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Literature summary extracted from

  • Matsuzawa, H.
    Aqualysin I (2004), Handbook of Proteolytic Enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , Eds. ) Academic Press, 2, 1799-1800.
No PubMed abstract available

Application

EC Number Application Comment Organism
3.4.21.111 additional information C-terminal pro sequence of the enzyme functions as an intramolecular chaperone that stabilizes the partially unfolded structure of the protease domain, and thereby facilitates its secretion Thermus aquaticus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.21.111 expression in Escherichia coli and Thermus thermophilus Thermus aquaticus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.21.111 DFP strongly inhibits Thermus aquaticus
3.4.21.111 N-terminal propeptide of aqualisin I potent inhibitor Thermus aquaticus
3.4.21.111 Streptomyces subtilisin inhibitor strongly inhibits Thermus aquaticus
3.4.21.111 Z-Ala-Gly-Phe-CH2Cl strongly inhibits Thermus aquaticus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.21.111 Ca2+ stabilizes, at least two Ca2+-binding sites, i. e. stronger and weaker binding sites, weaker binding site essential for heat stability of the enzyme, Ca2+ bound to the stronger binding site is hardly removed with EDTA Thermus aquaticus
3.4.21.111 La3+ stabilizes Thermus aquaticus
3.4.21.111 Nd3+ stabilizes Thermus aquaticus
3.4.21.111 Sr2+ stabilizes Thermus aquaticus
3.4.21.111 Tb3+ stabilizes Thermus aquaticus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.21.111 28350
-
 calculated Thermus aquaticus
3.4.21.111 38000
-
 precursor with a C-terminal pro sequence from the membrane fraction of Escherichia coli cells Thermus aquaticus
3.4.21.111 53910
-
 synthesized as a large precursor, calculated Thermus aquaticus

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.111 Thermus aquaticus
-
-
-
3.4.21.111 Thermus aquaticus YT-1
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.21.111 recombinant enzyme from Escherichia coli cells harboring an expression plasmid using the tac promoter by cation-exchange chromatography, larger scale production by using bacteriophage T7 RNA polymerase/promoter Thermus aquaticus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.111 elastin-orcein + H2O at 40°C, pH 7.5 Thermus aquaticus ?
-
 ?
3.4.21.111 elastin-orcein + H2O at 40°C, pH 7.5 Thermus aquaticus YT-1 ?
-
 ?
3.4.21.111 Hammarsten casein + H2O at 70°C, pH 7.5-10.4 Thermus aquaticus ?
-
 ?
3.4.21.111 Hammarsten casein + H2O at 70°C, pH 7.5-10.4 Thermus aquaticus YT-1 ?
-
 ?
3.4.21.111 additional information exhibits specificity toward ester of amino acids with small haydrophobic or aromatic residues in P1 Thermus aquaticus ?
-
 ?
3.4.21.111 additional information exhibits specificity toward ester of amino acids with small haydrophobic or aromatic residues in P1 Thermus aquaticus YT-1 ?
-
 ?
3.4.21.111 oxidized insulin chain B + H2O at 40°C, pH 7.5 Thermus aquaticus ?
-
 ?
3.4.21.111 oxidized insulin chain B + H2O at 40°C, pH 7.5 Thermus aquaticus YT-1 ?
-
 ?
3.4.21.111 Suc-Ala-Ala-Pro-Phe-p-nitroanilide + H2O at 40°C, pH 7.5 Thermus aquaticus Suc-Ala-Ala-Pro-Phe + p-nitroaniline
-
 ?
3.4.21.111 Suc-Ala-Ala-Pro-Phe-p-nitroanilide + H2O at 40°C, pH 7.5 Thermus aquaticus YT-1 Suc-Ala-Ala-Pro-Phe + p-nitroaniline
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.21.111 80
-
 in the presence of 1 mM CaCl2, which stabilizes the enzyme Thermus aquaticus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.4.21.111 40 80
-
 Thermus aquaticus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.21.111 10
-
-
 Thermus aquaticus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.4.21.111 7.5 10.4
-
 Thermus aquaticus