BRENDA - Enzyme Database

The rate-limiting step of sulfiredoxin is associated with the transfer of the gamma-phosphate of ATP to the sulfinic acid of overoxidized typical 2-Cys peroxiredoxins

Roussel, X.; Boukhenouna, S.; Rahuel-Clermont, S.; Branlant, G.; FEBS Lett. 585, 574-578 (2011)

Data extracted from this reference:

KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.8.98.2
0.125
-
ATP
pH 7.0, 30°C
Saccharomyces cerevisiae
1.8.98.2
0.13
-
gamma-S-ATP
pH 7.0, 30°C
Saccharomyces cerevisiae
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.8.98.2
Saccharomyces cerevisiae
-
-
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.8.98.2
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
the rate-limiting step of the reaction is associated with the chemical process of transfer of the gamma-phosphate of ATP to the sulfinic acid. Two pKapp values of 6.2 and 7.5 of the bell-shaped pH-rate profile correspond to the gamma-phosphate of ATP, and to an acid-base catalyst, respectively
725010
Saccharomyces cerevisiae
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
-
-
?
1.8.98.2
peroxiredoxin-(S-hydroxy-S-oxocysteine) + gamma-S-ATP + 2 R-SH
-
725010
Saccharomyces cerevisiae
peroxiredoxin-(S-hydroxycysteine) + ADP + thiophosphate + R-S-S-R
-
-
-
?
Turnover Number [1/s]
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.8.98.2
0.016
-
gamma-S-ATP
wild-type, pH 7.0, 30°C
Saccharomyces cerevisiae
1.8.98.2
0.03
-
ATP
wild-type, pH 7.0, 30°C
Saccharomyces cerevisiae
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.8.98.2
0.125
-
ATP
pH 7.0, 30°C
Saccharomyces cerevisiae
1.8.98.2
0.13
-
gamma-S-ATP
pH 7.0, 30°C
Saccharomyces cerevisiae
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.8.98.2
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
the rate-limiting step of the reaction is associated with the chemical process of transfer of the gamma-phosphate of ATP to the sulfinic acid. Two pKapp values of 6.2 and 7.5 of the bell-shaped pH-rate profile correspond to the gamma-phosphate of ATP, and to an acid-base catalyst, respectively
725010
Saccharomyces cerevisiae
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
-
-
?
1.8.98.2
peroxiredoxin-(S-hydroxy-S-oxocysteine) + gamma-S-ATP + 2 R-SH
-
725010
Saccharomyces cerevisiae
peroxiredoxin-(S-hydroxycysteine) + ADP + thiophosphate + R-S-S-R
-
-
-
?
Turnover Number [1/s] (protein specific)
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.8.98.2
0.016
-
gamma-S-ATP
wild-type, pH 7.0, 30°C
Saccharomyces cerevisiae
1.8.98.2
0.03
-
ATP
wild-type, pH 7.0, 30°C
Saccharomyces cerevisiae