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Information on EC 1.8.1.B1 - thioredoxin glutathione reductase and Organism(s) Mus musculus and UniProt Accession Q99MD6

for references in articles please use BRENDA:EC1.8.1.B1
preliminary BRENDA-supplied EC number
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This record set is specific for:
Mus musculus
UNIPROT: Q99MD6
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The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
Synonyms
thioredoxin glutathione reductase, smtgr, thioredoxin-glutathione reductase, tgrsec, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
thioredoxin-glutathione reductase
-
-
thioredoxin/glutathione reductase
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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
GSSG + NADPH + H+
GSH + NADP+
show the reaction diagram
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
show the reaction diagram
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
?
show the reaction diagram
-
-
-
-
?
glutathione disulfide + NADPH + H+
glutathione + NADP+
show the reaction diagram
-
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
show the reaction diagram
-
-
-
-
?
additional information
?
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-
TGR promotes isomerization of disulfide bonds formed between glutathione peroxidase 4 and certain sperm proteins, generating a 46-kDa species containing glutathione peroxidase 4 from high molecular weight nonspecific cross-links
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-
?
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
GSSG + NADPH + H+
GSH + NADP+
show the reaction diagram
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
much higher number of TGR transcripts in testis than in the rest of organs
Manually annotated by BRENDA team
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TGR is regulated by both selenium availability and selenocysteine tRNA status. This regulation is more pronounced in liver, whereas in testes, the expression level is only slightly affected
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TRXR3_MOUSE
652
0
71319
Swiss-Prot
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
small amounts of the soluble enzyme are obtained by purifying it from a large quantity of cells, in which protein synthesis is induced slowly for a period of 24 h at a low temperature
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant TGR is mostly insoluble when expressed in Escherichi coli, and neither cloning of the enzyme that contain various tags nor coexpression of TGR with chaperones increases its solubility
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Su, D.; Novoselov, S.V.; Sun, Q.A.; Moustafa, M.E.; Zhou, Y.; Oko, R.; Hatfield, D.L.; Gladyshev, V.N.
Mammalian selenoprotein thioredoxin/glutathione reductase: roles in disulfide bond formation and sperm maturation
J. Biol. Chem.
280
26491-26498
2005
Mus musculus
Manually annotated by BRENDA team
Sun, Q.A.; Su, D.; Novoselov, S.V.; Carlson, B.A.; Hatfield, D.L.; Gladyshev, V.N.
Reaction mechanism and regulation of mammalian thioredoxin/glutathione reductase
Biochemistry
44
14528-14537
2005
Bos taurus, Danio rerio, Gallus gallus, Homo sapiens, Mus musculus, no activity in Caenorhabditis elegans, no activity in Canis familiaris, no activity in Drosophila melanogaster, no activity in Sus scrofa, Pan troglodytes, Rattus norvegicus, Takifugu rubripes, Tetraodon nigroviridis, Xenopus laevis
Manually annotated by BRENDA team
Jurado, J.; Prieto-Alamo, M.J.; Madrid-Risquez, J.; Pueyo, C.
Absolute gene expression patterns of thioredoxin and glutaredoxin redox systems in mouse
J. Biol. Chem.
278
45546-45554
2003
Mus musculus (Q99MD6)
Manually annotated by BRENDA team
Dobrovolska, O.; Shumilina, E.; Gladyshev, V.N.; Dikiy, A.
Structural analysis of glutaredoxin domain of Mus musculus thioredoxin glutathione reductase
PLoS ONE
7
e52914
2012
Mus musculus (Q99MD6), Mus musculus
Manually annotated by BRENDA team