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1.8.5.1: glutathione dehydrogenase (ascorbate)

This is an abbreviated version!
For detailed information about glutathione dehydrogenase (ascorbate), go to the full flat file.

Word Map on EC 1.8.5.1

Reaction

2 glutathione +

dehydroascorbate
=
glutathione disulfide
 +
ascorbate

Synonyms

At1g19570, At1g75270, At5g16710, AtDHAR, AtDHAR1, AtDHAR2, AtDHAR3, CrDHAR1, DasA reductase, dehydroascorbate reductase, dehydroascorbate reductase 2, dehydroascorbic acid reductase, dehydroascorbic reductase, dehydrogenase, glutathione (ascorbate), DHA reductase, DHA-R, DHAR, DHAR1, DHAR2, DHAR3, DHAR3a, DHAR4, DHAR5, dioscorin, GDOR, glutathione dehydroascorbate reductase, glutathione-dependent dehydroascorate reductase, glutathione:dehydroascorbic acid oxidoreductase, GRX1, GRX2, GSH-DHAR, GSH:DHA-oxidoreductase, GSTO, GSTO1, GSTO1-1, GSTO2, GSTO2-2, LcDHAR, metallothionein-1, metallothionein-2, More, MT-I, MT-II, nlGSTO, OsDHAR, OsDHAR1, PbDHAR, PgDHAR1, PtrDHAR1, PtrDHAR2, PtrDHAR3A, PtrDHAR3B, SPD1

ECTree

     1 Oxidoreductases
         1.8 Acting on a sulfur group of donors
             1.8.5 With a quinone or similar compound as acceptor
                1.8.5.1 glutathione dehydrogenase (ascorbate)

Crystallization

Crystallization on EC 1.8.5.1 - glutathione dehydrogenase (ascorbate)

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
isoform DHAr2 bound to glutathione, hanging drop vapor diffusion method, using 2.0 M ammonium sulfate, 0.1 M sodium acetate, pH 4.8
-
isozyme AtDHAR2, X-ray diffraction structure determination and analysis
in complex with acetate or glycerol
-
isozyme PgDHAR1, X-ray diffraction structure determination and analysis
purified recombinant full-length wild-type enzyme CrDHAR1 (amino acids 1-226), and mutants CrDHAR1DELTAN (amino acids 5-226) or CrDHAR1DELTAC (amino acids 1-218), sitting drop vapor diffusion method, mixing of protein solution with an equal volume of crystallization solution containing 0.1 M Tris-HCl, pH 8.0, and 2 M ammonium sulfate, 20°C, X-ray diffraction structure determination and analysis at 2.46-2.55 A resolution, molecular replacement method using the structure of reduced wild-type OsDHAR (5D9T) as search model, modeling
in complex with ascorbate, hanging drop vapor diffusion method, using
-
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
isozyme OsDHAR1, X-ray diffraction structure determination and analysis
native, ascorbate-bound, and glutathione-bound enzyme forms, hanging drop vapor diffusion method, using 0.15 M potassium bromide and 30% (w/v) PEG MME 2000
sitting drop vapor diffusion method, using 0.15 M potassium bromide, 30% (w/v) PEG MME 2000
the structure of the enzyme in complex with GSH and calcium, PDB ID 5D9X and determined at 1.68 A resolution, is analyzed
modeling of structure. Protein has a typical glutathione S-transferase structure containing a smaller thioredoxin-like N-terminal domain and a larger helical C-terminal domain
recombinant enzyme produced in Escherichia coli, crystallized by hanging-drop vapour-diffusion method
-