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Literature summary for 3.6.4.10 extracted from

  • Wawrzynow, A.; Wojtkowiak, D.; Marszalek, J.; Banecki, B.; Jonsen, M.; Graves, B.; Georgopoulos, C.; Zylicz, M.
    The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone (1995), EMBO J., 14, 1867-1877.
    View publication on PubMedView publication on EuropePMC
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Activating Compound

Activating Compound Comment Organism Structure
lambdaO
-
 Escherichia coli

Cloned(Commentary)

Cloned (Comment) Organism
gene coding for ClpX sequenced Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.5
-
 ATP ClpX Escherichia coli

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-
Escherichia coli
-
-
-
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
ClpX Escherichia coli
DnaK Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
ATP + H2O = ADP + phosphate highly diverse group of enzymes that perform many functions that are similar to those of chaperonins. They comprise a number of heat-shock-cognate proteins. They are also active in clathrin uncoating and in the oligomerization of actin Bacillus subtilis
a
ATP + H2O = ADP + phosphate highly diverse group of enzymes that perform many functions that are similar to those of chaperonins. They comprise a number of heat-shock-cognate proteins. They are also active in clathrin uncoating and in the oligomerization of actin Escherichia coli
a
ATP + H2O = ADP + phosphate highly diverse group of enzymes that perform many functions that are similar to those of chaperonins. They comprise a number of heat-shock-cognate proteins. They are also active in clathrin uncoating and in the oligomerization of actin Saccharomyces cerevisiae
a

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
bona fide chaperone
-
 Escherichia coli
ClpX heat-shock protein
-
 Escherichia coli
DnaK
-
 Escherichia coli
DnaK chaperone
-
 Escherichia coli
heat shock protein GroEl
-
 Escherichia coli
Hsp100
-
 Saccharomyces cerevisiae
MecB protein
-
-