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Literature summary for 3.4.25.2 extracted from

  • Park, E.; Lee, J.W.; Yoo, H.M.; Ha, B.H.; An, J.Y.; Jeon, Y.J.; Seol, J.H.; Eom, S.H.; Chung, C.H.
    Structural alteration in the pore motif of the bacterial 20S proteasome homolog HslV leads to uncontrolled protein degradation (2013), J. Mol. Biol., 425, 2940-2954.
    View publication on PubMed
Search for more literature for 3.4.25.2

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BW21135 cells Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
mutant enzyme L88A, hanging drop vapor diffusion method, using 0.1 M Tris-HCl (pH 8.0), 28% (v/v) PEG monomethyl ether 550, and 0.2 M ammonium formate Escherichia coli

Protein Variants

Protein Variants Comment Organism
L88A the mutation leads to a tighter binding between HslV and HslU and a dramatic stimulation of both the proteolytic and ATPase activities. Furthermore, the HslV mutant shows a more than 7fold increase of basal hydrolytic activities toward small peptides and unstructured proteins Escherichia coli
L88F the muattion increases the peptidolytic activity of HslV in both the absence and presence of HslU and stimulates the ATPase activity of HslU more than wild type HslV Escherichia coli
L88G the HslV mutant shows a marked increase of basal hydrolytic activities toward small peptides and unstructured proteins Escherichia coli
L88S the HslV mutant shows a marked increase of basal hydrolytic activities toward small peptides and unstructured proteins Escherichia coli
L88W the muattion increases the peptidolytic activity of HslV in both the absence and presence of HslU and stimulates the ATPase activity of HslU more than wild type HslV Escherichia coli
R86A the mutant shows little peptidolytic activity compared to the wild type Escherichia coli
R89A the mutant shows little peptidolytic activity compared to the wild type Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
20000
-
 12 * 20000, SDS-PAGE Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A7B8
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alpha-casein + H2O
-
 Escherichia coli ?
-
 ?
Arc + H2O
-
 Escherichia coli ?
-
 ?
Arc/I37A + H2O
-
 Escherichia coli ?
-
 ?
carbobenzoxy-Gly-Gly-Leu-7-amido-4-methylcoumarin + H2O
-
 Escherichia coli carbobenzoxy-Gly-Gly-Leu + 7-amino-4-methylcoumarin
-
 ?
MBP-SulA + H2O
-
 Escherichia coli ?
-
 ?

Subunits

Subunits Comment Organism
homododecamer 12 * 20000, SDS-PAGE Escherichia coli

Synonyms

Synonyms Comment Organism
HslV protease
-
 Escherichia coli
hslVU a two-component protease complex, which consists of the HslV peptidase and the HslU ATPase Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP dependent on Escherichia coli