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1.8.4.2: protein-disulfide reductase (glutathione)

This is an abbreviated version!
For detailed information about protein-disulfide reductase (glutathione), go to the full flat file.

Word Map on EC 1.8.4.2

Reaction

2 glutathione +

protein-disulfide
=
glutathione-disulfide
+
protein-dithiol

Synonyms

BbdC, BdbD, C1orf31, CatA protein, ccdA associated thiol-disulfide oxidoreductase, COA6, DcbA, desulfothioredoxin, DIP1880, disulfide bond-forming thiol-disulfide oxidoreductase, disulphide interchange enzyme, DsbA, DsbA1, DsbA2, Dtrx, ERp57, GIT, glutathione-insulin transhydrogenase, glutathione-protein disulfide oxidoreductase, GRX1, GRX2, GRX3, GRX5, GRX6, GrxS12, GSH-dependent protein disulfide oxidoreductase, GSH-insulin transhydrogenase, HP_0231, insulin reductase, mcrophage migration inhibitory factor-2, MdbA, MdbACm, membrane-bound thiol-disulfide oxidoreductase, Mif-2, More, protein disulfide reductase (glutathione), protein disulfide transhydrogenase, protein-disulfide interchange enzyme, protein-disulfide isomerase/oxidoreductase, RCAP_rcc01743, reductase, protein disulfide (glutathione), ResA, SdbA, SGO_2006, SpyM18_2037, StoA, Streptococcus disulfide bond protein A, TDOR, thiol disulfide oxidoreductase, thiol-disulfide oxidoreductase, thiol-protein disulphide oxidoreductase, thiol:disulfide oxidoreductase, thiol:protein-disulfide oxidoreductase, WhiB1, WhiB1/Rv3219, YkuV, YMR244C-A

ECTree

     1 Oxidoreductases
         1.8 Acting on a sulfur group of donors
             1.8.4 With a disulfide as acceptor
                1.8.4.2 protein-disulfide reductase (glutathione)

Crystallization

Crystallization on EC 1.8.4.2 - protein-disulfide reductase (glutathione)

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallized at 25°C using the hanging-drop vapour-diffusion method, crystals belong to the space group I222 or I2(1)2(1)2(1), with unit-cell parameters a = 90.59, b = 102.43, c = 128.96 A
-
hanging-drop vapour diffusion
-
to 1.77 A resolution. The structure harbors a thioredoxin-like domain and an extended alpha-helical domain
purified recombinant enzyme MdbA, sitting drop vapor diffusion technique, a well solution containing 31.4% PEG 8000, 150 mM citrate buffer, pH 5.5 is used, 4-16 °C, 10 days, X-ray diffraction structure determination and analysis at 1.2 A, molecular replacement using the Corynebacterium diphtheriae MdbA structure (PDB ID 5C00) as the starting model
-
homology modeling.Csteine residues, Cys58 and Cys95 come in close proximity in the tertiary structure with pKa value 9. The residues are involved in the disulfide oxidoreductase catalytic activity