3.4.25.2: HslU-HslV peptidase
This is an abbreviated version!
For detailed information about HslU-HslV peptidase, go to the full flat file.
Reaction
ATP-dependent cleavage of peptide bonds with broad specificity. =
Synonyms
AAA+ HslUV protease, AAA+ protease HslUV, ATP-dependent protease, ATP-dependent protease hslV, ClpQ, ClpQY, ClpYQ, ClpYQ complex, ClpYQ protease, CodW, CodW-CodX, heat shock protein hslV, HslU ATPase, HslU chaperone, HslU/HslV, HslUV, HslUV complex, HslUV protease, HslUV protease-chaperone complex, HslV, HslV peptidase, HslV protease, HslV-HslU, hslVU, HslVU ATP-dependent protease, HslVU protease, LINF_150005800, PfHslUV, T01.006
ECTree
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Inhibitors
Inhibitors on EC 3.4.25.2 - HslU-HslV peptidase
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benzyloxycarbonyl-Ile-Glu(tert-butyl)-Ala-Leu-al
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0.001 mM, almost complete inhibition of peptidase activity, no inhibition of hydrolysis of insulin B-chain or other polypeptide substrates
benzyloxycarbonyl-Leu-Leu-norvalinal
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0.004 mM, inhibits hydrolysis of both benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin and insulin B-chain to a similar extent
NLVS
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in the presence of ATP, the proteasome inhibitor markedly increases the interaction between HslV and HslU and causes the activation of the HslU ATPase
ATP
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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
lactacystin
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irreversible, much greater inhibition of the degradation of insulin B-chain than on peptide hydrolysis
lactacystin
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in the presence of ATP, the proteasome inhibitor markedly increases the interaction between HslV and HslU and causes the activation of the HslU ATPase
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preincubation with followed by inactivation of dithiothreitol causes inhibition of peptide hydrolysis
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the I125-labeled nitrophenyl derivative 125iodo-NIP-Leu-Leu-Leu vinyl sulfone covalently modifies and inhibits HslV, but only in presence of HslU and ATP
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additional information
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enzyme inactivation by 7.5% SDS and 10% v/v 2-mercaptoethanol
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additional information
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protein binding, e.g. of Escherichia coli ClpS, SspB, or DegS PDZ domain polypeptides, to the C-terminus of substrates selectively slows HslUV degradation, the inhibition affects an early step in degradation. Synergistic effects of N- and C-terminal blocking
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additional information
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PSI, a classical proteasome inhibitor, does not influence the co-expression level of HslV and proteasome 20 in strain Be-78; PSI, a classical proteasome inhibitor, influences the co-expression level of HslV and proteasome 20 in strain Be-62
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