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Literature summary for 3.4.21.92 extracted from

  • Jennings, L.D.; Bohon, J.; Chance, M.R.; Licht, S.
    The ClpP N-terminus coordinates substrate access with protease active site reactivity (2008), Biochemistry, 47, 11031-11040.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.21.92

Cloned(Commentary)

Cloned (Comment) Organism
plasmid encoding ClpPDELTAN transformed into Escherichia coli SG1146GaBL21(DE3) cells Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information in the absence of ClpA, deletion of the ClpP N-terminus increases the initial degradation rate of large peptide substrates 5-15fold. ClpPDELTAN accelerates degradation of insulin chain B and induces distinct rapid and slow phases of product formation. The distinct slow phase of product formation is eliminated by the addition of hydroxylamine, truncation of the N-terminus leads to stabilization of the acyl-enzyme intermediate Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.04
-
 insulin chain B wild-type ClpP Escherichia coli
0.2167
-
 insulin chain B ClpPDELTAN Escherichia coli
0.3167
-
 insulin chain B ClpAP Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
ClpP-His6, ClpA and ClpPDELTAN Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
insulin chain B + H2O
-
 Escherichia coli ?
-
 ?
additional information the ClpP N-terminus acts as a gate controlling substrate access to the active sites, binding of ClpA opens this gate, allowing substrate entry and formation of the acyl-enzyme intermediate, and closing of the N-terminal gate stimulates acyl-enzyme hydrolysis Escherichia coli ?
-
 ?
N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O initial degradation rate is the same within error for wild-type ClpP, ClpAP, and ClpPDELTAN Escherichia coli ?
-
 ?
ssrA-dabsyl + H2O initial rate of degradation of this intermediate-sized substrate is 3fold faster with ClpAP as compared to wild-type Clp and 5fold faster with ClpPDELTAN as compared to wild-type ClpP Escherichia coli ?
-
 ?

Synonyms

Synonyms Comment Organism
ClpA
-
 Escherichia coli
ClpAP
-
 Escherichia coli
ClpP
-
 Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.33
-
 insulin chain B ClpAP Escherichia coli
0.34
-
 insulin chain B ClpPDELTAN Escherichia coli
0.35
-
 insulin chain B wild-type ClpP Escherichia coli