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Literature summary for 3.4.25.2 extracted from

  • Park, E.; Rho, Y.M.; Koh, O.J.; Ahn, S.W.; Seong, I.S.; Song, J.J.; Bang, O.; Seol, J.H.; Wang, J.; Eom, S.H.; Chung, C.H.
    Role of the GYVG pore motif of HslU ATPase in protein unfolding and translocation for degradation by HslV peptidase (2005), J. Biol. Chem., 280, 22892-22898.
    View publication on PubMed
Search for more literature for 3.4.25.2

Protein Variants

Protein Variants Comment Organism
G90P mutation of the GYVG motif residues affects protein unfolding, ATP hydrolysis, affinity for ADP, and interaction of HslU and HslV, overview, the mutant shows 41% reduced ATP hydrolysis activity compared to wild-type HslU Escherichia coli
G93A mutation of the GYVG motif residues affects protein unfolding, ATP hydrolysis, affinity for ADP, and interaction of HslU and HslV, overview Escherichia coli
G93P mutation of the GYVG motif residues affects protein unfolding, ATP hydrolysis, affinity for ADP, and interaction of HslU and HslV, overview Escherichia coli
V92A mutation of the GYVG motif residues affects protein unfolding, ATP hydrolysis, affinity for ADP, and interaction of HslU and HslV, overview Escherichia coli
V92I mutation of the GYVG motif residues affects protein unfolding, ATP hydrolysis, affinity for ADP, and interaction of HslU and HslV, overview Escherichia coli
V92S mutation of the GYVG motif residues affects protein unfolding, ATP hydrolysis, affinity for ADP, and interaction of HslU and HslV, overview Escherichia coli
Y91A mutation of the GYVG motif residues affects protein unfolding, ATP hydrolysis, affinity for ADP, and interaction of HslU and HslV, overview Escherichia coli
Y91F mutation of the GYVG motif residues affects protein unfolding, ATP hydrolysis, affinity for ADP, and interaction of HslU and HslV, overview Escherichia coli
Y91S mutation of the GYVG motif residues affects protein unfolding, ATP hydrolysis, affinity for ADP, and interaction of HslU and HslV, overview Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli the GYVG motif of HslU is important in unfolding of natively folded proteins as well as in translocation of unfolded proteins for degradation by HslV in its inner chamber ?
-
 ?
SulA + H2O Escherichia coli specific substrate degradation ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alpha-casein + H2O the structural features of the GYVG motif increase degrading activity Escherichia coli ?
-
 ?
ATP + H2O
-
 Escherichia coli ADP + phosphate
-
 ?
additional information the GYVG motif of HslU is important in unfolding of natively folded proteins as well as in translocation of unfolded proteins for degradation by HslV in its inner chamber Escherichia coli ?
-
 ?
N-carbobenzyloxy-Gly-Gly-Leu-7-amido-4-methylcoumarin + H2O
-
 Escherichia coli N-carbobenzyloxy-Gly-Gly-Leu + 7-amino-4-methylcoumarin
-
 ?
SulA + H2O specific substrate degradation Escherichia coli ?
-
 ?
SulA-maltose binding protein-fusion protein + H2O recombinant substrate, specific substrate degradation requires the flexibility provided by glycine residues and aromatic ring structures of the first 91 amino acids Escherichia coli ?
-
 ?

Subunits

Subunits Comment Organism
dodecamer HslV, the proteolytic active sites are sequestered in the inner chamber of HslV Escherichia coli
hexamer HslU Escherichia coli
More structure analysis using crystal structure PDB code 1G4A, the GYVG motif is essential for enzyme complex activity, overview Escherichia coli

Synonyms

Synonyms Comment Organism
HslU ATPase
-
 Escherichia coli
HslUV
-
 Escherichia coli
HslV peptidase
-
 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
8
-
 assay at Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP dependent on, HslU, ATP cleavage involves the pore motif GYVG Escherichia coli