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Literature summary for 3.4.25.2 extracted from

  • Lee, J.W.; Park, E.; Bang, O.; Eom, S.H.; Cheong, G.W.; Chung, C.H.; Seol, J.H.
    Nucleotide triphosphates inhibit the degradation of unfolded proteins by HslV peptidase (2007), Mol. Cells, 23, 252-257.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
ATP inhibits the degradation of unfolded proteins by HslV. This inhibitory effect of ATP is markedly diminished by substitution of the Arg86 residue located in the apical pore of HslV with Gly, suggesting that interaction of ATP with the Arg residue blocks access of unfolded proteins to the proteolytic chamber of HslV Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information HslVU is an ATP-dependent protease consisting of two heat shock proteins, the HslU ATPase and HslV peptidase. In the reconstituted enzyme, HslU stimulates the proteolytic activity of HslV by one to two orders of magnitude, while HslV increases the rate of ATP hydrolysis by HslU several-fold. HslV alone can efficiently degrade certain unfolded proteins, such as unfolded lactalbumin and lysozyme prepared by complete reduction of disulfide bonds, but not their native forms. HslV alone cleaves a lactalbumin fragment sandwiched by two thioredoxin molecules, indicating that it can hydrolyze the internal peptide bonds of lactalbumin. Uncomplexed HslV is inactive under normal conditions, but can degrade unfolded proteins when the ATP level is low, as it is during carbon starvation Escherichia coli ?
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Synonyms

Synonyms Comment Organism
hslVU ATP-dependent protease consisting of two heat shock proteins, the HslU ATPase and HslV peptidase Escherichia coli