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Information on EC 1.8.5.1 - glutathione dehydrogenase (ascorbate) and Organism(s) Homo sapiens

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Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
Synonyms
mt-ii, dehydroascorbate reductase, dhar, metallothionein-1, gsto1-1, dioscorin, metallothionein-2, dha reductase, dhar1, dhar2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DasA reductase
-
-
-
-
dehydroascorbate reductase
dehydroascorbic acid reductase
-
-
-
-
dehydroascorbic reductase
-
-
-
-
dehydrogenase, glutathione (ascorbate)
-
-
-
-
DHA reductase
DHA-R
-
-
-
-
GDOR
-
-
-
-
glutathione dehydroascorbate reductase
-
-
-
-
glutathione-dependent dehydroascorate reductase
-
-
-
-
glutathione:dehydroascorbic acid oxidoreductase
-
-
-
-
GSH-DHAR
-
-
-
-
GSH:DHA-oxidoreductase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
glutathione:dehydroascorbate oxidoreductase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9026-38-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 glutathione + dehydroascorbate
glutathione disulfide + ascorbate
show the reaction diagram
-
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
show the reaction diagram
-
-
-
r
glutathione + dehydroascorbate
GSSG + ascorbate
show the reaction diagram
-
-
-
?
GSH + dehydroascorbate
GSSG + ascorbate
show the reaction diagram
-
-
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.21 - 1.3
dehydroascorbate
4.18 - 11.8
glutathione
3.5 - 3.8
GSH
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0047 - 5.27
dehydroascorbate
0.0058 - 0.0293
glutathione
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.13
allelic variant A140/E155/E208 of GSTO1-1, dehydroascorbate as substrate, at 30°C
0.21
allelic variant D140/DELTAE155/K208 of GSTO1-1, dehydroascorbate as substrate, at 30°C
0.25
allelic variant A140/DELTAE155/E208 of GSTO1-1, dehydroascorbate as substrate, at 30°C
1.77
-
-
11.6
allelic variant D142 of GSTO2-2, dehydroascorbate as substrate, at 30°C
13.8
allelic variant N142 of GSTO2-2, dehydroascorbate as substrate, at 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GSTO2_HUMAN
243
0
28254
Swiss-Prot
other Location (Reliability: 2)
GSTO1_HUMAN
241
0
27566
Swiss-Prot
other Location (Reliability: 4)
V9HWG9_HUMAN
241
0
27566
TrEMBL
other Location (Reliability: 4)
B2R983_HUMAN
241
0
27539
TrEMBL
other Location (Reliability: 4)
Q5TA02_HUMAN
200
0
23341
TrEMBL
Mitochondrion (Reliability: 5)
B4DU59_HUMAN
166
0
19344
TrEMBL
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32000
-
1 * 32000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 32000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of isoform GSTO1 in complex with ascoric acid, to 1.7 A resolution. Ascorbic acid binds in the glutathione site, where the glutamyl moiety of GSH binds and stacks against a conserved aromatic residue, F34
crystal structures of isoform GSTO2-2, stabilized through site-directed mutagenesis of cysteine residues to serines and determined at 1.9 A resolution in the presence and absence of glutathione
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A140D
no alteration in specific activity compared to the wild type enzyme
E155
the deletion causes a 2-3fold increase in the specific activity with each substrate and a significant decrease in the enzyme's heat stability, it is also linked to abnormal arsenic excretion patterns
E208K
no alteration in specific activity compared to the wild type enzyme
N142D
no effect on the specific activity of the enzyme with any substrate
Y34A
complete loss of activity
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
53
at 53°C, both GSTO2-2 isoforms show a similar loss of activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-agarose affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
GSTO2-2, using 8 mM urea
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
significant association with the age-at-onset of Alzheimer's disease and Parkinson's disease
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bigley, R.; Riddle, M.; Layman, D.; Stankova, L.
Human cell dehydroascorbate reductase. Kinetic and functional properties
Biochim. Biophys. Acta
659
15-22
1981
Homo sapiens
Manually annotated by BRENDA team
Basu, S.; Som, S.; Deb, S.; Mukherjee, D.; Chatterjee, I.B.
Dehydroascorbic acid reduction in human erythrocytes
Biochem. Biophys. Res. Commun.
90
1335-1340
1979
Homo sapiens
Manually annotated by BRENDA team
Xu, D.P.; Washburn, M.P.; Sun, G.P.; Wells, W.W.
Purification and characterization of a glutathione dependent dehydroascorbate reductase from human erythrocytes
Biochem. Biophys. Res. Commun.
221
117-121
1996
Homo sapiens
Manually annotated by BRENDA team
Schmuck, E.M.; Board, P.G.; Whitbread, A.K.; Tetlow, N.; Cavanaugh, J.A.; Blackburn, A.C.; Masoumi, A.
Characterization of the monomethylarsonate reductase and dehydroascorbate reductase activities of Omega class glutathione transferase variants: implications for arsenic metabolism and the age-at-onset of Alzheimers and Parkinsons diseases
Pharmacogenet. Genomics
15
493-501
2005
Homo sapiens (P78417), Homo sapiens
Manually annotated by BRENDA team
Zhou, H.; Brock, J.; Liu, D.; Board, P.G.; Oakley, A.J.
Structural insights into the dehydroascorbate reductase activity of human omega-class glutathione transferases
J. Mol. Biol.
420
190-203
2012
Homo sapiens (P78417), Homo sapiens (Q9H4Y5), Homo sapiens
Manually annotated by BRENDA team