Information on EC 1.11.1.9 - glutathione peroxidase

New: Word Map on EC 1.11.1.9
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
1.11.1.9
-
RECOMMENDED NAME
GeneOntology No.
glutathione peroxidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 glutathione + H2O2 = glutathione disulfide + 2 H2O
show the reaction diagram
mechanism
-
2 glutathione + H2O2 = glutathione disulfide + 2 H2O
show the reaction diagram
2 GSH + ROOH = ROH + H2O + GSSG
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Arachidonic acid metabolism
-
-
arachidonic acid metabolism
-
-
Glutathione metabolism
-
-
glutathione redox reactions I
-
-
reactive oxygen species degradation
-
-
SYSTEMATIC NAME
IUBMB Comments
glutathione:hydrogen-peroxide oxidoreductase
A protein containing a selenocysteine residue. Steroid and lipid hydroperoxides, but not the product of reaction of EC 1.13.11.12 lipoxygenase on phospholipids, can act as acceptor, but more slowly than H2O2 (cf. EC 1.11.1.12 phospholipid-hydroperoxide glutathione peroxidase).
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6P229
-
-
-
-
ARMEP24
-
-
-
-
AtGPX1
-
-
-
-
Cellular glutathione peroxidase
-
-
-
-
Cuticular glycoprotein GP29
-
-
-
-
DI29
-
-
-
-
EGLP
-
-
-
-
Epididymis-specific glutathione peroxidase-like protein
-
-
-
-
Extracellular glutathione peroxidase
-
-
-
-
Gastrointestinal glutathione peroxidase
-
-
-
-
GP30
-
-
-
-
GPRP
-
-
-
-
GPX
-
-
-
-
GSH peroxidase
-
-
-
-
GSHPx-GI
-
-
-
-
Major androgen-regulated protein
-
-
-
-
Major surface antigen GP29
-
-
-
-
Nt-SubC08
-
-
-
-
Odorant-metabolizing protein RY2D1
-
-
-
-
peroxidase, glutathione
-
-
-
-
reduced glutathione peroxidase
-
-
-
-
Salt-associated protein
-
-
-
-
selenium-glutathione peroxidase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9013-66-5
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Aloa barbadensis Miller
-
-
Manually annotated by BRENDA team
ecotype Columbia
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
breed Holstein-Friesian
-
-
Manually annotated by BRENDA team
isozyme GPx-1
UniProt
Manually annotated by BRENDA team
zebra-seabream
-
-
Manually annotated by BRENDA team
Haemophilus influenzae RD
RD
-
-
Manually annotated by BRENDA team
; transgenic mice with 200 copies of the human GPx-1 gene
-
-
Manually annotated by BRENDA team
Hep-G2 cells
-
-
Manually annotated by BRENDA team
Saos-2 cell line; U2-OS cell line
-
-
Manually annotated by BRENDA team
cultivar Jubilant
-
-
Manually annotated by BRENDA team
variety gang-2
-
-
Manually annotated by BRENDA team
not in guinea pig
-
-
Manually annotated by BRENDA team
Greasyback shrimp
UniProt
Manually annotated by BRENDA team
B6C3F1/J mice, mating C57BL/6J female mice to C3H/HeJ male mice
-
-
Manually annotated by BRENDA team
fragment
UniProt
Manually annotated by BRENDA team
no activity in Bos taurus
-
-
-
Manually annotated by BRENDA team
no activity in Gallus gallus
-
-
-
Manually annotated by BRENDA team
no activity in Onchorhynchus mykiss
-
-
-
Manually annotated by BRENDA team
no activity in plants
-
-
-
Manually annotated by BRENDA team
isoform Gpx4a
UniProt
Manually annotated by BRENDA team
isoform Gpx4b
UniProt
Manually annotated by BRENDA team
ridgetail white prawn
UniProt
Manually annotated by BRENDA team
Fischer-344 rats
-
-
Manually annotated by BRENDA team
male Sprague-Dawley
-
-
Manually annotated by BRENDA team
rat theta-class glutathione transferase T2-2 (rGST T2-2) presents an ideal scaffold for the design of a novel glutathione peroxidase catalyst because it binds GSH and contains a serine close to substrate binding site, which can be chemically modified to bind selenium. The modified Se-rGST T2-2 efficiently catalyzes the reduction of hydrogen peroxide, and the glutathione peroxidase activity surpasses the activities of some natural glutathione peroxidases
-
-
Manually annotated by BRENDA team
strain YPH499
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae YPH499
strain YPH499
-
-
Manually annotated by BRENDA team
organism exposed to Aroclor 1254
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
methylmercury neurotoxicity is associated with inhibition of glutathione peroxidase
physiological function
-
anti-oxidant enzyme, essential for cell survival during oxidative stress
physiological function
-
glutathione peroxidase-3 is a key antioxidant enzyme in the plasma. Endothelial cell-derived GPx-3 protects the vasculature from oxidative stress
physiological function
Q6ESJ0
plants lacking mitochondrial isoform Gpx3 activity show shorter roots and shoots compared to control plants, and higher amounts of H2O2 mitochondrial release are observed in the roots of these plants cultivated under normal conditions. The accumulation of H2O2 is positively associated with shorter root length in Gpx3s plants
physiological function
-
the enzyme is potentially involved in mediating the immune response and antioxidant defense
physiological function
-
the enzyme plays important roles not only in immune defense, but also in oogenesis in the crayfish
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-linoleoyl lysophosphatidylcholine hydroperoxide + GSH
?
show the reaction diagram
-
-
-
-
?
5-hydroperoxyeicosatetraenoic acid + 2 GSH
5-hydroxyeicosatetraenoic acid + GSSG + H2O
show the reaction diagram
-
-
-
-
?
5-hydroperoxyeicosatetraenoic acid + 2 GSH
5-hydroxyeicosatetraenoic acid + GSSG + H2O
show the reaction diagram
-
-
-
-
?
arachidonic acid 15-hydroperoxide + GSH
15-hydroxyarachidonic acid + GSSG
show the reaction diagram
-
-
-
-
?
cholesterol 5alpha-hydroperoxide + GSH
5alpha-hydroxycholesterol + GSSG
show the reaction diagram
-
-
-
-
?
cholesterol 7alpha-hydroperoxide + GSH
7alpha-hydroxycholesterol + GSSG
show the reaction diagram
-
-
-
-
?
cholesterol 7beta-hydroperoxide + GSH
7beta-hydroxycholesterol + GSSG
show the reaction diagram
-
-
-
-
?
cumene hydroperoxide + GSH
?
show the reaction diagram
-
-
-
-
?
cumene hydroperoxide + GSH
?
show the reaction diagram
-
-
-
-
-
cumene hydroperoxide + GSH
?
show the reaction diagram
-
-
-
-
?
cumene hydroperoxide + GSH
?
show the reaction diagram
-
-
-
-
?
cumene hydroperoxide + GSH
?
show the reaction diagram
-
-
-
-
?
cumene hydroperoxide + GSH
?
show the reaction diagram
-
-
-
-
?
cumene hydroperoxide + GSH
?
show the reaction diagram
-
-
-
-
?
cumene hydroperoxide + GSH
?
show the reaction diagram
-
-
-
-
?
cumene hydroperoxide + GSH
2-phenylpropan-2-ol + GSSG + H2O
show the reaction diagram
-
-
-
-
?
cumene hydroperoxide + GSH
2-phenylpropan-2-ol + GSSG + H2O
show the reaction diagram
Q8MNZ6, Q8MPM5
-
-
-
?
cumene hydroperoxide + H2O2
?
show the reaction diagram
-
-
-
-
?
glutathione + cumene hydroperoxide
?
show the reaction diagram
-
-
-
-
?
glutathione + H2O2
glutathione disulfide + H2O
show the reaction diagram
-
-
-
-
?
glutathione + H2O2
glutathione disulfide + H2O
show the reaction diagram
-
-
-
-
?
glutathione + H2O2
glutathione disulfide + H2O
show the reaction diagram
-
-
-
-
?
glutathione + H2O2
glutathione disulfide + H2O
show the reaction diagram
-
-
-
-
?
glutathione + H2O2
glutathione disulfide + H2O
show the reaction diagram
H2CSR7
-
-
-
?
glutathione + H2O2
glutathione disulfide + H2O
show the reaction diagram
T1RK19
-
-
-
?
glutathione + H2O2
glutathione disulfide + H2O
show the reaction diagram
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
Q5XJZ8
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
lauryl hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
tert-butylhydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
tert-butylhydroperoxide, reduction of hydroperoxides increases with hydrophobicity of substrates
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
cumene hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
cumene hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
cumene hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
cumene hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
cumene hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
ethyl hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
ethyl hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
cholesterol 7beta-hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
menthane hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
ROOH can be: aliphatic or aromatic peroxide or H2O2
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
broad specificity for hydroperoxides
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
broad specificity for hydroperoxides
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
diisopropyl hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
hydroperoxyarachidonate
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
specificity for donor-substrate: free amino group near the SH group inhibits the reaction, free alpha-carboxylic group of glutamic acid residue in glutathione analogs increases reaction rate
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
peroxidized DNA
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
pregnenolone 17alpha-hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
thymine hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
gamma-glutamyl-L-cysteine-methyl ester has 26% of glutathione activity
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
dithiothreitol has 10% of glutathione activity
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
highly specific for glutathione
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
highly specific for glutathione
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
highly specific for glutathione
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
linoleic acid hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
linoleic acid hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
gamma-glutamyl-L-cysteine-methylester has 26% of glutathione activity
-
-
?
glutathione + tert-butyl hydroperoxide
?
show the reaction diagram
P04041
-
-
-
?
H2O2 + cumene peroxide
?
show the reaction diagram
-
-
-
-
?
H2O2 + cumene peroxide
?
show the reaction diagram
-
activity of seleno-glutathione transferase
-
-
?
H2O2 + GSH
H2O + GSSG
show the reaction diagram
-
-
-
-
?
H2O2 + GSH
H2O + GSSG
show the reaction diagram
-
-
-
-
?
H2O2 + GSH
H2O + GSSG
show the reaction diagram
-
-
-
-
?
H2O2 + GSH
H2O + GSSG
show the reaction diagram
-
-
-
-
?
H2O2 + GSH
H2O + GSSG
show the reaction diagram
-
-
-
-
?
H2O2 + GSH
H2O + GSSG
show the reaction diagram
-
-
-
-
?
H2O2 + GSH
H2O + GSSG
show the reaction diagram
-
-
-
-
?
H2O2 + GSH
H2O + GSSG
show the reaction diagram
-
-
-
-
?
H2O2 + GSH
H2O + GSSG
show the reaction diagram
-
-
-
-
?
H2O2 + GSH
H2O + GSSG
show the reaction diagram
-
-
-
-
?
H2O2 + GSH
H2O + GSSG
show the reaction diagram
-
-
-
-
?
H2O2 + GSH
H2O + GSSG
show the reaction diagram
Q5XJZ8
-
-
-
?
H2O2 + GSH
H2O + GSSG
show the reaction diagram
O75715, P07203, P18283, P22352, P59796, Q6PI42, Q8TED1, Q96SL4
-
-
-
?
H2O2 + GSH
H2O + GSSG
show the reaction diagram
-
-
-
-
?
H2O2 + GSH
H2O + GSSG
show the reaction diagram
P00435
-
-
-
?
H2O2 + GSH
H2O + GSSG
show the reaction diagram
Q00277
-
-
-
?
H2O2 + GSH
H2O + GSSG
show the reaction diagram
-
-
-
-
?
H2O2 + GSH
H2O + GSSG
show the reaction diagram
Q1PBM0, Q1PBM1
-
-
-
?
H2O2 + GSH
H2O + GSSG
show the reaction diagram
B4YA17
-
-
-
?
H2O2 + GSH
H2O + GSSG
show the reaction diagram
P67878
-
-
-
?
H2O2 + GSH
H2O + GSSG
show the reaction diagram
Q86EQ5
-
-
-
?
H2O2 + GSH
H2O + GSSG
show the reaction diagram
-
the enzyme protects cells against oxidative damage
-
-
?
H2O2 + GSH
H2O + GSSG
show the reaction diagram
-
activity of seleno-glutathione transferase
-
-
?
H2O2 + GSH
H2O + GSSG
show the reaction diagram
-
instead of tert-butyl hydroperoxide
-
-
?
H2O2 + GSH
H2O + GSSG
show the reaction diagram
Haemophilus influenzae RD
-
-
-
-
?
H2O2 + GSH
H2O + GSSG
show the reaction diagram
Saccharomyces cerevisiae YPH499
-
-
-
-
?
H2O2 + ROOH
H2O + ROH
show the reaction diagram
-
-
-
-
?
H2O2 + thioredoxin
H2O + ?
show the reaction diagram
O75715, P07203, P18283, P22352, P59796, Q6PI42, Q8TED1, Q96SL4
-
-
-
?
L-alpha-phosphatidylcholine hydroperoxide + GSH
?
show the reaction diagram
-
-
-
-
?
L-alpha-phosphatidylcholine hydroperoxide + GSH
?
show the reaction diagram
-
not hydrogen peroxide
-
-
?
linoleic acid hydroperoxide + GSH
?
show the reaction diagram
-
-
-
-
?
linoleic acid hydroperoxide + GSH
?
show the reaction diagram
-
-
-
-
?
linoleic acid hydroperoxide + GSH
?
show the reaction diagram
-
-
-
-
?
linolenic acid hydroperoxide + GSH
?
show the reaction diagram
-
-
-
-
?
linolenic acid hydroperoxide + GSH
?
show the reaction diagram
-
-
-
-
?
linolenic acid hydroperoxide + GSH
?
show the reaction diagram
-
-
-
-
?
linolenic acid hydroperoxide + GSH
?
show the reaction diagram
-
-
-
-
?
phosphatidylcholine hydroperoxide + GSH
?
show the reaction diagram
-
in the absence of phospholipase A2
-
-
?
phosphatidylcholine hydroperoxide + H2O
?
show the reaction diagram
-
phosphatidylcholine hydroperoxide is a substrate after being previously incubated with 51 mU of phospholipase A2 for 10 min
-
-
?
phosphatidylcholine hydroperoxide + thioredoxin
?
show the reaction diagram
Q9VZQ8
-
-
-
?
protamine + H2O2
?
show the reaction diagram
-
snGPx acts as a protamine cysteine thiol peroxidase
-
-
?
tert-butyl hydroperoxide + 2 GSH
tert-butyl alcohol + GSSG + H2O
show the reaction diagram
-
-
-
-
?
tert-butyl hydroperoxide + 2 GSH
tert-butyl alcohol + GSSG + H2O
show the reaction diagram
-
-
-
-
?
tert-butyl hydroperoxide + 2 GSH
tert-butyl alcohol + GSSG + H2O
show the reaction diagram
-
-
-
-
?
tert-butyl hydroperoxide + 2 GSH
tert-butyl alcohol + GSSG + H2O
show the reaction diagram
-
-
-
-
?
tert-butyl hydroperoxide + 2 GSH
tert-butyl alcohol + GSSG + H2O
show the reaction diagram
-
-
-
-
?
tert-butyl hydroperoxide + 2 GSH
tert-butyl alcohol + GSSG + H2O
show the reaction diagram
-
-
-
-
?
tert-butyl hydroperoxide + 2 GSH
tert-butyl alcohol + GSSG + H2O
show the reaction diagram
-
-
-
-
?
tert-butyl hydroperoxide + 2 GSH
tert-butyl alcohol + GSSG + H2O
show the reaction diagram
-
-
-
-
?
tert-butyl hydroperoxide + 2 GSH
tert-butyl alcohol + GSSG + H2O
show the reaction diagram
-
activity of seleno-glutathione transferase
-
-
?
tert-butyl hydroperoxide + GSH
tert-butyl alcohol + GSSG + H2O
show the reaction diagram
-
-
-
-
?
tert-butyl hydroperoxide + GSH
tert-butyl alcohol + GSSG + H2O
show the reaction diagram
-
-
-
-
?
tert-butyl hydroperoxide + GSH
tert-butyl alcohol + GSSG + H2O
show the reaction diagram
-
-
-
-
?
tert-butyl hydroperoxide + GSH
tert-butyl alcohol + GSSG + H2O
show the reaction diagram
-
-
-
-
?
tert-butyl hydroperoxide + GSH
tert-butyl alcohol + GSSG + H2O
show the reaction diagram
Haemophilus influenzae RD
-
-
-
-
?
tert-butylhydroperoxide + 3-carboxy-4-nitrobenzenethiol
?
show the reaction diagram
-
-
-
-
?
tert-butylhydroperoxide + GSH
?
show the reaction diagram
-
-
-
-
?
tert-butylhydroperoxide + GSH
?
show the reaction diagram
P83645
-
-
-
?
lipid peroxide + GSH
? + GSSG
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
involved in mainenance of the steady state levels of H2O2 in heart mitochondria matrix
-
-
-
additional information
?
-
-
major antioxidant enzyme
-
-
-
additional information
?
-
-
N-ribosyl-1-glutathione can not be used as substrate. Coupling of GSH with a monosaccharide such as ribose might contribute to the decreased cell GSH and glutathione peroxidase activity observed in diabetics
-
-
-
additional information
?
-
-
the enzyme can reduce fatty acid, phospholipid, and short chain organic hydroperoxides utilizing a novel redox cycle in which enzyme activity is linked to the reduction of trypanothione, by glutathione. The activity of TcGPXI can also be linked to trypanothione reduction by an alternative pathway involving thioredoxin-like protein tryparedoxin. Overexpression of TcGPXI in transfected parasites confers increased resistance to exogenous hydroperoxides
-
-
-
additional information
?
-
-
the enzyme is uniquely involved in the detoxification of oxidative damage to membrane lipids. It plays a role in vivo in the mechanism of apoptosis induced by oxidative stress that most likely occurs through oxidative damage to mitochondrial phospholipids such as cardiolipin
-
-
-
additional information
?
-
Q8MNZ6, Q8MPM5
the enzyme may be important in removing host derived fatty acid hydroperoxides which, as well as being potentially damaging to the parasite themselves, form an important part of plant defence signalling pathways
-
-
-
additional information
?
-
-
the enzyme plays a critical role in antioxidant defense system by catalyzing detoxification of H2O2 and organic hydroperoxides. Significant down-regulation of immunodetectable glutathione peroxidase proteins in remnant kidney in chronic renal failure, glutathione peroxidase activity is not significantly affected
-
-
-
additional information
?
-
Q8MNZ6, Q8MPM5
the protein is likely to have a role in metabolism of active oxygen species derived from internal metabolism
-
-
-
additional information
?
-
-
upregulation of GPx-1 gene expression in prostate cancer cells bei genistein
-
-
-
additional information
?
-
-
N-ribosyl-1-glutathione can not be used as substrate
-
-
-
additional information
?
-
Q8MNZ6, Q8MPM5
the enzyme does not metabolise H2O2
-
-
-
additional information
?
-
-
adenosine may protect the cardiovascular system from ischemia/reperfusion injury, in part, by enhancing the expression of the central intracellular antioxidant enzyme, GPx-1
-
-
-
additional information
?
-
O22850
ATGPX3 is involved in the regulation of ABA-activated calcium signaling in guard cells. ATGPX3 might play dual and distinctive roles in H2O2 homeostasis, acting as a general scavenger and specifically relaying the H2O2 signal as an oxidative signal transducer in abscisic acid and drought stress signaling
-
-
-
additional information
?
-
-
GPX1 protects against diquat-induced cell death, but promotes peroxynitrite induced cell death. GPX1 seems to play contrasting roles in coping with reactive oxygen species vs. reactive nitrogen species
-
-
-
additional information
?
-
-
Gpx2 affords resistance to gastrointestinal pathology in Se-depleted mice
-
-
-
additional information
?
-
-
increased GPx-1 expression in immature cortical neurons of transgenic mice with 200 copies of the human GPx-1 gene confers protection from oxidative stress
-
-
-
additional information
?
-
-
glutathione peroxidase 3 of Saccharomyces cerevisiae regulates the activity of methionine sulfoxide reductase in a redox state-dependent way
-
-
-
additional information
?
-
Q5XJZ8
does not accept thioredoxin as hydrogen donor
-
-
-
additional information
?
-
-
Gpx3 protects glutamine synthetase from non-enzymatic proteolysis
-
-
-
additional information
?
-
-
glutathione peroxidase 2 inhibits malignant characteristics of tumor cells, such as migration and invasion, by counteracting cyclooxygenase-2 expression but is required for the growth of transformed intestinal cells and may, therefore, facilitate tumor cell growth
-
-
-
additional information
?
-
-
selenium containing glutathione transferase zeta1-1 does also possess glutathione peroxidase activity
-
-
-
additional information
?
-
Saccharomyces cerevisiae YPH499
-
Gpx3 protects glutamine synthetase from non-enzymatic proteolysis
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
1-linoleoyl lysophosphatidylcholine hydroperoxide + GSH
?
show the reaction diagram
-
-
-
-
?
5-hydroperoxyeicosatetraenoic acid + 2 GSH
5-hydroxyeicosatetraenoic acid + GSSG + H2O
show the reaction diagram
-
-
-
-
?
5-hydroperoxyeicosatetraenoic acid + 2 GSH
5-hydroxyeicosatetraenoic acid + GSSG + H2O
show the reaction diagram
-
-
-
-
?
cumene hydroperoxide + GSH
?
show the reaction diagram
-
-
-
-
?
cumene hydroperoxide + GSH
?
show the reaction diagram
-
-
-
-
?
cumene hydroperoxide + GSH
?
show the reaction diagram
-
-
-
-
?
cumene hydroperoxide + GSH
?
show the reaction diagram
-
-
-
-
?
cumene hydroperoxide + GSH
?
show the reaction diagram
-
-
-
-
?
cumene hydroperoxide + GSH
?
show the reaction diagram
-
-
-
-
?
glutathione + H2O2
glutathione disulfide + H2O
show the reaction diagram
-
-
-
-
?
glutathione + H2O2
glutathione disulfide + H2O
show the reaction diagram
-
-
-
-
?
glutathione + H2O2
glutathione disulfide + H2O
show the reaction diagram
-
-
-
-
?
glutathione + H2O2
glutathione disulfide + H2O
show the reaction diagram
-
-
-
-
?
glutathione + H2O2
glutathione disulfide + H2O
show the reaction diagram
H2CSR7
-
-
-
?
glutathione + H2O2
glutathione disulfide + H2O
show the reaction diagram
T1RK19
-
-
-
?
glutathione + H2O2
glutathione disulfide + H2O
show the reaction diagram
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
-
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
lauryl hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
tert-butylhydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
tert-butylhydroperoxide, reduction of hydroperoxides increases with hydrophobicity of substrates
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
cumene hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
cumene hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
cumene hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
cumene hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
cumene hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
ethyl hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
ethyl hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
cholesterol 7beta-hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
menthane hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
ROOH can be: aliphatic or aromatic peroxide or H2O2
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
broad specificity for hydroperoxides
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
broad specificity for hydroperoxides
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
diisopropyl hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
hydroperoxyarachidonate
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
specificity for donor-substrate: free amino group near the SH group inhibits the reaction, free alpha-carboxylic group of glutamic acid residue in glutathione analogs increases reaction rate
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
peroxidized DNA
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
pregnenolone 17alpha-hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
thymine hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
dithiothreitol has 10% of glutathione activity
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
highly specific for glutathione
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
highly specific for glutathione
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
highly specific for glutathione
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
linoleic acid hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
linoleic acid hydroperoxide
-
-
?
glutathione + ROOH
glutathione disulfide + ROH + H2O
show the reaction diagram
-
gamma-glutamyl-L-cysteine-methylester has 26% of glutathione activity
-
-
?
H2O2 + GSH
H2O + GSSG
show the reaction diagram
-
-
-
-
?
H2O2 + GSH
H2O + GSSG
show the reaction diagram
-
-
-
-
?
H2O2 + GSH
H2O + GSSG
show the reaction diagram
-
-
-
-
?
H2O2 + GSH
H2O + GSSG
show the reaction diagram
-
-
-
-
?
H2O2 + GSH
H2O + GSSG
show the reaction diagram
-
-
-
-
?
H2O2 + GSH
H2O + GSSG
show the reaction diagram
-
-
-
-
?
H2O2 + GSH
H2O + GSSG
show the reaction diagram
-
-
-
-
?
H2O2 + GSH
H2O + GSSG
show the reaction diagram
-
the enzyme protects cells against oxidative damage
-
-
?
linolenic acid hydroperoxide + GSH
?
show the reaction diagram
-
-
-
-
?
linolenic acid hydroperoxide + GSH
?
show the reaction diagram
-
-
-
-
?
linolenic acid hydroperoxide + GSH
?
show the reaction diagram
-
-
-
-
-
tert-butyl hydroperoxide + 2 GSH
tert-butyl alcohol + GSSG + H2O
show the reaction diagram
-
-
-
-
?
tert-butyl hydroperoxide + 2 GSH
tert-butyl alcohol + GSSG + H2O
show the reaction diagram
-
-
-
-
?
tert-butyl hydroperoxide + 2 GSH
tert-butyl alcohol + GSSG + H2O
show the reaction diagram
-
-
-
-
?
tert-butyl hydroperoxide + 2 GSH
tert-butyl alcohol + GSSG + H2O
show the reaction diagram
-
-
-
-
?
tert-butyl hydroperoxide + 2 GSH
tert-butyl alcohol + GSSG + H2O
show the reaction diagram
-
-
-
-
?
linolenic acid hydroperoxide + GSH
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
involved in mainenance of the steady state levels of H2O2 in heart mitochondria matrix
-
-
-
additional information
?
-
-
major antioxidant enzyme
-
-
-
additional information
?
-
-
N-ribosyl-1-glutathione can not be used as substrate. Coupling of GSH with a monosaccharide such as ribose might contribute to the decreased cell GSH and glutathione peroxidase activity observed in diabetics
-
-
-
additional information
?
-
-
the enzyme can reduce fatty acid, phospholipid, and short chain organic hydroperoxides utilizing a novel redox cycle in which enzyme activity is linked to the reduction of trypanothione, by glutathione. The activity of TcGPXI can also be linked to trypanothione reduction by an alternative pathway involving thioredoxin-like protein tryparedoxin. Overexpression of TcGPXI in transfected parasites confers increased resistance to exogenous hydroperoxides
-
-
-
additional information
?
-
-
the enzyme is uniquely involved in the detoxification of oxidative damage to membrane lipids. It plays a role in vivo in the mechanism of apoptosis induced by oxidative stress that most likely occurs through oxidative damage to mitochondrial phospholipids such as cardiolipin
-
-
-
additional information
?
-
Q8MNZ6, Q8MPM5
the enzyme may be important in removing host derived fatty acid hydroperoxides which, as well as being potentially damaging to the parasite themselves, form an important part of plant defence signalling pathways
-
-
-
additional information
?
-
-
the enzyme plays a critical role in antioxidant defense system by catalyzing detoxification of H2O2 and organic hydroperoxides. Significant down-regulation of immunodetectable glutathione peroxidase proteins in remnant kidney in chronic renal failure, glutathione peroxidase activity is not significantly affected
-
-
-
additional information
?
-
Q8MNZ6, Q8MPM5
the protein is likely to have a role in metabolism of active oxygen species derived from internal metabolism
-
-
-
additional information
?
-
-
upregulation of GPx-1 gene expression in prostate cancer cells bei genistein
-
-
-
additional information
?
-
-
adenosine may protect the cardiovascular system from ischemia/reperfusion injury, in part, by enhancing the expression of the central intracellular antioxidant enzyme, GPx-1
-
-
-
additional information
?
-
O22850
ATGPX3 is involved in the regulation of ABA-activated calcium signaling in guard cells. ATGPX3 might play dual and distinctive roles in H2O2 homeostasis, acting as a general scavenger and specifically relaying the H2O2 signal as an oxidative signal transducer in abscisic acid and drought stress signaling
-
-
-
additional information
?
-
-
GPX1 protects against diquat-induced cell death, but promotes peroxynitrite induced cell death. GPX1 seems to play contrasting roles in coping with reactive oxygen species vs. reactive nitrogen species
-
-
-
additional information
?
-
-
Gpx2 affords resistance to gastrointestinal pathology in Se-depleted mice
-
-
-
additional information
?
-
-
increased GPx-1 expression in immature cortical neurons of transgenic mice with 200 copies of the human GPx-1 gene confers protection from oxidative stress
-
-
-
additional information
?
-
-
glutathione peroxidase 2 inhibits malignant characteristics of tumor cells, such as migration and invasion, by counteracting cyclooxygenase-2 expression but is required for the growth of transformed intestinal cells and may, therefore, facilitate tumor cell growth
-
-
-
additional information
?
-
-
selenium containing glutathione transferase zeta1-1 does also possess glutathione peroxidase activity
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
cadmium
H9AZT5, H9AZT6
in liver, by 24 h, exposure to alow dose of Cd causes 13% loss of Gpx4a expression. At higher dose, Cd leads to 40% decrease in Gpx4a expression. Longer exposure periods cause about 20% loss of liver Gpx4a expression by low Cd dose; olfactory isoform Gpx4b mRNA expression is not extensively modulated by presence of cadmium ions. In liver, by 24 h, exposure to alow dose of Cd causes 18% loss of Gpx4b expression. At higher dose, Cd leads to 37% decrease in Gpx4b expression. Longer exposure periods cause about 22% loss of liver Gpx4b expression by low Cd dose, whereas at higher Cd exposures, a 33% loss in Gpx4b expression is observed
Se
-
selenium-dependent enzyme
selenium
-
selenocysteine
selenium
-
selenocysteine
selenium
-
selenocysteine
selenium
-
selenocysteine
selenium
-
selenocysteine
selenium
-
selenocysteine
selenium
-
selenocysteine
selenium
-
selenocysteine
selenium
-
one atom of selenium per subunit
selenium
-
selenium-dependent enzyme
selenium
A0EYM2
-
selenium
-
selenium supplementation by selenoprotein P prevents oxidative damage of human endothelial cells by restoring expression and enzymatic activity of glutathione peroxidase
selenium
-
subtoxic range of selenium (100 nM) concentrations are required to increase and maintain the expression of anti-oxidant selenoproteins glutathione peroxidase GPX1 and GPX4 at a constant level in cultures of human adenocarcinoma cell lines (H460, H1703 and H1944) and in HPL1D, a non-transformed lung epithelial cell line
selenium
P00435
selenoprotein
selenium
O75715, P18283, P59796, Q8TED1, Q96SL4
activity depends on selenium; activity depends on selenium; activity depends on selenium; activity depends on selenium; activity depends on selenium; activity depends on selenium; activity depends on selenium; activity depends on selenium
selenium
Q5XJZ8
selenoprotein
selenium
P83645
selenoprotein, selenium is necessary for activity
selenium
-
contains one selenium ion per subunit
selenium
-
dependent on
selenium
-
selenium supplementation (0.2 mg/kg) remarkably improves glutathione peroxidase activity
selenium
-
the enzyme contains selenium
selenium
-
selenoenzyme
selenium
-
Gpx is a selenium-containing enzyme
selenium
-
selenium-containing enzyme
selenium
-
dependent on
selenium
H2CSR7
dependent on
selenium
-
dependent on
Mn2+
-
221% relative activity
additional information
-
induction of cellular selenium-dependent glutathione peroxidase activity: 2.2fold by 0.015 mM Na2SeO3, 1.9fold by 0.1 mM Na2SeO4, 4.3fold by 0.03 mM L-selenocystine. 4.6fold by 0.1 mM L-selenocystine,2-oxoselenazolidine-4(R)-carboxylic acid, 1.4fold by 0.1 mM D-selenocystine,2-oxoselenazolidine-4(R)-carboxylic acid, 2.1fold by 0.1 mM L-selenocystine,2-(RS)-methylselenazolidine-4(R)-carboxylic acid, 1.3fold by 0.1 mM D-L-selenocystine,2-(RS)-methylselenazolidine-4(R)-carboxylic acid, 5.9fold by 0.1 mM L-selenoproline, 1.5fold by Se-methyl-L-selenocysteine, 1.8fold by L-selenomethionine
additional information
-
selenium, zinc and tellurium have no stimulatory effect on glutathione peroxidase
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-deoxyglucosone
-
-
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
adenosine
-
inhibition probably due to inhibition of glutathione reductase in coupled assay
Ag+
-
-
alpha-Mercaptopropionylglycine
-
-
Chloroacetate
-
-
CN-
-
no inhibition if simultaneously incubated with 2-mercaptoethanol, glutathione or dithiothreitol
cysteine
-
GPx-1 is inhibited by 0.5 mM cysteine
diethyldithiocarbamate
-
significant inhibition of selenium-dependent enzyme after intraperitoneal injection of rats with diethyldithiocarbamate, which returns to normal at 48 h after administration of injection. It is possible that inhibition of superoxide dismutase by diethyldithiocarbamate leads to accumulation of superoxide anion which in turn inactivates selenium-dependent glutathione peroxidase by its reaction with slenium at the active site of the enzyme
docosahexaenoic acid
-
0.1 mM reduces the level of protein expression of GPx-4 by at least 50%
glutathione
-
-
Glyoxal
-
-
Gold(I)-thioglucose
-
-
homocysteine
-
GPx-1 is inhibited by 0.05-0.5 mM homocysteine, especially at low glutathione concentrations
iodoacetamide
-
inhibitory only after preincubation with glutathione, not after preincubation with H2O2
iodoacetate
-
-
iodoacetate
-
inhibitory only after preincubation with glutathione, not after preincubation with H2O2
iodoacetate
-
-
Mercaptosuccinate
-
-
Mercaptosuccinate
-
-
Mercaptosuccinate
-
-
methylglyoxal
-
Arg184 and Arg185, located in the glutathione binding site of the enzyme are irreversibly modified by treatment with methylglyoxal
NADPH
-
inhibition probably due to inhibition of glutathione reductase in coupled assay
p-chloromercuribenzoate
-
-
Penicillamine
-
-
Phenylglyoxal
-
-
Polyvalent anions
-
e.g. phosphate, sulfate, maleate
-
S-nitro-N-acetyl-DL-penicillamine
-
-
tellurium
-
a decrease in specific activity is seen after combined treatment with zinc (515 mg/l) and tellurium (9.4 mg/l), but not with tellurium alone
Zn2+
-
a decrease in specific activity is seen after combined treatment with zinc (515 mg/l) and tellurium (9.4 mg/l), but not with Zn2+ alone
additional information
-
not: ophthalmic acid
-
additional information
-
dicarbonyl compounds directly inactivate the enzyme, resulting in an increase in intracellular peroxides, which are responsible for oxidative cellular damage
-
additional information
-
administration of lead acetate evokes decrease of GPx activity in the kidney of both male and female rats, GPx activity decreases only in male hearts
-
additional information
-
for each 1 year increase in age, GPx activity decreases by 0.0029 mmol/min
-
additional information
-
aging decreases expression and activity of glutathione peroxidase-1 in human endothelial progenitor cells, increasing selenium concentration in the cell culture does not affect the protein levels of GPX1, suggesting the reduced GPX1 in old subject's endothelial progenitor cells is selenium independent
-
additional information
-
reduced plasma glutathione peroxidase 3 levels are found in patients with type 2 diabetes mellitus
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cysteine
-
cysteine increases activity at low glutathione concentrations
etoposide
-
activates p53, wich induces the expression of glutathione peroxidase
genistein
-
-
reduced glutathione
-
activated by 2 to 6 mM
Selenite
-
-
hyperglycemia
-
increased GPX1 activity in rat VSM cell. When cells are exposed to high glucose (25 mM) for 48 h, GPX1 activity is 2.5fold greater than in cells grown in normal glucose (5 mM), while the GPX1 expression levels are the same
-
additional information
-
administration of lead acetate (100 and 1000 mg/l for 18 weeks) evokes increase of GPx activity in the kidney of female, but not male rats
-
additional information
-
postmenopausal women have significantly greater plasma GPx activities compared to premenopausal women possibly in response to oxidative processes associated with aging
-
additional information
-
thiazolidinediones-mediated activation of peroxisome proliferatoractivated receptor gamma induces gene expression of glutathione peroxidase 3
-
additional information
-
Cd+- and Hg+-induced root growth inhibition is strongly correlated with increased glutathione peroxidase activity, a slight increase of glutathione peroxidase activity is observed after application of Pb2+, Ni2+, and Zn2+, while Co2+ does not affect glutathione peroxidase activity, GPX activity is not affected by cold, heat or drought treatment and only a slight increase is observed after salt or H2O2 treatment
-
additional information
-
neither prostate tissue nor serum selenium concentrations are associated with prostate glutathione peroxidase activity
-
additional information
-
systemic oxidative stress long lasting rat pregnancy induces, at seventeen days of pregnancy, an increase of membrane glutathione peroxidase activity
-
additional information
-
injection of the O-GlcNAcase inhibitor 1,2-dideoxy-2'-propyl-alpha-D-glucopyranoso-[2,1-d]-DELTA2'-thiazoline increases GPX1 activity in the mouse liver
-
additional information
-
increasing the cellular O-GlcNAcylation level enhances GPX1 activity
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.004
cholesterol 5alpha-hydroperoxide
-
-
0.011
cholesterol 7alpha-hydroperoxide
-
-
0.003
cholesterol 7beta-hydroperoxide
-
-
0.006
cumene hydroperoxide
-
-
0.111
cumene hydroperoxide
-
-
0.144
cumene hydroperoxide
-
-
0.26
cumene hydroperoxide
-
-
7.8
cumene hydroperoxide
-
pH 7.5, 25C
0.09
cumene peroxide
-
25C, pH 8
0.42
cumene peroxide
-
27C, pH 7.0, activity of seleno-glutathione transferase
1.33
glutathione
-
-
0.033
GSH
-
in 50 mM potassium phosphate buffer (pH 7.4), at 25C
0.15
GSH
-
27C, pH 7.0, reaction with tert-butyl hydroperoxide, activity of seleno-glutathione transferase
0.2
GSH
-
apparent value, imprinted GSH-selenosubtilisin in the presence of 0.5 mM H2O2, in 50 mM PIPES buffer, pH 7.0 at 37C
0.22
GSH
-
27C, pH 7.0, reaction with cumene peroxide, activity of seleno-glutathione transferase
0.26
GSH
-
27C, pH 7.0, reaction with H2O2, activity of seleno-glutathione transferase
0.3
GSH
-
apparent value, imprinted GSH-selenosubtilisin in the presence of 1 mM H2O2, in 50 mM PIPES buffer, pH 7.0 at 37C
0.4
GSH
-
apparent value, imprinted GSH-selenosubtilisin in the presence of 2 mM H2O2, in 50 mM PIPES buffer, pH 7.0 at 37C
2.1
GSH
-
pH 7.5, 25C, reaction with H2O2
2.6
GSH
-
pH 7.5, 25C, reaction with cumene hydroperoxide
3.2
GSH
-
-
4.9
GSH
-
pseudo Km
5.5
GSH
-
pH 7.5, 25C, reaction with tert-butyl hydroperoxide
5.9
GSH
-
25C, pH 8
5.93
GSH
-
wild type enzyme, in the presence of 0.1 mM H2O2, at 37C and pH 7.0
7.96
GSH
-
wild type enzyme, in the presence of 0.2 mM H2O2, at 37C and pH 7.0
9.87
GSH
-
wild type enzyme, in the presence of 0.5 mM H2O2, at 37C and pH 7.0
11.1
GSH
-
wild type enzyme, in the presence of 1 mM H2O2, at 37C and pH 7.0
0.00229
H2O2
-
-
0.003
H2O2
-
-
0.012
H2O2
-
25C, pH 8
0.208
H2O2
-
in 50 mM potassium phosphate buffer (pH 7.4), at 25C
0.26
H2O2
-
27C, pH 7.0, activity of seleno-glutathione transferase
0.45
H2O2
-
apparent value, imprinted GSH-selenosubtilisin in the presence of 0.5 mM GSH, in 50 mM PIPES buffer, pH 7.0 at 37C
0.62
H2O2
-
apparent value, imprinted GSH-selenosubtilisin in the presence of 1 mM GSH, in 50 mM PIPES buffer, pH 7.0 at 37C
0.77
H2O2
-
apparent value, imprinted GSH-selenosubtilisin in the presence of 2 mM GSH, in 50 mM PIPES buffer, pH 7.0 at 37C
4.3
H2O2
-
pH 7.5, 25C
8.99
H2O2
-
wild type enzyme, in the presence of 0.25 mM GSH, at 37C and pH 7.0
12.6
H2O2
-
wild type enzyme, in the presence of 0.5 mM GSH, at 37C and pH 7.0
15.88
H2O2
-
wild type enzyme, in the presence of 1 mM GSH, at 37C and pH 7.0
19.08
H2O2
-
wild type enzyme, in the presence of 2 mM GSH, at 37C and pH 7.0
0.026
L-alpha-phosphatidylcholine hydroperoxide
-
-
-
9.7
L-alpha-phosphatidylcholine hydroperoxide
-
-
-
0.007
linolenic acid hydroperoxide
-
-
3.8
linolenic acid hydroperoxide
-
-
0.059
tert-butyl hydroperoxide
-
-
0.09
tert-butyl hydroperoxide
-
25C, pH 8
0.2088
tert-butyl hydroperoxide
-
-
0.91
tert-butyl hydroperoxide
-
27C, pH 7.0, activity of seleno-glutathione transferase
7.9
tert-butyl hydroperoxide
-
pH 7.5, 25C
0.024
tert-butylhydroperoxide
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.8
cumene peroxide
-
27C, pH 7.0, activity of seleno-glutathione transferase
35.78
cumene peroxide
-
27C, pH 7.0, activity of seleno-glutathione transferase
14.48
GSH
-
apparent value, imprinted GSH-selenosubtilisin in the presence of 0.5 mM H2O2, in 50 mM PIPES buffer, pH 7.0 at 37C
19.5
GSH
-
apparent value, imprinted GSH-selenosubtilisin in the presence of 1 mM H2O2, in 50 mM PIPES buffer, pH 7.0 at 37C
24.5
GSH
-
apparent value, imprinted GSH-selenosubtilisin in the presence of 2 mM H2O2, in 50 mM PIPES buffer, pH 7.0 at 37C
221.7
GSH
-
wild type enzyme, in the presence of 0.1 mM H2O2, at 37C and pH 7.0
293.3
GSH
-
wild type enzyme, in the presence of 0.2 mM H2O2, at 37C and pH 7.0
361.7
GSH
-
wild type enzyme, in the presence of 0.5 mM H2O2, at 37C and pH 7.0
408.3
GSH
-
wild type enzyme, in the presence of 1 mM H2O2, at 37C and pH 7.0
5.7
H2O2
-
27C, pH 7.0, activity of seleno-glutathione transferase
10.55
H2O2
-
apparent value, imprinted GSH-selenosubtilisin in the presence of 0.5 mM GSH, in 50 mM PIPES buffer, pH 7.0 at 37C
16.02
H2O2
-
apparent value, imprinted GSH-selenosubtilisin in the presence of 1 mM GSH, in 50 mM PIPES buffer, pH 7.0 at 37C
20.83
H2O2
-
apparent value, imprinted GSH-selenosubtilisin in the presence of 2 mM GSH, in 50 mM PIPES buffer, pH 7.0 at 37C
44.03
H2O2
-
27C, pH 7.0, activity of seleno-glutathione transferase
316.7
H2O2
-
wild type enzyme, in the presence of 0.25 mM GSH, at 37C and pH 7.0
445
H2O2
-
wild type enzyme, in the presence of 0.5 mM GSH, at 37C and pH 7.0
560
H2O2
-
wild type enzyme, in the presence of 1 mM GSH, at 37C and pH 7.0
670
H2O2
-
wild type enzyme, in the presence of 2 mM GSH, at 37C and pH 7.0
25.3
tert-butyl hydroperoxide
-
27C, pH 7.0, activity of seleno-glutathione transferase
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.013
-
crude enzyme, at 25C
0.07
-
cholesterol 5alpha-hydroperoxide
0.1
-
cholesterol 7beta-hydroperoxide
0.13
-
linolenic acid hydroperoxide
0.16
-
L-alpha-phosphatidylcholine hydroperoxide
0.18
-
cholesterol 7alpha-hydroperoxide
0.24
Q9VZQ8
mutant enzyme N136A, using thioredoxin and phosphatidylcholine hydroperoxide as substrates
0.4
Q9VZQ8
mutant enzyme N136H, using thioredoxin and phosphatidylcholine hydroperoxide as substrates
1.462
-
after 112.46fold purification, at 25C
4.29
Q9VZQ8
mutant enzyme N40A, using thioredoxin and phosphatidylcholine hydroperoxide as substrates
5
-
Saos-2
5.5
-
Saos-2 treated with etoposide
5.81
Q9VZQ8
mutant enzyme C74A, using thioredoxin and phosphatidylcholine hydroperoxide as substrates
6.7
-
U2-OS
11.9
-
U2-OS treated with etoposide
14.38
Q9VZQ8
wild type enzyme, using thioredoxin and phosphatidylcholine hydroperoxide as substrates
120
-
subcellular fractionation
281
-
outer mitochondrial membrane
337
-
inner mitochondrial membrane
350
-
-
402
-
linolenic acid hydroperoxide
408
-
linoleic acid hydroperoxide
472
-
cumene hydroperoxide
511
-
arachidonic acid 15-hydroperoxide
1300
-
plasma membrane
1407
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8
-
reaction with cumene hydroperoxide
8.7
-
-
8.8
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7
-
less than 20% of maximal activity below
7.2 - 7.6
-
-
7.5 - 9
-
pH 7.5: about 45% of maximal activity, pH 9.0: about 50% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
-
reaction with cumene hydroperoxide
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 45
-
25C: about 40% of maximal activity, 45C: about 40% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.4
-
calculated from amino acid sequence
7.6
P83645
isoelectric focusing
7.7
T1RK19
calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
pGPx is expressed during bovine adipocyte differentiation, transcriptional control of pGPx in cattle might be carried out by C/EBPdelta
Manually annotated by BRENDA team
-
intraperitoneal fat, high expression of pGPx
Manually annotated by BRENDA team
-
GPx1 is highly expressed in adrenal glands
Manually annotated by BRENDA team
-
GPx-3 is detected at very low levels under basal conditions
Manually annotated by BRENDA team
-
GPX activity was significantly higher in HIV-positive than in HIV-negative subjects. When GPX activity is compared by HIV status and ARTuse, HIV-negative subjects have the lowest median, HIV-positive subjects not taking ART have an intermediate median (11% greater than that of HIV-negative subjects), and HIV-positive subjects taking ART have the highest median (21% higher than that of the HIV-positive subjects not taking ART)
Manually annotated by BRENDA team
-
highest expression
Manually annotated by BRENDA team
-
activity in brain is much lower than in liver
Manually annotated by BRENDA team
H9AZT5, H9AZT6
highest mRNA expression in ovary, followed by pyloric ceca, heart, liver and brain
Manually annotated by BRENDA team
-
GPx is detected on the membranes of vacuoles situated in the gland's epithelial cells
Manually annotated by BRENDA team
-
potential for Gpx1 and Gpx2 redundancy in lymphatic tissue, but not in epithelial cells of the colon crypt or in the lamina propria, sub-mucosa, muscularis or serosa
Manually annotated by BRENDA team
-
human endothelial cell line Ea.hy926
Manually annotated by BRENDA team
-
extremely highly expressed in early embryos
Manually annotated by BRENDA team
O75715, P18283, P59796, Q8TED1, Q96SL4
Gpx-5
Manually annotated by BRENDA team
-
activity in erythrocytes from patients with non-small-cell lung cancer and small-cell lung cancer is slightly increased compared to healthy control group
Manually annotated by BRENDA team
O75715, P18283, P59796, Q8TED1, Q96SL4
GPx-2
Manually annotated by BRENDA team
-
GPx-3 is detected at very low levels under basal conditions
Manually annotated by BRENDA team
-
overexpression of glutathione peroxidase attenuates myocardial remodeling and preserves diastolic function in diabetic heart
Manually annotated by BRENDA team
-
weak expression of pGPx
Manually annotated by BRENDA team
H9AZT5, H9AZT6
highest mRNA expression in ovary, followed by pyloric ceca, heart, liver and brain
Manually annotated by BRENDA team
H9AZT5, H9AZT6
highest mRNA expression in pyloric ceca, followed by brain, heart and liver
Manually annotated by BRENDA team
T1RK19
highest expression
Manually annotated by BRENDA team
-
most abundantly expressed in hepatopancreas
Manually annotated by BRENDA team
-
human primary pulmonary artery endothelial cells
Manually annotated by BRENDA team
-
a non-transformed lung epithelial cell line
Manually annotated by BRENDA team
-
GPx-3 is detected at very low levels under basal conditions
Manually annotated by BRENDA team
Q8MNZ6, Q8MPM5
restricted to
Manually annotated by BRENDA team
-
significant down-regulation of immunodetectable glutathione peroxidase proteins in remnant kidney in chronic renal failure, glutathione peroxidase activity is not significantly affected
Manually annotated by BRENDA team
-
high expression of pGPx
Manually annotated by BRENDA team
H2CSR7
highest expression
Manually annotated by BRENDA team
-
activity in brain is much lower than in liver
Manually annotated by BRENDA team
-
weak expression of pGPx
Manually annotated by BRENDA team
H9AZT5, H9AZT6
highest mRNA expression in ovary, followed by pyloric ceca, heart, liver and brain
Manually annotated by BRENDA team
H9AZT5, H9AZT6
highest mRNA expression in pyloric ceca, followed by brain, heart and liver
Manually annotated by BRENDA team
-
weak expression of pGPx
Manually annotated by BRENDA team
T1RK19
lowest expression
Manually annotated by BRENDA team
-
vascular smooth muscles cell
Manually annotated by BRENDA team
-
upregulated Gpx-1 activity is associated with neuroprotection in vitro
Manually annotated by BRENDA team
O75715, P18283, P59796, Q8TED1, Q96SL4
GPx-6
Manually annotated by BRENDA team
B4YA17
highly expressed in pre-vitellogenic and mid-vitellogenic oocytes, while no expression is detected in late-vitellogenic oocytes
Manually annotated by BRENDA team
B4YA17
specifically expressed in shrimp ovaries, but not in other tissues
Manually annotated by BRENDA team
-
extremely highly expressed in ovary
Manually annotated by BRENDA team
H9AZT5, H9AZT6
highest mRNA expression in ovary, followed by pyloric caeca, heart, liver and brain
Manually annotated by BRENDA team
-
the intrinsically low level of Gpx activity in the islets sets up the beta cell as an organelle particularly susceptible to oxidative stress secondary to high levels of glucose. Adenoviral overexpression of Gpx increases Gpx activity and protects islets against adverse effects of ribose
Manually annotated by BRENDA team
-
intraperitoneal fat, high expression of pGPx
Manually annotated by BRENDA team
O75715, P18283, P59796, Q8TED1, Q96SL4
GPx-3
Manually annotated by BRENDA team
-
GPx-3 is secreted into the plasma
Manually annotated by BRENDA team
-
GPx3 is widely inactivated in prostate cancer cells
Manually annotated by BRENDA team
-
expression is observed in the membranes of vacuoles contained in prostate secretions as well as in the endothelium of arterioles and venules
Manually annotated by BRENDA team
H9AZT5, H9AZT6
highest mRNA expression in ovary, followed by pyloric ceca, heart, liver and brain
Manually annotated by BRENDA team
H9AZT5, H9AZT6
highest mRNA expression in pyloric ceca, followed by brain, heart and liver
Manually annotated by BRENDA team
Q6ESJ0
main expression
Manually annotated by BRENDA team
-
GPx is detected in the tubulo-alveolar structures of the gland's parenchyma, in the apical part of secreting epithelial cells of the gland's alveoli, and in the vascular endothelium of blood vessels found in interstitial connective tissue
Manually annotated by BRENDA team
-
weak expression of pGPx
Manually annotated by BRENDA team
Q5XJZ8
isozyme n-GPx-4 is specifically expressed in late spermatocytes
Manually annotated by BRENDA team
-
weak expression of pGPx
Manually annotated by BRENDA team
-
GPx4 is highly expressed in testis
Manually annotated by BRENDA team
-
GPx3 is exclusively expressed in thyrocytes
Manually annotated by BRENDA team
additional information
Q8MNZ6, Q8MPM5
the mRNA is present throughout the nematode second stage juvenile and is particularly abundant in metabolically active tissues including the genital primordia
Manually annotated by BRENDA team
additional information
-
GPX transcript is absent from both immature and mature oocytes
Manually annotated by BRENDA team
additional information
-
not detected at all in muscle, brain or liver
Manually annotated by BRENDA team
additional information
-
glial cells are devoid of GPx4
Manually annotated by BRENDA team
additional information
-
in general, isoform Gpx4b mRNA expression exceeds that of isoform Gpx4a in all tissues with the exception of the pyloric caeca. The ratio of gpx4b/gpx4a is highest in ovary, and lowest in pyloric caeca
Manually annotated by BRENDA team
additional information
-
not detected in heart, brain, gut, muscle, epidermis, and testis
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
of alveolar macrophages
Manually annotated by BRENDA team
H9AZT5, H9AZT6
higher GPx activities are observed in cytosolic fractions than mitochondrial fractions in both the olfactory and liver tissues
Manually annotated by BRENDA team
-
co-localization with BiP
Manually annotated by BRENDA team
A4L7I9
full-length fusion protein with enhanced green fluorescent protein is localised to the trans-Golgi.The secretion of the enzyme into the culture medium requires an amino-terminal signal peptide
-
Manually annotated by BRENDA team
A4L7I9
full-length fusion protein with enhanced green fluorescent protein is localised to the trans-Golgi.The secretion of the enzyme into the culture medium requires an amino-terminal signal peptide
Manually annotated by BRENDA team
O75715, P18283, P59796, Q8TED1, Q96SL4
GPx-4
Manually annotated by BRENDA team
-
inner membrane: 95%, outer membrane: 2.5%
Manually annotated by BRENDA team
H9AZT5, H9AZT6
higher GPx activities are observed in cytosolic fractions than mitochondrial fractions in both the olfactory and liver tissues
Manually annotated by BRENDA team
additional information
-
not in peroxisomes
-
Manually annotated by BRENDA team
additional information
Q8MNZ6, Q8MPM5
the protein has a functional signal peptide that targets the protein for secretion
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Clostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10)
Clostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10)
Clostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10)
Clostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10)
Clostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10)
Clostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10)
Clostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10)
Clostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10)
Clostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
19000
Q5XJZ8
isozyme c-GPx4, SDS-PAGE
685439
19500
-
gel filtration
396644
20000
-
SDS-PAGE
688924
20000
-
SDS-PAGE
690120
21000
-
gel filtration
671114
21510
P00435
electrospray ionization mass spectrometry; MALDI-TOF mass spectrometry
684392
21800
P00435
theoretical molecular mass of alkylated GPx
684392
21900
P83645
SDS-PAGE
685921
22000
P00435
SDS-PAGE
684392
24000
-
SDS-PAGE, truncated and active form of snGPx produced by cleavage at the N-terminal end
685333
34000
-
SDS-PAGE, inactive full-length enzyme
685333
34000
Q5XJZ8
isozyme n-GPx4, SDS-PAGE
685439
62000
-
gel filtration
396640
70000
-
gel filtration
396642
75000 - 85500
-
gel filtration
396610
75000 - 85500
-
gel filtration
396611
75000 - 85500
-
sedimentation and diffusion constants, partial specific volume, sedimentation equilibrium centrifugation
396614
75000 - 85500
-
gel filtration
396616
75000 - 85500
-
gel filtration
396618, 396619
75000 - 85500
-
sedimentation equilibrium centrifugation
396623
80000
-
gel filtration
396637
85000
-
gel filtration
673160
88000
-
Toyopearl HW-65 column chromatography
695719
90000 - 100000
-
gel filtration
396643
92000
-
SDS-PAGE
685411
100000
-
gel filtration
396609
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 23000, SDS-PAGE
?
-
x * 44000, SDS-PAGE
?
A0EYM2
x * 26400, calculated from sequence
?
-
x * 20900, calculated from amino acid sequence
?
T1RK19
x * 21350, calculated from amino acid sequence
homodimer
-
alpha2, 2 * 35000, SDS-PAGE
homodimer
O75715, P18283, P59796, Q8TED1, Q96SL4
GPx-8
homotetramer
-
-
homotetramer
-
4 * 23000, SDS-PAGE
homotetramer
-
alpha4, 4 * 21900, nucleotide sequence, SDS-PAGE
homotetramer
-
alpha4, 4 * 23100, SDS-PAGE
homotetramer
-
alpha4, 4 * 29000, SDS-PAGE
homotetramer
-
alpha4, 4 * 17000-20000, SDS-PAGE, amino acid composition
homotetramer
-
alpha4, 4 * 16000, SDS-PAGE
homotetramer
-
alpha4, 4 * 22000-23000, SDS-PAGE
monomer
-
1 * 20000, SDS-PAGE
monomer
-
1 * 19500, SDS-PAGE
monomer
-
Gpx3 is a monomer in solution at a concentration of about 2 mg/ml
monomer
Q5XJZ8
1 * 19000, isozyme c-GPx4, SDS-PAGE, 1 * 34000, isozyme c-GPx4, SDS-PAGE
tetramer
-
4 * 24000, SDS-PAGE
monomer
-
1 * 19400, estimated from SDS-PAGE
additional information
-
fibrillar aggregates show the same level of activity as native protein
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
-
proteolytic modification
Q8MNZ6, Q8MPM5
the protein has a functional signal peptide that targets the protein for secretion
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure
-
hanging-drop vapour-diffusion method, 2.6 A resolution. The crystals are triclinic and belong to space group P1, with unit-cell parameters a = 38.187, b = 43.372, c = 56.870 A, alpha = 71.405, beta = 73.376, gamma = 89.633
-
sitting drop vapor diffusion method, using 0.2 M LiSO4,0.2 M sodium acetate, 24% (w/v) PEG 8000, pH 4.5 for mutant enzyme U43C and 0.2 M NaH2PO4, 0.1 M MES, 32% (w/v) PEG-MME 5000, pH 6.0 for mutant enzyme U43S
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2
-
complete inactivation but reactivation by neutralization
396605
5
-
extremely unstable below
396616
6.8 - 8
-
a decrease in pH to 6.8 or an increase to 8.0 drastically suppresses the enzyme activity, since at these pH values, glutathione peroxidase becomes unstable
695719
7 - 10
-
-
396611
additional information
-
unstable at low pH
396643
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 25
-
freezing the preparation with subsequent thawing with a gradual increase in temperature from 0C to 25C causes a 75% loss of the enzyme activity compared to the initial level
695719
30 - 70
-
glutathione peroxidase activity is retained after incubation at 30C for 3.5 h and at 40C for 1.5 h, an increase in the incubation temperature to 50C and 70C leads to inactivation of the enzyme within 1 h and 40 min, respectively
695719
100
-
complete inactivation
396605
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stabilization by glutathione or dithiothreitol
-
dithiothreitol restores about 50% of the S-nitro-N-acetyl-DL-penicillamine inhibited enzyme
-
selenoprotein P protects endothelial cells from oxidative damage by stimulation of glutathione peroxidase expression and activity
-
stabilization by 2-mercaptoethanol
-
stabilization by glutathione or dithiothreitol
-
stable to H2O2, linoleic hydroperoxide, peroxidizing linolate, methylethylketone peroxide
-
stabilization by glutathione or dithiothreitol
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Glycerol
-
in the presence of glycerol, the enzyme activity decreases by 40% of the initial value if the enzyme is stored at 0-4C for 24 h and by 90% if the enzyme is frozen
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
autooxidation, reactivation by glutathione
-
396611
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-30C, GSH or DTT in the buffer, stable for several months
-
4C, precipitated in 2.5 M potassium phosphate
-
4C, more than 4 months
-
4C, 50 mM potassium phosphate buffer, pH 7.2, 10% ethanol
-
-20C, 10 mM phosphate buffer, pH 7.0, 1 mM EDTA, 0.1 M NaCl, 50% glycerol
-
0-4C, 50 mM potassium phosphate buffer (pH 7.4), 24 h, no loss of activity
-
4C, 1 month, less than 50% loss of activity
-
frozen, 1 mM dithiothreitol, 3 months stable, or 2 mM glutathione, 1 month, 15-22% loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Superdex 75 gel filtration and DEAE column chromatography
P67878
Ni-NTA resin column chromatography and Superdex 75 gel filtration
Q9VZQ8
nickel-agarose column chromatography
-
oxidized and reduced form
-
Superdex 75 gel filtration and DEAE column chromatography; Superdex 75 gel filtration and DEAE column chromatography
Q1PBM0, Q1PBM1
ammonium sulfate precipitation and Mono P HR 5/20 column chromatography
-
DEAE-cellulose column chromatography, Sephadex G-25 gel filtration, and Toyopearl HW-65 column chromatography
-
Superdex 75 gel filtration and DEAE column chromatography
Q86EQ5
glutathione-Sepharose column chromatography and HiTrap SP FF column chromatography
-
Superdex 75 gel filtration and DEAE column chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Spodoptera frugiperda cells
-
expressed in Escherichia coli JM109 cells
Q9VZQ8
expression in Escherichia coli
-
expressed in Escherichia coli
-
expressed in Mus musculus
-
expressed in PC-3 cells, LNCaP cells, and DU-145 cells
-
expression constructs encoding full-length (1-201) and C-terminal deletion (1-100) versions of human GPX1 (Sec47Cys) for overexpression in HEK-293 cells
-
expression in MCF-7c1 cells
-
human enzyme expressed in transgenic mice. Overexpression of glutathione peroxidase with two isoforms of superoxide dismutase protects mouse islets from oxidative injury and improves islet graft function
-
overexpression of Gpx4 in mice
-
the human GPx-1 gen is expressed in transgenic mice
-
the recombinant plasmid is introduced into Agrobacterium tumefaciens strain Ag11 amd transformation of Lycopersicon esculentum is performed
-
expressed in HEK-293T cells
-
expression in Escherichia coli
-
Strep-tagged Gpx3 is expressed in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
-
overexpression in bacteria
-
expression in fish cell line
A4L7I9
expression in Escherichia coli
-
overexpression of TcGPXI in transfected parasites confers increased resistance to exogenous hydroperoxides
-
-
A0EYM2
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme activity in the serum of late-lactation cows is 2fold higher compared to dry cows and 4fold higher than in first-calving heifers and multiparous cows in early lactation
-
in the brain, enzyme activity is significantly inhibited (51% after 28 days) during methylmercury exposure. In the case of co-exposure to methylmercury and selenium, inhibition of enzyme activity is less pronounced (25% at day 28)
-
the enzyme expression level shows a 4 and a 2.6fold decrease after 3 and 7 days of exposure to polychlorinated biphenyl 77, respectively
H2CSR7
no variation of enzyme expression is observed after a 1-day exposure to polychlorinated biphenyl 77
H2CSR7
GPx-3 is induced by MG132 in HUVEC cells with an exponential increase in GPx-3 mRNA up to 120fold of control levels within 48 h. GPx-3 is still upregulated by a factor of 3-4 even after 72 and 96 h of proteasome inhibition. HAEC cells upregulate GPx-3 by more than 40fold in response to MG132. Proteasome inhibition clearly induces GPx-3 in HAoSMCs by a factor of 18
-
selenium treatment (0.01-0.03 mg/ml) significantly increases glutathione peroxidases activity in young barley seedlings
-
adult male Swiss mice treated with 40 mg/ml methylmercury for 21 days show about 50% decrease in GPx activity in the brain
-
in liver, by 24 h, exposure to alow dose of Cd causes 13% loss of Gpx4a expression. At higher dose, Cd leads to 40% decrease in Gpx4a expression. Longer exposure periods cause about 20% loss of liver Gpx4a expression by low Cd dose
H9AZT5, H9AZT6
olfactory isoform Gpx4b mRNA expression is not extensively modulated by presence of cadmium ions. In liver, by 24 h, exposure to alow dose of Cd causes 18% loss of Gpx4b expression. At higher dose, Cd leads to 37% decrease in Gpx4b expression. Longer exposure periods cause about 22% loss of liver Gpx4b expression by low Cd dose, whereas at higher Cd exposures, a 33% loss in Gpx4b expression is observed
H9AZT5, H9AZT6
after Vibrio anguillarum and white spot syndrome virus challenge, glutathione peroxidase transcripts both in hemocytes and hepatopancreas increases about 3fold in the first 6 h and 3 h, respectively
T1RK19
the level of mRNA significantly increases 6 h after challenge with Vibrio harveyi, Staphyloccocus aureus or white spot syndrome virus
-
a selenium deficient diet decreases glutathione reductase activity
-
feeding selenium-enriched Agaricus bisporus (0.001 mg Se/g feed) increases expression and activity of glutathione peroxidase-1 in rat colon by 1.65fold
P04041
feeding selenium-enriched Agaricus bisporus (0.001 mg Se/g feed)increases expression of glutathione peroxidase-2 in rat colon by 2.3fold
P04041
Vibrio challenge can significantly upregulate the mRNA expression of the enzyme, and the highest expression level (6.5fold) is detected at 24 h post infection with 6.5fold increase compared with that in the control group. Enzyme expression is significantly induced by 0.02 and 0.04 mg l-1 Cd (both 2.9fold after 24 h) and 0.01 and 0.02 mg l-1 Cu (2.7fold after 24 h and 1.6fold at 96 h, respectively). The mRNA expression is maximally induced (6.29fold) at 96 h post challenge with 0.05 mg l-1 benzo[a]pyrene
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C74A
Q9VZQ8
mutation results in a decline of specific activity
N136A
Q9VZQ8
mutation results in a dramatic decline of specific activity
N136D
Q9VZQ8
mutation results in not detectable specific activity
N136H
Q9VZQ8
mutation results in a dramatic decline of specific activity
S14A
-
mutant shows reduced selenium content and strongly reduced glutathione peroxidase activity
U43C
-
inactive
U43S
-
inactive
N40A
Q9VZQ8
mutation results in a decline of specific activity
additional information
-
full-length (1-201) and C-terminal deletion (1-100) versions of human GPX1 (Sec47Cys), full-length FLAG-GPX1 is modified with O-GlcNAc, while the truncated FLAG-GPX1 is not, despite the fact that truncated GPX1 is still able to bind OGT. O-GlcNAcylation occurs on the C-terminal half of GPX1
S15A
-
mutant shows reduced selenium content and reduced glutathione peroxidase activity
additional information
-
the enzyme has potential therapeutic value as an antioxidant, but its pharmacological development is limited because the enzyme uses a selenocysteine as its catalytic group and it is difficult to generate selenium-containing proteins with traditional recombinant DNA technology. Rat theta-class glutathione transferase T2-2 (rGST T2-2) presents an ideal scaffold for the design of a novel glutathione peroxidase catalyst because it binds GSH and contains a serine close to substrate binding site, which can be chemically modified to bind selenium. The modified Se-rGST T2-2 efficiently catalyzes the reduction of hydrogen peroxide, and the glutathione peroxidase activity surpasses the activities of some natural glutathione peroxidases
additional information
-
GPX1 modified with O-GlcNAc on its C-terminus, cell lysate of VSMCs treated with the O-GlcNAcase inhibitor PUGNAc
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
activity is important in predicting tissue redox state
medicine
H9AZT5, H9AZT6
in liver, by 24 h, exposure to alow dose of Cd causes 13% loss of Gpx4a expression. At higher dose, Cd leads to 40% decrease in Gpx4a expression. Longer exposure periods cause about 20% loss of liver Gpx4a expression by low Cd dose
medicine
H9AZT5, H9AZT6
olfactory isoform Gpx4b mRNA expression is not extensively modulated by presence of cadmium ions. In liver, by 24 h, exposure to alow dose of Cd causes 18% loss of Gpx4b expression. At higher dose, Cd leads to 37% decrease in Gpx4b expression. Longer exposure periods cause about 22% loss of liver Gpx4b expression by low Cd dose, whereas at higher Cd exposures, a 33% loss in Gpx4b expression is observed
analysis
-
activity is important in predicting tissue redox state
medicine
-
the enzyme has potential therapeutic value as an antioxidant, but its pharmacological development is limited because the enzyme uses a selenocysteine as its catalytic group and it is difficult to generate selenium-containing proteins with traditional recombinant DNA technology