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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

General Stability

General Stability on EC 1.8.1.8 - protein-disulfide reductase

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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme is highly piezostable. The effect of pressure on the molecule is not uniform and that different areas of the protein can have different local compressibility and resistance to high hydrostatic pressure. alpha-Helices are more sensitive than beta-sheets to pressure up to 5 kbar, whilst within 5.1-8.0 kbar the loss of eta-sheets is more pronounced than the loss of alpha-helices
-
The structure and thermal stability of the protein are analyzed under different conditions by Fourier transform infrared spectroscopy and Molecular Dynamics simulations. The effects of SDS, pH, and temperature on the protein structure are characterized. The data indicated that pD affects differently the thermostability of alpha-helices and beta-sheets, and that 0.5% or higher SDS concentration have a significant repercussion on the structure
-