Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.21.53 extracted from

  • Besche, H.; Tamura, N.; Tamura, T.; Zwickl, P.
    Mutational analysis of conserved AAA+ residues in the archaeal Lon protease from Thermoplasma acidophilum (2004), FEBS Lett., 574, 161-166.
    View publication on PubMed
Search for more literature for 3.4.21.53

Activating Compound

Activating Compound Comment Organism Structure
ATP hydrolysis of FITC casein is 10fold increase in presence of ATP Thermoplasma acidophilum

Protein Variants

Protein Variants Comment Organism
D241A 99% of wild-type peptidase activity Thermoplasma acidophilum
K63A 113% of wild-type peptidase activity Thermoplasma acidophilum
additional information Walker A and B motifs, and the sensor 1 and sensor 2’ are essential for the ATPase activity, while sensor 2 and the arginine finger are involved in activation of the protease domain Thermoplasma acidophilum
N293A 122% of wild-type peptidase activity Thermoplasma acidophilum
R305A 2% of wild-type peptidase activity Thermoplasma acidophilum
R375A 112% of wild-type peptidase activity Thermoplasma acidophilum
R382A 6% of wild-type peptidase activity Thermoplasma acidophilum

Inhibitors

Inhibitors Comment Organism Structure
ADP wild-type, up to 60% inhibition, mutant K63A, slight activation, mutants D241A, N293A, R375A, about 50% inhibition of peptidase activity. Complete inhibition of hydrolysis of FITC Thermoplasma acidophilum
ATP peptidase activity of enzyme is modulated by the ATP-state of the AAA+ domain. Absence of nucleotide results in basal activity, presence of ATP reduces the basal activity. Presence of ATP stimulates hydrolysis of FITC 10fold Thermoplasma acidophilum

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane native enzyme and recombinant enzyme in Escherichia coli Thermoplasma acidophilum 16020
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
72000
-
 6 * 72000, SDS-PAGE Thermoplasma acidophilum
430000
-
 gel filtration Thermoplasma acidophilum

Organism

Organism UniProt Comment Textmining
Thermoplasma acidophilum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant membrane enzyme in Escherichia coli Thermoplasma acidophilum

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 enzyme degrades substrates in a processive manner Thermoplasma acidophilum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
FITC casein + H2O presence of ATP stimulates reaction 10fold Thermoplasma acidophilum ?
-
 ?
N-succinyl-LLVY-7-amido-4-methylcoumarin + H2O no cleavage of bond between Y and 7-amido-4-methylcoumarin Thermoplasma acidophilum N-succinyl-L-leucyl-L-leucine + Val-Tyr-7-amido-4-methylcoumarin + N-succinyl-L-leucine + Leu-Val-Tyr-7-amido-4-methylcoumarin
-
 ?

Subunits

Subunits Comment Organism
hexamer 6 * 72000, SDS-PAGE Thermoplasma acidophilum