Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.25.2 extracted from

  • Seol, J.H.; Yoo, S.J.; Shin, D.H.; Shim, Y.K.; Kang, M.S.; Goldberg, A.L.; Chung, C.H.
    The heat-shock protein HslVU from Escherichia coli is a protein-activated ATPase as well as an ATP-dependent proteinase (1997), Eur. J. Biochem., 247, 1143-1150.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
HslU HslV can slowly hydrolyze insulin B-chain, casein or carboxymethylated lactalbumin, but its activity is stimulated 20fold by HslU in presence of ATP Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
benzyloxycarbonyl-Ile-Glu(tert-butyl)-Ala-Leu-al 0.001 mM, almost complete inhibition of peptidase activity, no inhibition of hydrolysis of insulin B-chain or other polypeptide substrates Escherichia coli
benzyloxycarbonyl-Leu-Leu-norvalinal 0.004 mM, inhibits hydrolysis of both benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin and insulin B-chain to a similar extent Escherichia coli
lactacystin irreversible, much greater inhibition of the degradation of insulin B-chain than on peptide hydrolysis Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.014
-
Insulin B-chain pH 8, 37°C 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
-
?
carboxymethylated lactalbumin + H2O
-
Escherichia coli ?
-
?
casein + H2O
-
Escherichia coli ?
-
?
Insulin B-chain + H2O
-
Escherichia coli ?
-
?
additional information no hydrolysis of gamma-globulin, lysozyme and bovine serum albumin Escherichia coli ?
-
?

Cofactor

Cofactor Comment Organism Structure
ATP HslV can slowly hydrolyze insulin B-chain, casein or carboxymethylated lactalbumin, but its activity is stimulated 20fold by HslU in presence of ATP Escherichia coli