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Literature summary for 3.4.25.2 extracted from

  • Huang, H.; Goldberg, A.L.
    Proteolytic activity of the ATP-dependent protease HslVU can be uncoupled from ATP hydrolysis (1997), J. Biol. Chem., 272, 21364-21372.
    View publication on PubMed
Search for more literature for 3.4.25.2

Metals/Ions

Metals/Ions Comment Organism Structure
CaCl2 allows some peptidase and caseinase activity in the absence of any nucleotide, however Ca2+ abolishes ATP hydrolysis and prevents further activation by ATP and 5'-adenylyl beta,gamma-imidodiphosphate Escherichia coli
Cs+ stimulates 4-6fold the peptidase activity with 5'-adenylyl beta,gamma-imidodiphosphate present and eliminates the time lag for activation, no stimulatory effect with ATP Escherichia coli
KCl stimulates 4-6fold the peptidase activity with 5'-adenylyl beta,gamma-imidodiphosphate present and eliminates the time lag for activation, no stimulatory effect with ATP Escherichia coli
MgCl2 allows some peptidase and caseinase activity in the absence of any nucleotide Escherichia coli
MnCl2 allows some peptidase and caseinase activity in the absence of any nucleotide, however Mn2+ abolishes ATP hydrolysis and prevents further activation by ATP and 5'-adenylyl beta,gamma-imidodiphosphate Escherichia coli
NH4+ stimulates 4-6fold the peptidase activity with 5'-adenylyl beta,gamma-imidodiphosphate present and eliminates the time lag for activation, no stimulatory effect with ATP Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin + H2O
-
 Escherichia coli benzyloxycarbonyl-GGL + 7-amino-4-methylcoumarin
-
 ?
casein + H2O
-
 Escherichia coli ?
-
 ?

Subunits

Subunits Comment Organism
More HslVU is a ATP-dependent protease composed of two multimeric complexes: the hslU ATPase and the HslV peptitase Escherichia coli

Cofactor

Cofactor Comment Organism Structure
5'-adenylyl beta,gamma-imidotriphosphate can support peptide hydrolysis, but only after an initial time lag not seen with ATP. This delay decreases at higher temperatures and with higher HslV or HslU concentrations and is eliminated by preincubation of HslV and HslU together Escherichia coli
5'-adenylyl beta,gamma-imidotriphosphate can support peptide hydrolysis, but only after an initial time lag not seen with ATP. This delay decreases at higher temperatures and with higher HslV or HslU concentrations and is eliminated by preincubation of HslV and HslU together. Supports hydrolysis of casein and other polypeptides only 20% as well as ATP. But in presence of K+, Cs+ or NH4+, activation of casein degradation is even better than that by ATP, although it is not hydrolyzed Escherichia coli
ATP ATP concentrations that activate hydrolysis of benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin are 50-100fold lower than those necessary for degradation of proteins, e.g. casein. ATP binding to a high affinity site triggers the formation of an active state capable of peptide cleavage, although ATP hydrolysis facilitates this process Escherichia coli