1.8.1.14: CoA-disulfide reductase

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

Reaction

2 CoA +

Synonyms

BACoADR, BB0728, CoA disulfide reductase, CoA-disulfide reductase (NADH), CoA-disulfide reductase (NADH2), CoADR, coenzyme A disulfide reductase, coenzyme A disulphide reductase, coenzyme A-disulfide reductase, EC 1.6.4.10, NADH-dependent coenzyme A disulfide reductase, NADH2:CoA-disulfide oxidoreductase, NADH:CoA-disulfide oxidoreductase, PH0572

ECTree

     1 Oxidoreductases

         1.8 Acting on a sulfur group of donors

             1.8.1 With NAD⁺ or NADP⁺ as acceptor

                1.8.1.14 CoA-disulfide reductase

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Results	in table
1995	AA Sequence
1	CAS Registry Number
8	Cloned(Commentary)
37	Cofactor
8	Crystallization (Commentary)
5	General Information
7	Inhibitors
8	kcat/KM [mM/s]
7	Ki Value [mM]
27	KM Value [mM]
2	Molecular Weight [Da]
5	Natural Substrates/ Products (Substrates)
25	Organism
2	Pathway
27	PDB ID
1	pH Optimum
12	Protein Variants
10	Purification (Commentary)
2	Reaction
3	Reaction Type
23	Reference
2	Source Tissue
4	Specific Activity [micromol/min/mg]
42	Substrates and Products (Substrate)
8	Subunits
48	Synonyms
1	Systematic Name
1	Temperature Optimum [°C]
35	Turnover Number [1/s]

Engineering

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Engineering on EC 1.8.1.14 - CoA-disulfide reductase

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PROTEIN VARIANTS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

Y367/Y425F

Bacillus anthracis

-

inactive mutant enzyme

685242

Y367F

2 entries

Y367F/Y425F

Bacillus anthracis

-

inactive

685242

Y425F

2 entries

Y65A/Y66A/P67G/H367G

2 entries

C43S

Staphylococcus aureus

Q2FIA5

the enzyme has ca. 0.03% activity relative to the wild type enzyme

724355

Y361F

Staphylococcus aureus

Q2FIA5

the mutant shows increased catalytic efficiency compared to the wild type enzyme

724355

Y361F/Y419F

Staphylococcus aureus

Q2FIA5

the mutant shows reduced catalytic efficiency compared to the wild type enzyme

724355

Y419F

Staphylococcus aureus

Q2FIA5

the mutant shows reduced catalytic efficiency compared to the wild type enzyme

724355

Y367F

Bacillus anthracis

-

kcat for NADH is 3.9fold lower than wild-type value, kcat for NADPH is 5.6fold lower than wild-type value

685242

Y367F

Bacillus anthracis

-

the mutant is 18% as active as wild type enzyme

685242

Y425F

Bacillus anthracis

-

kcat for NADH is 30fold lower than wild-type value, kcat for NADPH is 93fold lower than wild-type value

685242

Y425F

Bacillus anthracis

-

the mutant is 1% as active as wild type enzyme

685242

Y65A/Y66A/P67G/H367G

Pyrococcus horikoshii

O58308

the structure of the quadruple mutant shows a widened substrate channel, which is supported by a fourfold increase in kcat for the NAD(P)H-dependent reduction of CoA disulfide and enhanced activity toward the substrate at lower temperatures

764676

Y65A/Y66A/P67G/H367G

Pyrococcus horikoshii ATCC 700860

-

the structure of the quadruple mutant shows a widened substrate channel, which is supported by a fourfold increase in kcat for the NAD(P)H-dependent reduction of CoA disulfide and enhanced activity toward the substrate at lower temperatures

-