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

BRENDA support

Literature summary for 3.4.25.2 extracted from

  • Yoo, S.J.; Seol, J.H.; Seong, I.S.; Kang, M.S.; Chung, C.H.
    ATP binding, but not its hydrolysis, is required for assembly and proteolytic activity of the HslVU protease in Escherichia coli (1997), Biochem. Biophys. Res. Commun., 238, 581-585.
    View publication on PubMed
Search for more literature for 3.4.25.2

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
-
 ?
Insulin B-chain + H2O HslVU degrades insulin B-chain even more rapidly in the presence of ATPgammaS than with ATP Escherichia coli ?
-
 ?
additional information ATP-binding, but not its hydrolysis, is essential for assembly and proteolytic activity of HslVU Escherichia coli ?
-
 ?

Subunits

Subunits Comment Organism
More HslVU is an ATP-dependent protease consisting of two multimeric components: the HslU ATPase and the HslV peptidase Escherichia coli

Cofactor

Cofactor Comment Organism Structure
adenosine 5'-(alpha,beta-methylene)triphosphate HslVU degrades insulin B-chain more rapidly in the presence of ATPgammaS than with ATP Escherichia coli
ATP ATP-binding, but not its hydrolysis, is essential for assembly and proteolytic activity of HslVU. The ability of ATP and its analogs in supporting the proteolytic activity is closely correlated with their ability in supporting the oligomerization of HslU and the formation of the HslVU complex Escherichia coli
ATPgammaS HslVU degrades insulin B-chain more rapidly in the presence of ATPgammaS than with ATP Escherichia coli
beta,gamma-Imido-ATP supports proteolytic activity to an extent less than 10% of that seen with ATP Escherichia coli