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Literature summary for 3.4.25.2 extracted from

  • Yakamavich, J.A.; Baker, T.A.; Sauer, R.T.
    Asymmetric nucleotide transactions of the HslUV protease (2008), J. Mol. Biol., 380, 946-957.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.25.2

Organism

Organism UniProt Comment Textmining
Escherichia coli
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-
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
HslUV
-
 Escherichia coli
HslUV protease
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP ATP binding and hydrolysis are critical for protein degradation by HslUV, an AAA+ machine containing one or two HslU ATPases and the HslV peptidase. Asymmetric mechanism of ATP binding and hydrolysis. Molecular contacts between HslU and HslV vary dynamically throughout the ATPase cycle. Nucleotide binding controls HslUV assembly and activity. Binding of a single ATP allows HslU to bind HslV, whereas additional ATPs must bind HslU to support substrate recognition and to activate ATP hydrolysis, which powers substrate unfolding and translocation Escherichia coli