oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
electron transfer activity
Cellular component
cytoplasm
cytosol
mitochondrial matrix
mitochondrion
extracellular exosome
external side of plasma membrane
Biological process
nucleobase-containing small molecule interconversion
glutathione metabolic process
cell redox homeostasis
cellular oxidant detoxification
cellular response to oxidative stress
electron transport chain
Sources:Amigo / QuickGO
Orthologs
Species
Human
Mouse
Entrez
2936
14782
Ensembl
ENSG00000104687
ENSMUSG00000031584
UniProt
P00390
P47791
RefSeq (mRNA)
NM_001195104 NM_000637 NM_001195102 NM_001195103
NM_010344
RefSeq (protein)
NP_000628 NP_001182031 NP_001182032 NP_001182033
NP_034474
Location (UCSC)
Chr 8: 30.68 – 30.73 Mb
Chr 8: 34.14 – 34.19 Mb
PubMed search
[3]
[4]
Wikidata
View/Edit Human
View/Edit Mouse
Glutathione reductase (GR) also known as glutathione-disulfide reductase (GSR) is an enzyme that in humans is encoded by the GSR gene. Glutathione reductase (EC 1.8.1.7) catalyzes the reduction of glutathione disulfide (GSSG) to the sulfhydryl form glutathione (GSH), which is a critical molecule in resisting oxidative stress and maintaining the reducing environment of the cell.[5][6][7] Glutathione reductase functions as dimeric disulfide oxidoreductase and utilizes an FAD prosthetic group and NADPH to reduce one molar equivalent of GSSG to two molar equivalents of GSH:
General reaction catalyzed by glutathione reductase
The glutathione reductase is conserved between all kingdoms. In bacteria, yeasts, and animals, one glutathione reductase gene is found; however, in plant genomes, two GR genes are encoded. Drosophila and trypanosomes do not have any GR at all.[8] In these organisms, glutathione reduction is performed by either the thioredoxin or the trypanothione system, respectively.[8][9]
^ abcGRCh38: Ensembl release 89: ENSG00000104687 – Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000031584 – Ensembl, May 2017
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Cite error: The named reference GSH Review was invoked but never defined (see the help page).
^Meister A (November 1988). "Glutathione metabolism and its selective modification". J. Biol. Chem. 263 (33): 17205–8. doi:10.1016/S0021-9258(19)77815-6. PMID 3053703.
^Mannervik B (August 1987). "The enzymes of glutathione metabolism: an overview". Biochem. Soc. Trans. 15 (4): 717–8. doi:10.1042/bst0150717. PMID 3315772.
^ abKanzok SM, Fechner A, Bauer H, Ulschmid JK, Müller HM, Botella-Munoz J, Schneuwly S, Schirmer R, Becker K (2001). "Substitution of the thioredoxin system for glutathione reductase in Drosophila melanogaster". Science. 291 (5504): 643–6. Bibcode:2001Sci...291..643K. doi:10.1126/science.291.5504.643. PMID 11158675.
^Krauth-Siegel RL, Comini MA (2008). "Redox control in trypanosomatids, parasitic protozoa with trypanothione-based thiol metabolism". Biochim Biophys Acta. 1780 (11): 1236–48. doi:10.1016/j.bbagen.2008.03.006. PMID 18395526.
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enzymology, a methylarsonate reductase (EC 1.20.4.2) is an enzyme that catalyzes the chemical reaction methylarsonate + 2 glutathione ⇌ {\displaystyle \rightleftharpoons...
members of the disulfide oxidoreductase family like glutathionereductase and thioredoxin reductase. The remaining unbound arsenic (≤ 10%) accumulates...
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Global Information
