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.

Reaction

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

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Results	in table
14437	AA Sequence
1	CAS Registry Number
10	Cloned(Commentary)
21	Cofactor
6	Crystallization (Commentary)
363	Disease/ Diagnostics
1	General Information
2	General Stability
13	Inhibitors
2	Ki Value [mM]
17	KM Value [mM]
1	Localization
2	Metals/Ions
11	Molecular Weight [Da]
4	Natural Substrates/ Products (Substrates)
1	Organic Solvent Stability
35	Organism
82	PDB ID
4	pH Optimum
2	pH Range
4	pH Stability
3	pI Value
1	Protein Variants
10	Purification (Commentary)
2	Reaction
8	Reaction Type
34	Reference
17	Source Tissue
2	Specific Activity [micromol/min/mg]
7	Storage Stability
53	Substrates and Products (Substrate)
17	Subunits
56	Synonyms
1	Systematic Name
2	Temperature Optimum [°C]
6	Temperature Stability [°C]
12	Turnover Number [1/s]

pH Stability

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pH Stability on EC 1.8.1.8 - protein-disulfide reductase

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pH STABILITY

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

10

Pyrococcus furiosus

-

at pH 10.0 the protein undergoes partial unfolding. Decrease in alpha-helix content at pH 10.0, whereas the beta-sheet content remains unaltered. At pH 5.8, pH not optimum for the activity, and at 10°C and 100°C, the alpha2 helix region, where the N-terminal active site is localized, is less flexible than at pH 7.0 and pH 10.0. 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

745638

5.5

Pisum sativum

-

5°C or 22°C, irreversible inactivation

437710

5.8

Pyrococcus furiosus

-

the residual amide II band intensity is higher at pH 5.8 than at pH 7.0 suggesting that the acidic pH induces a more compact structure At pH 5.8, pH not optimum for the activity, and at 10°C and 100°C, the alpha2 helix region, where the N-terminal active site is localized, is less flexible than at pH 7.0 and pH 10.0

745638

7

Pyrococcus furiosus

-

the residual amide II band intensity is higher at pH 5.8 than at pH 7.0 suggesting that the acidic pH induces a more compact structure. At pH 5.8, pH not optimum for the activity, and at 10°C and 100°C, the alpha2 helix region, where the N-terminal active site is localized, is less flexible than at pH 7.0 and pH 10.0

745638