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1.8.1.8: protein-disulfide reductase

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

Word Map on EC 1.8.1.8

Reaction

protein-dithiol
+
NAD(P)+
=
protein-disulfide
+
NAD(P)H
+
H+

Synonyms

AhpF, disulfide reductase, EC 1.6.4.4, ERdj5, ERp16, glutaredoxin, HvTrxh2, insulin-glutathione transhydrogenase, LpdA, MA3736, MA_1658, MdrA, methanoredoxin, More, NAD(P)H:protein-disulfide oxidoreductase, NADH-linked disulfide reductase, panthethine 4'4-diphosphate-specific reductase, PDI reductase, PDO, PfPDO, PH1130 protein, PhDsb, protein disulfide isomerase reductase, protein disulfide oxidoreductase, protein disulfide reductase, protein-disulfide oxidoreductase, protein-disulfide reductase (NAD(P)H), reductase, protein disulfide, thiol-disulfide oxidoreductase, TON_0319, TTC0486, WhiB1, WhiB1/Rv3219

ECTree

     1 Oxidoreductases
         1.8 Acting on a sulfur group of donors
             1.8.1 With NAD+ or NADP+ as acceptor
                1.8.1.8 protein-disulfide reductase

Temperature Stability

Temperature Stability on EC 1.8.1.8 - protein-disulfide reductase

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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
-
flexibility increases with the pH, with a high value at pH 7.0
20
-
the C terminal active site at 20°C shows a reduced flexibility at all pH values, while at 100°C the flexibility increases with the pH, with a high value at pH 7.0
60
-
10 min, stable
70
-
10 min, complete inactivation
90
-
3 h, no loss of activity
additional information
-
pH affects differently the thermostability of alpha-helices and beta-sheets