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Literature summary 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

Activating Compound

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

Protein Variants

EC Number Protein Variants Comment Organism
3.4.21.53 D241A 99% of wild-type peptidase activity Thermoplasma acidophilum
3.4.21.53 K63A 113% of wild-type peptidase activity Thermoplasma acidophilum
3.4.21.53 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
3.4.21.53 N293A 122% of wild-type peptidase activity Thermoplasma acidophilum
3.4.21.53 R305A 2% of wild-type peptidase activity Thermoplasma acidophilum
3.4.21.53 R375A 112% of wild-type peptidase activity Thermoplasma acidophilum
3.4.21.53 R382A 6% of wild-type peptidase activity Thermoplasma acidophilum

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.21.53 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
3.4.21.53 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

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.21.53 72000
-
 6 * 72000, SDS-PAGE Thermoplasma acidophilum
3.4.21.53 430000
-
 gel filtration Thermoplasma acidophilum

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.53 Thermoplasma acidophilum
-
-
-

Purification (Commentary)

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

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.53 FITC casein + H2O presence of ATP stimulates reaction 10fold Thermoplasma acidophilum ?
-
 ?
3.4.21.53 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

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