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Literature summary for 3.4.25.2 extracted from

  • Sundar, S.; Baker, T.A.; Sauer, R.T.
    The I domain of the AAA+ HslUV protease coordinates substrate binding, ATP hydrolysis, and protein degradation (2012), Protein Sci., 21, 188-198.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.25.2

Protein Variants

Protein Variants Comment Organism
additional information construction of deletion mutants DELTA175-209linker, DELTA175-209GG, and DELTA108-243GG Escherichia coli
Y91A site-directed mutagenesis of the HslU GYVG pore loop, the mutant shows no remaining activity, the mutant hydrolyzes ATP and stimulates HslV peptidase activity Escherichia coli
Y91F site-directed mutagenesis of the HslU GYVG pore loop, the mutant shows reduced activity, the mutant hydrolyzes ATP and stimulates HslV peptidase activity Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten steady-state kinetics of wild-type and point mutant as well as deletion mutant enzymes with Arc substrates and ATP, overview Escherichia coli
0.02
-
 Arc-st11-ssrA wild-type HslU, pH 7.6, 37°C Escherichia coli
0.026
-
 Arc-st11-ssrA HslU mutant Y91F, pH 7.6, 37°C Escherichia coli
0.125
-
 Arc-st11-ssrA deletion mutant DELTA175-209linker, pH 7.6, 37°C Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Arc repressor + H2O interaction of Arc substrates with HslU variants bearing mutations in the GYVG pore loop or the I domain, overview. N-terminal residues of Arc initially interact with the GYVG loop in the axial pore of HslU, while other portions of Arc contact disordered I-domain loops, residues 175-209, that project into the substrate-binding funnel above the pore Escherichia coli ?
-
 ?
Arc-st11-ssrA + H2O wild-type HslU binds this fluorescent substrate with an average affinity, whereas the Y91A mutant variant shows no detectable binding. Tyr91 side chain plays an important role in allowing HslU to bind Arc-st11-ssrA Escherichia coli ?
-
 ?
additional information substrates are typically targeted to specific AAA+ proteases by peptide sequences. In the AAA+ HslUV protease, substrates are bound and unfolded by a ring hexamer of HslU, before translocation through an axial pore and into the HslV degradation chamber. The I domain plays an active role in coordinating substrate binding, ATP hydrolysis, and protein degradation by the HslUV proteolytic machine Escherichia coli ?
-
 ?
SulA + H2O as MBP-SulA fusion protein Escherichia coli ?
-
 ?

Synonyms

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

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.6
-
 assay at Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP dependent on. The intermediate domain of HslU is required for robust ATP hydrolysis, ATP hydrolysis activities of wild-type and mutant enzymes, overview Escherichia coli
additional information HslU does not hydrolyze ATPgammaS, an ATP analogue Escherichia coli