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Literature summary for 3.4.25.2 extracted from

  • Yoo, S.J.; Seol, J.H.; Shin, D.H.; Rohrwild, M.; Kang, M.S.; Tanaka, K.; Goldberg, A.L.; Chung, C.H.
    Purification and characterization of the heat shock proteins HslV and HslU that form a new ATP-dependent protease in Escherichia coli (1996), J. Biol. Chem., 271, 14035-14040.
    View publication on PubMed
Search for more literature for 3.4.25.2

General Stability

General Stability Organism
rapid freezing and thawing inactivates Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
diisopropyl fluorophosphate 10 mM, about 70% inhibition Escherichia coli
dithiothreitol
-
 Escherichia coli
NEM preincubation with followed by inactivation of dithiothreitol causes inhibition of peptide hydrolysis Escherichia coli
phenylmethylsulfonyl fluoride 2 mM, about 70% inhibition Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
19000
-
 x * 19000, HslV protein, SDS-PAGE Escherichia coli
250000
-
 purified HslV in presence or absence of ATP, gel filtration Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Storage Stability

Storage Stability Organism
-70°C, stable for at least 1 month in presence of 20% glycerol and 1 mM dithiothreitol Escherichia coli
4°C rapid inactivation in absence of dithiothreitol Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin + H2O HslV alone cleaves to a much lesser extent than in presence of HslU Escherichia coli benzyloxycarbonyl-GGL + 7-amino-4-methylcoumarin
-
 ?
additional information HslV and HslU can function together as a novel ATP-dependent protease, the HslVU protease. Pure HslV is a weak peptidase degrading certain hydrophobic peptides. HslU dramatically stimulates peptide hydrolysis by HslV when ATP is present. With a 1:4 molar ratio of HslV to HslU, approximately a 200fold increase in peptide hydrolysis is observed. HslV stimulates the ATPase activity of HslU 2-4fold. CTP and dATP are slowly hydrolyzed by HslU and allow some peptide hydrolysis Escherichia coli ?
-
 ?
succinyl-LLVY-7-amido-4-methylcoumarin + H2O
-
 Escherichia coli succinyl-LLVY + 7-amino-4-methylcoumarin
-
 ?

Subunits

Subunits Comment Organism
? x * 19000, HslV protein, SDS-PAGE Escherichia coli
More HslVU protease is a two-component protease in which HslV harbors the peptidase activity, while HslU provides an essential ATPase activity Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP HslV and HslU can function together as a novel ATP-dependent protease, the HslVU protease. Pure HslV is a weak peptidase degrading certain hydrophobic peptides. HslU dramatically stimulates peptide hydrolysis by HslV when ATP is present. With a 1:4 molar ratio of HslV to HslU, approximately a 200fold increase in peptide hydrolysis is observed. HslV stimulates the ATPase activity of HslU 2-4fold. CTP and dATP are slowly hydrolyzed by HslU and allow some peptide hydrolysis Escherichia coli