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Information on EC 1.11.1.9 - glutathione peroxidase and Organism(s) Schistosoma mansoni and UniProt Accession Q00277

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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:
Schistosoma mansoni
UNIPROT: Q00277
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Word Map
The taxonomic range for the selected organisms is: Schistosoma mansoni
The enzyme appears in selected 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
phospholipid glutathione peroxidase
-
phospholipid hydroperoxide Gpx
-
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
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
H2O2 + GSH
H2O + GSSG
show the reaction diagram
tert-butyl hydroperoxide + 2 GSH
tert-butyl alcohol + GSSG + H2O
show the reaction diagram
-
-
-
?
cumene hydroperoxide + GSH
?
show the reaction diagram
-
-
-
-
?
H2O2 + GSH
H2O + GSSG
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
H2O2 + GSH
H2O + GSSG
show the reaction diagram
-
-
-
?
tert-butyl hydroperoxide + 2 GSH
tert-butyl alcohol + GSSG + H2O
show the reaction diagram
-
-
-
?
cumene hydroperoxide + GSH
?
show the reaction diagram
-
-
-
-
?
H2O2 + GSH
H2O + GSSG
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
selenium
Gpx is a selenium-containing enzyme
selenium
-
selenocysteine
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GPX1_SCHMA
169
0
19471
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
19400
1 * 19400, estimated from SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 19400, estimated from SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
glutathione-Sepharose column chromatography and HiTrap SP FF column chromatography
Superdex 75 gel filtration and DEAE column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
overexpression in bacteria
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mei, H.; Thakur, A.; Schwartz, J.; Lo Verde, P.T.
Expression and characterization of glutathione peroxidase activity in the human blood fluke Schistosoma mansoni
Infect. Immun.
64
4299-4306
1996
Schistosoma mansoni
Manually annotated by BRENDA team
Bae, Y.; Cai, G.; Kim, S.; Zo, Y.; Kong, Y.
Modular evolution of glutathione peroxidase genes in association with different biochemical properties of their encoded proteins in invertebrate animals
BMC Evol. Biol.
9
72
2009
Homo sapiens (P07203), Homo sapiens (P22352), Brugia pahangi (P67878), Schistosoma mansoni (Q00277), Paragonimus westermani (Q1PBM0), Paragonimus westermani (Q1PBM1), Schistosoma japonicum (Q86EQ5)
Manually annotated by BRENDA team
Dimastrogiovanni, D.; Anselmi, M.; Miele, A.E.; Boumis, G.; Petersson, L.; Angelucci, F.; Nola, A.D.; Brunori, M.; Bellelli, A.
Combining crystallography and molecular dynamics: The case of Schistosoma mansoni phospholipid glutathione peroxidase
Proteins
78
259-270
2009
Schistosoma mansoni (Q00277), Schistosoma mansoni
Manually annotated by BRENDA team