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Information on EC 1.11.1.9 - glutathione peroxidase

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EC Tree
     1 Oxidoreductases
         1.11 Acting on a peroxide as acceptor
             1.11.1 Peroxidases
                1.11.1.9 glutathione peroxidase
IUBMB Comments
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).
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This record set is specific for:
UNIPROT: Q9VZQ8
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Word Map
The enzyme appears in viruses and cellular organisms
Synonyms
glutathione peroxidase, gpx, gsh-px, ebselen, gshpx, gpx-1, gsh peroxidase, glutathione peroxidase 1, plasma glutathione peroxidase, selenium-dependent glutathione peroxidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6P229
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-
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ARMEP24
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-
-
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AtGPX1
-
-
-
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Cellular glutathione peroxidase
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-
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Cuticular glycoprotein GP29
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-
-
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DI29
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-
-
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EGLP
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-
-
-
Epididymis-specific glutathione peroxidase-like protein
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-
-
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Extracellular glutathione peroxidase
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-
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Gastrointestinal glutathione peroxidase
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-
-
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GP30
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-
-
-
GPRP
-
-
-
-
GPX
-
-
-
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GSH peroxidase
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-
-
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GSHPx-GI
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-
-
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Major androgen-regulated protein
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-
-
-
Major surface antigen GP29
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-
-
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Nt-SubC08
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-
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Odorant-metabolizing protein RY2D1
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-
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peroxidase, glutathione
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-
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reduced glutathione peroxidase
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-
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Salt-associated protein
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selenium-glutathione peroxidase
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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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).
CAS REGISTRY NUMBER
COMMENTARY hide
9013-66-5
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
phosphatidylcholine hydroperoxide + thioredoxin
?
show the reaction diagram
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-
-
?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.24
mutant enzyme N136A, using thioredoxin and phosphatidylcholine hydroperoxide as substrates
0.4
mutant enzyme N136H, using thioredoxin and phosphatidylcholine hydroperoxide as substrates
14.38
wild type enzyme, using thioredoxin and phosphatidylcholine hydroperoxide as substrates
4.29
mutant enzyme N40A, using thioredoxin and phosphatidylcholine hydroperoxide as substrates
5.81
mutant enzyme C74A, using thioredoxin and phosphatidylcholine hydroperoxide as substrates
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q9VZQ8_DROME
169
0
18676
TrEMBL
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C74A
mutation results in a decline of specific activity
N136A
mutation results in a dramatic decline of specific activity
N136D
mutation results in not detectable specific activity
N136H
mutation results in a dramatic decline of specific activity
N40A
mutation results in a decline of specific activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA resin column chromatography and Superdex 75 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli JM109 cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tosatto, S.C.; Bosello, V.; Fogolari, F.; Mauri, P.; Roveri, A.; Toppo, S.; Flohe, L.; Ursini, F.; Maiorino, M.
The catalytic site of glutathione peroxidases
Antioxid. Redox Signal.
10
1515-1526
2008
Drosophila melanogaster (Q9VZQ8)
Manually annotated by BRENDA team