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Literature summary for 1.8.98.2 extracted from

  • Roussel, X.; Boukhenouna, S.; Rahuel-Clermont, S.; Branlant, G.
    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 (2011), FEBS Lett., 585, 574-578.
    View publication on PubMed
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KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.125
-
 ATP pH 7.0, 30°C Saccharomyces cerevisiae
0.13
-
 gamma-S-ATP pH 7.0, 30°C Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 Saccharomyces cerevisiae peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
 ?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + gamma-S-ATP + 2 R-SH
-
 Saccharomyces cerevisiae peroxiredoxin-(S-hydroxycysteine) + ADP + thiophosphate + R-S-S-R
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.016
-
 gamma-S-ATP wild-type, pH 7.0, 30°C Saccharomyces cerevisiae
0.03
-
 ATP wild-type, pH 7.0, 30°C Saccharomyces cerevisiae