-butyl hydroperoxide
?
show the reaction diagram
-
-
-
-
?
glutathione + tert-butyl hydroperoxide
?
show the reaction diagram
-
-
-
-
?
glutathione + tert-butyl hydroperoxide
?
show the reaction diagram
-
-
-
-
?
glutathione + tert-butyl hydroperoxide
?
show the reaction diagram
-
no activity
-
-
-
glutathione + tert-butyl-hydroperoxide
?
show the reaction diagram
-
-
-
?
glutathione + tert-butyl-hydroperoxide
?
show the reaction diagram
-
activity assay
-
-
?
glutathione + tert-butylhydroperoxide
?
show the reaction diagram
-
-
-
-
?
GSH + cumene hydroperoxide
GSSG + ?
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
-
-
-
?
GSH + tert-butyl hydroperoxide
GSSG + ?
show the reaction diagram
-
about 80% of the activity with cumene hydroperoxide
-
?
KKSQCCQQKT + H2O2
KKSQ-L-cystinyl-QQKT + 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
-
-
-
-
?
KPPCCPPK + H2O2
KPP-L-cystinyl-PPK + 2 H2O
show the reaction diagram
-
-
?
additional information
?
-
-
reduces hydroxyperoxide derivatives of phospholipids into alcohol derivatives
-
-
-
additional information
?
-
-
enzyme inhibits lipid peroxidation, which is induced by Fe3+-triethylenetetramine complex, NADPH and ascorbate in presence of glutathione, therefore a physiological amount of alpha-tocopherol, vitamin E, is necessary in the membranes
-
-
-
additional information
?
-
-
enzyme inhibits lipid peroxidation, which is induced by Fe3+-triethylenetetramine complex, NADPH and ascorbate in presence of glutathione, therefore a physiological amount of alpha-tocopherol, vitamin E, is necessary in the membranes
-
-
-
additional information
?
-
-
enzyme inhibits lipid peroxidation, which is induced by Fe3+-triethylenetetramine complex, NADPH and ascorbate in presence of glutathione, therefore a physiological amount of alpha-tocopherol, vitamin E, is necessary in the membranes
-
-
-
additional information
?
-
-
enzyme inhibits lipid peroxidation, which is induced by Fe3+-triethylenetetramine complex, NADPH and ascorbate in presence of glutathione, therefore a physiological amount of alpha-tocopherol, vitamin E, is necessary in the membranes
-
-
-
additional information
?
-
-
phospholipid hydroperoxide glutathione peroxidase and 15-lipoxygenase are counterparts in the metabolism of hydroperoxy lipids
-
-
-
additional information
?
-
-
mitochondrial enzyme inhibits the release of cytochrome c from mitochondria by suppressing the peroxidation of cardiolipin in hypoglycaemia-induced apoptosis
-
-
-
additional information
?
-
-
controlled by gonadotropin
-
-
-
additional information
?
-
-
enzyme inhibits peroxidation of microsomes
-
-
-
additional information
?
-
-
in addition to a structural role, PHGPx may also be involved in the non-enzymatic protection of sperm surface against detrimental effects caused by accumulation of modified lipids
-
-
-
additional information
?
-
-
the enzyme appears to be indispensable for structural integrity of spermatozoa and to codetermine sperm motility and viability
-
-
-
additional information
?
-
-
the enzyme is not enzymatically active but may be able to interact with modified phospholipids on the membrane, thereby masking or removing potentially damaging lipids from the surface of the parasitpoid‘s eggs
-
-
-
additional information
?
-
-
the enzyme plays an essential role in breast cancer cells in alleviating oxidative stress generated from polyunsaturated fatty acid metabolism
-
-
-
additional information
?
-
-
tyrosine phosphorylation of the enzyme may represent an important event in the signaling cascade associated with capacitation that may impact the regulation of hyperactivation of sperm motility and/or mitochondrial function
-
-
-
additional information
?
-
-
the enzyme shows phospholipid hydroperoxide glutathione peroxidase activity and thioredoxin peroxidase activity. Thioredoxin peroxidase activity is higher than phospholipid hydroperoxidase activity in terms of efficiency and substrate affinities. No activity with glutathione + H2O2
-
-
-
additional information
?
-
-
PhGPx prevents NF-kappaB activation, oxLDL-induced proliferation and linoleic acid-induced apoptosis
-
-
-
additional information
?
-
-
PHGPx-/- mice are embryonically lethal at gestation day 7.5. PHGPx+/- mice cells show decreased life span after exposure to irradiation and increased susceptibility to oxidative and genotoxic stress
-
-
-
additional information
?
-
-
GPx4 can react with H2O2 and a wide range of lipid hydroperoxides including oxidized phospholipids and cholesterol hydroperoxides
-
-
-
additional information
?
-
PHGPx is an antioxidant enzyme that can reduce peroxidized phospholipids produced in cell membranes
-
-
-
additional information
?
-
-
preferred substrates are found to be hydroperoxide groups of phosphatidylcholine and on cumene and t-butyl hydroperoxides
-
-
-
additional information
?
-
-
reduces lipid hydroperoxides in biomembranes
-
-
-
additional information
?
-
-
specifically detoxifies phospholipid peroxide
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
glutathione + a lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
-
-
?
glutathione + a lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
-
-
?
glutathione + a lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
-
-
?
glutathione + a lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
-
-
?
glutathione + a lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
-
-
?
glutathione + a lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
-
-
?
glutathione + a lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
animal
-
-
-
?
glutathione + a lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
C3VVL8
-
-
?
glutathione + a lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
Q8W259
-
-
?
glutathione + lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
-
-
?
glutathione + lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
-
-
?
glutathione + lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
-
-
?
glutathione + lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
-
-
?
glutathione + lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
protection of biomembranes against oxidative damage
-
?
glutathione + lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
protection of biomembranes against oxidative damage
-
?
glutathione + lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
protection of biomembranes against oxidative damage
-
?
glutathione + lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
protection of biomembranes against oxidative damage
-
?
glutathione + lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
protection of biomembranes against oxidative damage
-
?
glutathione + lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
protection of biomembranes against oxidative damage
-
?
glutathione + lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
enzyme reduces amphiphilic peroxides, possibly at the water-lipid interface
-
?
glutathione + lipid hydroperoxide
glutathione disulfide + lipid + H2O
show the reaction diagram
-
role in cellular detoxification of a wide variety of lipid hydroperoxides in membranes and internalized lipoproteins
-
?
additional information
?
-
-
enzyme inhibits lipid peroxidation, which is induced by Fe3+-triethylenetetramine complex, NADPH and ascorbate in presence of glutathione, therefore a physiological amount of alpha-tocopherol, vitamin E, is necessary in the membranes
-
-
-
additional information
?
-
-
enzyme inhibits lipid peroxidation, which is induced by Fe3+-triethylenetetramine complex, NADPH and ascorbate in presence of glutathione, therefore a physiological amount of alpha-tocopherol, vitamin E, is necessary in the membranes
-
-
-
additional information
?
-
-
enzyme inhibits lipid peroxidation, which is induced by Fe3+-triethylenetetramine complex, NADPH and ascorbate in presence of glutathione, therefore a physiological amount of alpha-tocopherol, vitamin E, is necessary in the membranes
-
-
-
additional information
?
-
-
enzyme inhibits lipid peroxidation, which is induced by Fe3+-triethylenetetramine complex, NADPH and ascorbate in presence of glutathione, therefore a physiological amount of alpha-tocopherol, vitamin E, is necessary in the membranes
-
-
-
additional information
?
-
-
phospholipid hydroperoxide glutathione peroxidase and 15-lipoxygenase are counterparts in the metabolism of hydroperoxy lipids
-
-
-
additional information
?
-
-
mitochondrial enzyme inhibits the release of cytochrome c from mitochondria by suppressing the peroxidation of cardiolipin in hypoglycaemia-induced apoptosis
-
-
-
additional information
?
-
-
controlled by gonadotropin
-
-
-
additional information
?
-
-
enzyme inhibits peroxidation of microsomes
-
-
-
additional information
?
-
-
in addition to a structural role, PHGPx may also be involved in the non-enzymatic protection of sperm surface against detrimental effects caused by accumulation of modified lipids
-
-
-
additional information
?
-
-
the enzyme appears to be indispensable for structural integrity of spermatozoa and to codetermine sperm motility and viability
-
-
-
additional information
?
-
-
the enzyme is not enzymatically active but may be able to interact with modified phospholipids on the membrane, thereby masking or removing potentially damaging lipids from the surface of the parasitpoid‘s eggs
-
-
-
additional information
?
-
-
the enzyme plays an essential role in breast cancer cells in alleviating oxidative stress generated from polyunsaturated fatty acid metabolism
-
-
-
additional information
?
-
-
tyrosine phosphorylation of the enzyme may represent an important event in the signaling cascade associated with capacitation that may impact the regulation of hyperactivation of sperm motility and/or mitochondrial function
-
-
-
additional information
?
-
-
PhGPx prevents NF-kappaB activation, oxLDL-induced proliferation and linoleic acid-induced apoptosis
-
-
-
additional information
?
-
-
PHGPx-/- mice are embryonically lethal at gestation day 7.5. PHGPx+/- mice cells show decreased life span after exposure to irradiation and increased susceptibility to oxidative and genotoxic stress
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
glutathione
-
-
glutathione
-
-
glutathione
animal
-
-
glutathione
-
glutathione
-
-
glutathione
-
-
glutathione
-
-
glutathione
-
-
glutathione
-
-
glutathione
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Se
-
1 g-atom Se per mol protein; Se in selenol form
Se
-
enzyme contains a selenocysteine residue at the active site
Se
-
10 selenocysteines per protein molecule
Se
-
enzyme contains a selenocysteine residue at the active site
Se
TGA-encoded selenocysteine at residue 46 and active site residues Gln82 and Trp135 that interact with the selenocysteine
selenium
-
selenoprotein
selenium
-
selenoprotein
selenium
-
-
selenium
-
-
selenium
-
-
selenium
-
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
alpha-tocopherol
-
complete inhibition of glutathione oxidation
deoxycholate
-
-
deoxycholate
-
in reaction with cumene hydroperoxide and linoleic acid hydroperoxide
iodoacetate
-
-
iodoacetate
-
-
iodoacetate
-
2 mM, complete inhibition
Mercaptosuccinate
-
0.1 mM
unsaturated fatty acids
-
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
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
-
-
NaCl
-
-
selenoprotein P
-
2 nM, 3fold stimulation of activity after 24h
-
Sodium selenite
-
100 nM, 3fold stimulation of activity after 24h
Triton X-100
-
-
Triton X-100
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00014
1-palmitoyl-2-(13-hydroperoxy-cis-9,trans-11-octadecadienoyl)-L-3-phosphatidylcholine
-
cosubstrate: glutathione
0.0362
1-palmitoyl-2-(13-hydroperoxy-cis-9,trans-11-octadecadienoyl)-L-3-phosphatidylcholine
-
cosubstrate: thioredoxin
0.0017
cumene hydroperoxide
-
recombinant enzyme
0.119
cumene hydroperoxide
-
-
608
cumene hydroperoxide
-
-
1.37
glutathione
-
-
0.0008656
H2O2
apparent KM
0.6383
H2O2
apparent KM
0.799
H2O2
-
cosubstrate: glutathione
0.00074
L-alpha-phosphatidylcholine hydroperoxide
-
recombinant enzyme
-
0.00058
linoleic acid hydroperoxide
-
recombinant enzyme
-
0.0393
linoleic acid hydroperoxide
-
-
-
0.0827
linoleic acid hydroperoxide
-
-
-
0.0121
phosphatidylcholine dilinoleoyl hydroperoxide
-
-
-
0.0249
phosphatidylcholine dilinoleoyl hydroperoxide
-
-
-
0.0002353
phosphatidylcholine hydroperoxide
apparent KM
0.01113
phosphatidylcholine hydroperoxide
apparent KM
0.011
phospholipid hydroperoxide
-
-
-
0.0056
tert-butyl hydroperoxide
-
recombinant enzyme
0.0953
tert-butyl hydroperoxide
-
-
0.128
tert-butyl hydroperoxide
-
-
4.344
tert-butyl hydroperoxide
-
cosubstrate: glutathione
2.932
tert-butyl-hydroperoxide
apparent KM
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
91
(beta-(13-hydroperoxy-cis-9,trans-11-octadecadienoyl)-gamma-palmitoyl)-L-alpha-phosphatidylcholine
Homo sapiens
-
-
additional information
additional information
Homo sapiens
-
mutant compared to wild-type enzyme
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.019
alpha-tocopherol
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0038
-
crude platelet homogenate
0.0048
-
cytosolic fraction
0.006
-
mitochondrial fraction
0.009
-
-
0.0096
-
membrane fraction
0.04
-
low-PHGPx group
0.051
-
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
-
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
-
activity distribution in rat tissues
additional information
-
activity is age-dependent
additional information
-
mutant compared to wild-type enzyme
additional information
-
specific activity of cytosolic and mitochondrial enzymes with several hydroperoxide substrates and reducing agents
additional information
-
reduction of hydroperoxides of phosphatidylcholine and cholesteryllinolate associated to oxidized LDL and oxidized HDL
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
-
assay at
7.4
-
assay at
7.4
-
activity assay
7.4
-
activity assay
7.5
-
assay at
7.5
activity assay
7.5
-
activity assay
7.6
-
assay at
7.6
-
assay at
8
-
assay at
8
-
activity assay
9
activity assay
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8 - 11
-
pH 8.0: about 40% of maximal activity, pH 11: about 80% of maximal activity
8 - 9.5
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
23
activity assay at room temperature, ferrithiocyanate assay
23
-
activity assay at room temperature
25
-
activity assay
37
-
assay at
37
-
assay at
37
-
assay at
40
activity assay
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 40
-
10°C: 80% of maximal activity, 40°C: 60% of maximal activity
10 - 45
-
-
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
-
isoelectric focusing electrophoresis
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
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
-
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
-
white matter
Manually annotated by BRENDA team
extraction of genomic DNA
Manually annotated by BRENDA team
-
keratinized surface epithelium
Manually annotated by BRENDA team
-
parenchym
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 90% decrease in GPx-4 level
Manually annotated by BRENDA team
-
Paneth cells
Manually annotated by BRENDA team
-
; tubular epithelium
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
-
parenchym
Manually annotated by BRENDA team
-
parenchym
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
-
exocrine portion
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
-
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
-
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
-
mitochondrial capsule
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
-
epididymal, hormone regulated appearance
Manually annotated by BRENDA team
-
activity does not differ between normo- and hypomotile human sperm samples
Manually annotated by BRENDA team
-
hormone regulated appearance
Manually annotated by BRENDA team
-
strongly linked to mitochondria of cells undergoing differentiation to spermatozoa, under gonadotropin control
Manually annotated by BRENDA team
-
PHGPx mRNA is highly expressed in spermiogenic cells and Leydig cell
Manually annotated by BRENDA team
-
treatment with testosterone slightly decreases PHGPx mRNA levels in testes by the reverse transcription-polymerase chain reaction. Anti-androgenic compounds (flutamide, ketoconazole, and diethylhexyl phthalate) and estrogenic compounds (nonylphenol, octylphenol, and diethylstilbestrol) significantly upregulate PHGPx mRNA in the testes. Endocrine disrupting chemicals might have a detrimental effect on spermatogenesis via abnormal enhancement of PHGPx expression in testes
Manually annotated by BRENDA team
-
parafollicular cells and follicular basement membrane
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
only in testicle
Manually annotated by BRENDA team
-
L-form of the enzyme
Manually annotated by BRENDA team
; transgenic mice in which PHGPx is overexpressed solely in the mitochondrion. Mitochondria-specific GPx4 overexpression protects cardiac contractile function and preserves electron transport chain complex activities following ischemia/reperfusion
Manually annotated by BRENDA team
-
only in testicle
Manually annotated by BRENDA team
-
high-salt extract from retina
-
Manually annotated by BRENDA team
additional information
-
interfacial character of the enzyme
-
Manually annotated by BRENDA team
additional information
-
extracellular localisation
-
Manually annotated by BRENDA team
additional information
not detected in the nucleus
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6000
-
below, retina enzyme, gel filtration
394876
16100
-
gel filtration
394878
18000
His6-tagged fusion protein, determined by SDS-PAGE
698037
18300
-
recombinant enzyme, glutathione-S-transferase-tag cut off, SDS-PAGE
394877
18500
-
cytosolic enzyme form, SDS-PAGE
676554
19000
determined by SDS-PAGE
697468
19400
-
determined by gel filtration
701138
20000
-
gel filtration
394868
20000
-
gel filtration
394882
20000
-
mitochondrial and cytosolic enzyme form, SDS-PAGE
673176
20000
-
-
696435
20000
-
SDS-PAGE
701060
21000
-
20 to 22 kDa
698045
21480
calculated from sequence of cDNA
673837
21500
-
mitochondrial enzyme form, SDS-PAGE
676554
22000
-
gel filtration
394880
22500
His6-McPHGPx fusion protein, determined by SDS-PAGE
696173
23000
-
gel filtration
394864
34000
-
nucleic enzyme form, SDS-PAGE
673176
69000
-
native PAGE
394873
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 20000, cytosolic enzyme form, SDS-PAGE; x * 25900, truncated form of nuclear enzyme, lacking the basic nuclear localization signal, SDS-PAGE
?
-
x * 21000, recombinant enzyme containing a six-histidine tag at its N-terminus, SDS-PAGE
?
x * 21000, SDS-PAGE
monomer
-
1 * 20000, SDS-PAGE; 1 * 23000, SDS-PAGE
monomer
-
1 * 20000, SDS-PAGE
monomer
-
1 * 66000, SDS-PAGE
monomer
-
1 * 6000, about, retina enzyme, SDS-PAGE
monomer
-
1 * 18300-20000, recombinant and wild-type, SDS-PAGE
monomer
-
1 * 22000, SDS-PAGE
monomer
-
1 * 20000, SDS-PAGE
monomer
-
1 * 20000, non-mitochondrial S-form of the enzyme; 1 * 23000, mitochondrial L-form of the enzyme
monomer
-
-
monomer
-
-
monomer
-
-
additional information
-
cytosolic enzyme shows also a minor component in SDS-PAGE at higher molecular weight, which is not further characterized
additional information
like the wild-type enzyme, the U46C mutant exhibits a strong tendency toward protein polymerization, which was prevented by reductants
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
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
LITERATURE
40
thermal stability shows that the activity is significantly decreased when the temperature is higher than 40°C
697468
65
-
complete loss of activity after 5 min
394868
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
394872
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
presence of thiol, e.g. 2-mercaptoethanol, during purification is necessary for stabilization
-
alpha-tocopherol stabilizes triple mutant against H2O2 and unsaturated linolenate
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
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
-40°C, about 30% loss of activity during 1 freeze-thaw-cycle
-
4°C, loss of 10% activity in 1 week
-
-20°C, 10% glycerol, stable for several months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
using a HisTrap column
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
by nickel affinity chromatography
recombinant enzyme
-
Percoll step gradient and nickel affinity chromatography
-
ammonium sulfate precipitation, DEAE-Sepharose column chromatography, Sephadex G-50 gel filtration, and HiTrap SP column chromatography
-
from cytosol and mitochondria
-
partially from testis and to homogenity from sperm as recombinant enzyme expressed in Escherichia coli and as wild-type enzyme
-
on a Ni-NTA column, further purified by gel filtration
-
wild-type and mutant proteins
-
Sec43Cys is purified on a GSH-Sepharose column, Sec43Ser is purified by ionic exchange chromatography, the GST-tags are cleaved with bovine thrombin
-
by Ni2+-nitrilotriacetic acid Sepharose
recombinant enzyme from Escherichia coli
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
expression in Escherichia coli; expression in Escherichia coli; expression in Escherichia coli; expression in Escherichia coli
for sequencing
-
expression in Escherichia coli
-
expressed in MIA PaCa-2 and AsPC-1 human pancreatic cancer cells
-
expressed in tumor cell transfectant clone 7G4
-
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
-
expresssion in HEK-293T cell
transgenic mice overexpressing human GPx4 are generated
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into the vector pET-28a+ for expression in Escherichia coli BL21DE3 cells, into the vector YEpGAP112 for a functional complementation test in yeast
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
expression in Escherichia coli
-
the entire encoding region for Oryza sativa PHGPx is expressed in Escherichia coli M15
-
expressed in Escherichia coli
-
expression vector encoding mitochondrial enzyme for overexpression in (RBL)2H3 cell line
-
spermatozoa enzyme, expression in Escherichia coli as glutathione-S-transferase fusion protein
-
the open reading frame of Hyr1/YIR037W is cloned into a pET28a-derived vector for expression in Escherichia coli Rosetta DE3 cells
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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
-
the codon optimized gene is cloned into the vector pGex4T-1 for expression in Escherichia coli BL21DE3 cells
-
expression in Escherichia coli
-
into the vector pYEX-S1 for transformation into Saccharomyces cerevisiae cells
His-tagged protein termed TcGPX1, expression in Escherichia coli
-
expression in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
Bi-PHGPx transcripts are up-regulated by stresses, such as wounding, H2O2 exposure, external temperature shock, and starvation
PHGPx expression is up-regulated in spermatozoa by unknown mechanisms
-
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%
-
in liver direct exposure to low temperature increases the transcription of gpx4b by 2.5fold
-
expression in rice seedlings can be markedly induced by H2O2 and NaCl
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Sec43Cys
-
mutation of the selenium cysteine in the active site
Sec43Ser
-
mutation of the selenium cysteine in the active site
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
-
(RBL)2H3 cell line stably overexpressing mitochondrial phospholipid hydroperoxide glutathione peroxidase from transfected expression plasmid
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
additional information
-
deletion mutants of gpx1delta, gpx2delta and gpx3delta showing diminished enzyme activity, triple mutant gpx1delta/gpx2delta/gpx3delta has almost no remaining activity
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
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
-
tumor growth inhibitor
medicine
-
PHGPx downregulation could be related with a poorer prognosis in breast invasive ductal carcinoma
medicine
-
overexpression of GPx4 inhibits the development of atherosclerosis by decreasing lipid peroxidation and inhibiting the sensitivity of vascular cells to oxidized lipids
medicine
-
MPHGPx transgenic mice made diabetic by multiple low-dose streptozotocin injections show decreased ejection fraction and fractional shortening in diabetic hearts that is reversed with hydroperoxide glutathione peroxidase mPHDPx4 overexpression. MPHGPx overexpression increases electron transport chain function while attenuating hydrogen peroxide production and lipid peroxidation in diabetic mPHGPx interfibrillar mitochondria. mPHGPx overexpression lessens proteomic loss observed in diabetic interfibrillar mitochondria. Posttranslational modifications, including oxidations and deamidations, are attenuated with mPHGPx overexpression. Mitochondrial protein import dysfunction in diabetic interfibrillar mitochondria is reversed with mPHGPx overexpression correlating with protein import constituent preservation. Oxidative phosphorylation, tricarboxylic acid cycle, and fatty acid oxidation processes most influenced in diabetic interfibrillar mitochondria are preserved by mPHGPx overexpression
medicine
-
PHGPx is useful as a biomarker to screen for detrimental effects of exogenous endocrine disrupting chemicals in testes
additional information
animal
-
comparative analysis of invertebrate GPx genes provides information evidence to support the modular pathways of GPx evolution, which have been accompanied with sporadic expansion-deletion and exon-intron remodeling, the study would be beneficial to get detailed insights into the complex GPx evolution, and to understand the molecular basis of the specialized physiological implications of the antioxidant system in their respective organisms
additional information
-
an assay for sperm PHGPx activity emerges as a unique tool to evaluate semen quality for sire selection