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Literature summary for 3.4.25.2 extracted from

  • Lee, J.W.; Park, E.; Jeong, M.S.; Jeon, Y.J.; Eom, S.H.; Seol, J.H.; Chung, C.H.
    HslVU ATP-dependent protease utilizes maximally six among twelve threonine active sites during proteolysis (2009), J. Biol. Chem., 284, 33475-33484.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression of His-tagged wild-type and mutant enzymes in BW25113 DELTAhslVU::kan cells Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information construction of mixed dodecamers having varied numbers of HslV and T1A subunits, and of a series of HslV dodecamers containing different numbers of active sites showing that HslV with only 6 active sites is sufficient to support full catalytic activity, a further reduction of the number of active sites leads to a proportional decrease in activity. Substrate-mediated stabilization of the HslV-HslU interaction remains unchanged until the number of the active sites is decreased to 6 but is gradually compromised upon further reduction. Deletion of Thr1 causes a dramatic increase in affinity between HslV and HslU Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
lactacystin in the presence of ATP, the proteasome inhibitor markedly increases the interaction between HslV and HslU and causes the activation of the HslU ATPase Escherichia coli
NLVS in the presence of ATP, the proteasome inhibitor markedly increases the interaction between HslV and HslU and causes the activation of the HslU ATPase Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
SulA + H2O Escherichia coli degradation ?
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged wild-type and mutant enzymes from BW25113 DELTAhslVU::kan cells by nickel affinity chromatography Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
ATP-dependent cleavage of peptide bonds with broad specificity. model for a proteolytic cycle by HslVU protease, overview Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alpha-casein + H2O degradation Escherichia coli ?
-
?
Arc + H2O degradation Escherichia coli ?
-
?
Arc mutant I137A + H2O monomeric mutant, degradation Escherichia coli ?
-
?
additional information HslVU is a bacterial ATP-dependent protease consisting of hexameric HslU ATPase and dodecameric HslV protease. HslV uses the N-terminal threonine as the active site residue. HslV has 12 active sites among the 14beta-subunits that can potentially contribute to proteolytic activity, but only 6 active sites are sufficient to support full catalytic activity. Substrate-mediated stabilization of the HslV-HslU interaction Escherichia coli ?
-
?
SulA + H2O degradation Escherichia coli ?
-
?
SulA + H2O recombinant substrate, produced as maltose-binding fusion protein and cleaved by factorXa Escherichia coli ?
-
?

Subunits

Subunits Comment Organism
More mathematical models for stochastically assembled HslV dodecamers, overview Escherichia coli
oligomer HslVU is a bacterial ATP-dependent protease consisting of hexameric HslU ATPase and dodecameric HslV protease. HslV has 12 active sites among the 14beta-subunits that can potentially contribute to proteolytic activity Escherichia coli

Synonyms

Synonyms Comment Organism
HslV protease
-
Escherichia coli
HslVU ATP-dependent protease
-
Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP dependent on Escherichia coli