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Literature summary for 3.4.21.111 extracted from

  • Lin, S.J.; Yoshimura, E.; Sakai, H.; Wakagi, T.; Matsuzawa, H.
    Weakly bound calcium ions involved in the thermostability of aqualysin I, a heat-stable subtilisin-type protease of Thermus aquaticus YT-1 (1999), Biochim. Biophys. Acta, 1433, 132-138.
    View publication on PubMed
Search for more literature for 3.4.21.111

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ 1 mol per mol enzyme Thermus aquaticus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
28000
-
 SDS-PAGE Thermus aquaticus

Organism

Organism UniProt Comment Textmining
Thermus aquaticus
-
 YT-1
-
Thermus aquaticus YT-1
-
 YT-1
-

Purification (Commentary)

Purification (Comment) Organism
-
 Thermus aquaticus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
-
 Thermus aquaticus N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
 ?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
-
 Thermus aquaticus YT-1 N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
80
-
-
 Thermus aquaticus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
80
-
 stable in presence of 1 mM Ca2+, after gel filtration to remove free Ca2+ the enzyme still binds Ca2+ but is no longer stable, La3+, Sr2+, Nd3+ and Tb3+ stabilize the enzyme Thermus aquaticus