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Literature summary for 3.6.4.10 extracted from

  • Sugimoto, S.; Saruwatari, K.; Higashi, C.; Tsuruno, K.; Matsumoto, S.; Nakayama, J.; Sonomoto, K.
    In vivo and in vitro complementation study comparing the function of DnaK chaperone systems from halophilic lactic acid bacterium Tetragenococcus halophilus and Escherichia coli (2008), Biosci. Biotechnol. Biochem., 72, 811-822.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Escherichia coli
-
Tetragenococcus halophilus

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Tetragenococcus halophilus Q93R27
-
-
Tetragenococcus halophilus JCM 5888 Q93R27
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli
-
Tetragenococcus halophilus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O
-
Escherichia coli ADP + phosphate
-
?
ATP + H2O
-
Tetragenococcus halophilus ADP + phosphate
-
?
ATP + H2O
-
Tetragenococcus halophilus JCM 5888 ADP + phosphate
-
?

Synonyms

Synonyms Comment Organism
DnaK chaperone
-
Escherichia coli
DnaK chaperone
-
Tetragenococcus halophilus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information ATPase activity is enhanced by co-chaperones DnaJ and GrpE, more than 12fold stimulation is observed in the presence of each of these co-chaperones Escherichia coli
additional information
-
additional information ATPase activity is not stimulated by co-chaperones DnaJ and GrpE Tetragenococcus halophilus
0.00033
-
ATP at 20°C Tetragenococcus halophilus
0.0005
-
ATP at 20°C Escherichia coli
0.0037
-
ATP at 50°C Tetragenococcus halophilus
0.012
-
ATP at 50°C Escherichia coli
0.012
-
ATP at 50°C Tetragenococcus halophilus