BRENDA - Enzyme Database
show all sequences of 1.8.1.10

Characterization of a NADPH-dependent coenzyme A-SS-glutathione reductase from yeast

Ondarza, R.N.; Abney, R.; Lopez-Colome, A.M.; Biochim. Biophys. Acta 191, 239-248 (1969)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
phosphate
25 mM, partially inhibits
Saccharomyces cerevisiae
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.2
-
CoA-glutathione
at pH 5.5 and a fixed value of 110 nmol NADPH
Saccharomyces cerevisiae
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
108000
-
sucrose density gradient ultracentrifugation
Saccharomyces cerevisiae
Organism
Organism
UniProt
Commentary
Textmining
Saccharomyces cerevisiae
-
strain ATCC 1946
-
Purification (Commentary)
Purification (Commentary)
Organism
143fold partial purification, separated from GSSG reductase activity, EC 1.6.4.2
Saccharomyces cerevisiae
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
-
Saccharomyces cerevisiae
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
CoA-glutathione + NADPH
-
395110
Saccharomyces cerevisiae
glutathione + CoA + NADP+
-
395110
Saccharomyces cerevisiae
ir
additional information
no reduction of CoASSCys, GSSCys or CysSSCys
395110
Saccharomyces cerevisiae
?
-
-
-
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
24
-
assay at
Saccharomyces cerevisiae
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
5.5
-
-
Saccharomyces cerevisiae
Cofactor
Cofactor
Commentary
Organism
Structure
NADPH
NADPH-dependent
Saccharomyces cerevisiae
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADPH
NADPH-dependent
Saccharomyces cerevisiae
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
phosphate
25 mM, partially inhibits
Saccharomyces cerevisiae
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.2
-
CoA-glutathione
at pH 5.5 and a fixed value of 110 nmol NADPH
Saccharomyces cerevisiae
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
108000
-
sucrose density gradient ultracentrifugation
Saccharomyces cerevisiae
Purification (Commentary) (protein specific)
Commentary
Organism
143fold partial purification, separated from GSSG reductase activity, EC 1.6.4.2
Saccharomyces cerevisiae
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
-
Saccharomyces cerevisiae
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
CoA-glutathione + NADPH
-
395110
Saccharomyces cerevisiae
glutathione + CoA + NADP+
-
395110
Saccharomyces cerevisiae
ir
additional information
no reduction of CoASSCys, GSSCys or CysSSCys
395110
Saccharomyces cerevisiae
?
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
24
-
assay at
Saccharomyces cerevisiae
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
5.5
-
-
Saccharomyces cerevisiae
Other publictions for EC 1.8.1.10
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
395111
delCardayre
Staphylococcus aureus coenzyme ...
Staphylococcus aureus, Staphylococcus aureus NCTC 8325
J. Biol. Chem.
273
5752-5757
1998
-
2
1
-
-
-
-
2
-
-
2
2
-
12
-
-
1
-
-
-
1
-
4
1
3
-
-
-
1
-
-
-
3
-
-
-
-
2
1
3
-
-
-
-
-
-
2
-
-
2
2
-
-
-
1
-
-
1
-
4
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
395105
Acuna
-
Distribution of GSSG- and CoAS ...
Rattus norvegicus
Temas Bioquim. Actual. (Pina, E. , Pena, A. , Chagoya de Sanchez, V. , eds. )
93
355-359
1978
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
10
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
10
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
395106
Loewen
Identification of a coenzyme A ...
Escherichia coli
Can. J. Biochem.
55
1019-1027
1977
-
-
-
-
-
-
-
-
-
-
-
1
-
3
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
395107
Eriksson
The nature of the enzymatic re ...
Rattus norvegicus
FEBS Lett.
39
296-300
1974
-
-
-
-
-
-
-
-
1
-
-
1
-
1
-
-
1
-
-
1
-
-
2
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
-
1
-
-
-
1
-
1
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
395108
Ondarza
CoAS-Sglutathione and GSSG red ...
Rattus norvegicus
Biochim. Biophys. Acta
341
162-171
1974
-
-
-
-
-
-
-
1
-
-
1
-
-
1
-
-
2
-
-
1
1
-
2
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
1
-
-
-
-
2
-
1
1
-
2
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
395012
Dyar
Rat liver levels of coenzyme A ...
Rattus norvegicus
Arch. Biochem. Biophys.
153
619-626
1972
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
1
2
1
2
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
2
1
2
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
395110
Ondarza
Characterization of a NADPH-de ...
Saccharomyces cerevisiae
Biochim. Biophys. Acta
191
239-248
1969
-
-
-
-
-
-
1
1
-
-
1
-
-
3
-
-
1
-
-
-
1
-
2
-
-
1
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
1
-
1
-
-
1
-
-
-
-
1
-
-
1
-
2
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-