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Literature summary for 3.4.21.92 extracted from

  • Shi, X.; Wu, T.; M Cole, C.; K Devaraj, N.; Joseph, S.
    Optimization of ClpXP activity and protein synthesis in an E. coli extract-based cell-free expression system (2018), Sci. Rep., 8, 3488 .
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
analysis development of a ClpXP protein degradation systemusing purified ClpXP in a cell-free transcription-translation system Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.000043
-
fEGFP-ssrA presence of adaptor protein SspB, pH 7.6, 30°C Escherichia coli
0.00056
-
fEGFP-ssrA absence of adaptor protein SspB, pH 7.6, 30°C Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A6G7
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
fEGFP-ssrA + H2O i.e. N-terminal His-tagged superfolder enhanced green fluorescent protein with the ssrA tag sequence at the C-terminus Escherichia coli ?
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0077
-
fEGFP-ssrA presence of adaptor protein SspB, pH 7.6, 30°C Escherichia coli
0.0083
-
fEGFP-ssrA absence of adaptor protein SspB, pH 7.6, 30°C Escherichia coli

General Information

General Information Comment Organism
physiological function purified ClpXP added to a cell-free transcription-translation system that uses Escherichia coli S30 cell extract, has very low proteolytic activity. Addition of exogenous ATP and an energy regeneration system improves activity Escherichia coli