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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Cofactor
Cofactor on EC 3.4.25.2 - HslU-HslV peptidase
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adenosine 5'-(alpha,beta-methylene)triphosphate
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HslVU degrades insulin B-chain more rapidly in the presence of ATPgammaS than with ATP
ATPgammaS
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HslVU degrades insulin B-chain more rapidly in the presence of ATPgammaS than with ATP
beta,gamma-Imido-ATP
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supports proteolytic activity to an extent less than 10% of that seen with ATP
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the enzyme degrades SulA and the fusion protein of SulA and maltose-binding protein in presence of ATP but not with ATPgammaS
5'-adenylyl beta,gamma-imidotriphosphate
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can support peptide hydrolysis, but only after an initial time lag not seen with ATP. This delay decreases at higher temperatures and with higher HslV or HslU concentrations and is eliminated by preincubation of HslV and HslU together
5'-adenylyl beta,gamma-imidotriphosphate
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can support peptide hydrolysis, but only after an initial time lag not seen with ATP. This delay decreases at higher temperatures and with higher HslV or HslU concentrations and is eliminated by preincubation of HslV and HslU together. Supports hydrolysis of casein and other polypeptides only 20% as well as ATP. But in presence of K+, Cs+ or NH4+, activation of casein degradation is even better than that by ATP, although it is not hydrolyzed
ATP
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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
ATP
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ATP activates hydrolysis of benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin 150fold
ATP
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HslV and HslU can function together as a novel ATP-dependent protease, the HslVU protease. Pure HslV is a weak peptidase degrading certain hydrophobic peptides. HslU dramatically stimulates peptide hydrolysis by HslV when ATP is present. With a 1:4 molar ratio of HslV to HslU, approximately a 200fold increase in peptide hydrolysis is observed. HslV stimulates the ATPase activity of HslU 2-4fold. CTP and dATP are slowly hydrolyzed by HslU and allow some peptide hydrolysis
ATP
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the enzyme degrades SulA and the fusion protein of SulA and maltose-binding protein in presence of ATP but not with ATPgammaS
ATP
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HslV can slowly hydrolyze insulin B-chain, casein or carboxymethylated lactalbumin, but its activity is stimulated 20fold by HslU in presence of ATP
ATP
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ATP concentrations that activate hydrolysis of benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin are 50-100fold lower than those necessary for degradation of proteins, e.g. casein. ATP binding to a high affinity site triggers the formation of an active state capable of peptide cleavage, although ATP hydrolysis facilitates this process
ATP
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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
ATP
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dependent on, an ATP-binding site in domain N, separate from its role in polypeptide, ClpY, oligomerization, is required for complex formation with ClpQ
ATP
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dependent on. The intermediate domain of HslU is required for robust ATP hydrolysis, ATP hydrolysis activities of wild-type and mutant enzymes, overview
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HslU requires Mg2+ together with ATP for activity
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additional information
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HslU does not hydrolyze ATPgammaS, an ATP analogue
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additional information
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no activity with ATP-gammaS analogue, thermodynamic analysis of ATP-gammaS-binding and ATPase activity of wild-type ClpY and its T87I mutant, overview. In the presence of MBP-SulA and ClpQ, the mutant has about one-fourth of the ATPase activity of wild-type ClpY, ClpY mutant T87I in its hexameric form is defective in ATPase activity
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