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Literature summary for 3.6.4.10 extracted from

  • Sehorn, M.G.; Slepenkov, S.V.; Witt, S.N.
    Characterization of two partially unfolded intermediates of the molecular chaperone DnaK at low pH (2002), Biochemistry, 41, 8499-8507.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
Asn-Asp-Leu-Leu-Leu-Thr-Gly peptide NRLLLTG, 5fold and 2fold increase in ATPase activity at pH 7.0 and pH 9.0, respectively Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O Escherichia coli
-
ADP + phosphate
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
DnaK
-
Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information kcat for ATP approx. 0.0008, 0.0025 and 0.002 at pH 4.5, pH 7.0 and pH 9.0, respectively, in the presence of peptide NRLLLTG Escherichia coli

pH Range

pH Minimum pH Maximum Comment Organism
4.5 9 no ATPase activity below pH 4.5 Escherichia coli