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The enzyme appears in viruses and cellular organisms
Synonyms
glutathione-cystine transhydrogenase, gsh-cystine transhydrogenase,
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GSH-cystine transhydrogenase
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NADPH-dependent GSH-cystine transhydrogenase
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transhydrogenase, glutathione-cystine
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2 glutathione + cystine = glutathione disulfide + 2 cysteine
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glutathione:cystine oxidoreductase
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beta-hydroxyethyl disulfide + GSH
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cystine + GSH
cysteine + GSSG
D-cystine + 2 GSH
2 D-cysteine + GSSG
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diacetyl-L-cystine + GSH
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dimethyl disulfide + GSH
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dithiodiglycolic acid + GSH
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GSSG + GSH
GSSG + GSH
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homocystine + GSH
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L-cystine + GSH
L-cysteine + GSSG
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L-cystine diamide + GSH
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L-cystinyldiglycine + GSH
L-Cys-Gly-Gly + GSSG
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lipoic acid oxidized + GSH
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additional information
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cystine + GSH
cysteine + GSSG
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cystine + GSH
cysteine + GSSG
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additional information
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inactive with albumin and kreatin
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inactive with: insulin and other proteins
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additional information
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at low substrate concentration the reaction rate is greater with L-cystine than with any of the other substances
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additional information
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at low substrate concentration the reaction rate is greater with L-cystine than with any of the other substances
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additional information
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at low substrate concentration the reaction rate is greater with L-cystine than with any of the other substances
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cystine + GSH
cysteine + GSSG
cystine + GSH
cysteine + GSSG
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cystine + GSH
cysteine + GSSG
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61.6
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beta-hydroxyethyldisulfide
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8.6
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pH 7.8 chosen for the assay to achieve smaller nonenzymatic rate
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6 - 8.5
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pH 6.0: 10% of activity maximum, pH 8.5: activity maximum
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additional information
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no activity in brush border
brenda
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supernatant fraction
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24 h, complete inactivation
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crude state, quite labile to heat above 54°C
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denaturation, crude state
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ammonium sulfate, 1 M, complete stabilization, 6 days at 20°C
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cystine, alone: no stabilization, in addition to glutathione: increases stabilizing effect
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ethylene glycol, 10%, stabilizes
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glutathione stabilizes, stabilizing effect increased by cystine
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glycerol, no stabilization
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-20°C, pH 5.8, 1 mM glutathione, several months
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4°C, 24 h, complete inactivation, crude state
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Nagai, S.; Black, S.
A thiol-disulfide transhydrogenase from yeast
J. Biol. Chem.
243
1942-1947
1968
Saccharomyces cerevisiae
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Nagai, S.
Thiol-disulfide transhydrogenase (yeast)
Methods Enzymol.
17B
510-515
1971
Saccharomyces cerevisiae
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Minoda, Y.; Kurane, R.; Yamada, K.
Thiol-disulfide transhydrogenase from baker's yeast and a new method for the direct assay of an enzyme-catalyzed thiol-disulfide interchange activity
Agric. Biol. Chem.
37
2511-2516
1973
Saccharomyces cerevisiae
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Wendell, P.L.
Distribution of glutathione reductase and detection of glutathione-cystine transhydrogenase in rat tissues
Biochim. Biophys. Acta
159
179-181
1968
Rattus norvegicus
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States, B.; Segal, S.
Distribution of glutathione-cystine transhydrogenase activity in subcellular fractions of rat intestinal mucosa
Biochem. J.
113
443-444
1969
Rattus norvegicus
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States, B.; Segal, S.
Interrelationship of glutathione-cystine transhydrogenase and glutathione reductase in developing rat intestine
Biochem. J.
132
623-631
1973
Rattus norvegicus
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1.8.4.4 glutathione-cystine transhydrogenase
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