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Literature summary for 3.4.21.92 extracted from

  • Cordova, J.C.; Olivares, A.O.; Shin, Y.; Stinson, B.M.; Calmat, S.; Schmitz, K.R.; Aubin-Tam, M.E.; Baker, T.A.; Lang, M.J.; Sauer, R.T.
    Stochastic but highly coordinated protein unfolding and translocation by the ClpXP proteolytic machine (2014), Cell, 158, 647-658.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A6H1
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information protease ClpXP unfolds most domains by a single pathway, with kinetics that depend on the native fold and structural stability. Subsequent translocation or pausing occurs at rates that vary with the sequence of the unfolded substrate. During translocation, ClpXP does not exhibit a sequential pattern of step sizes, supporting a fundamentally stochastic reaction, but a mechanism of enzymatic memory results in short physical steps being more probable after short steps and longer physical steps being more likely after longer steps, allowing the enzyme to run at different speeds. Two ATP-hydrolysis events can drive more than two power strokes. Solution proteolysis is many times slower than predicted from single-molecule results Escherichia coli ?
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Synonyms

Synonyms Comment Organism
ClpX
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Escherichia coli