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Literature summary for 3.4.21.62 extracted from

  • Smith, C.A.; Toogood, H.S.; Baker, H.M.; Daniel, R.M.; Baker, E.N.
    Calcium-mediated thermostability in the subtilisin superfamily: the crystal structure of Bacillus Ak.1 protease at 1.8 A resolution (1999), J. Mol. Biol., 294, 1027-1040.
    View publication on PubMed
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Cloned(Commentary)

Cloned (Comment) Organism
AkP gene cloned and expressed in Escherichia coli PB5517 Bacillus sp. (in: Bacteria)

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure determined by molecular replacement, crystals grown in hanging drops, monoclinic space group P2(1), with cell dimensions a : 44.1 A, b : 51.7 A, c : 52.8 A, coordinates and structure factor amplitudes in the ProteinDataBank codes 1DBI and R1DBISF Bacillus sp. (in: Bacteria)

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ bound calcium ions play a key role in protecting against autolysis and thermal denaturation Bacillus sp. (in: Bacteria)

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
27800
-
 calculated from the sequence Bacillus sp. (in: Bacteria)

Organism

Organism UniProt Comment Textmining
Bacillus sp. (in: Bacteria) Q45670 strain Ak.1
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Bacillus sp. (in: Bacteria) Ak1 Q45670 strain Ak.1
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Bacillus sp. (in: Bacteria)

Synonyms

Synonyms Comment Organism
Ak.1 protease
-
 Bacillus sp. (in: Bacteria)

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
70 105 highly thermostable, heat-treating for 2 h at 70°C activates the protease, half-life at 85°C in presence of DTT is 34 min, in absence of DTT 317 min, at 105°C complete loss of activity is virtually instantaneous in absence of sorbitol, in presence of 90% sorbitol the half-life is 104 min Bacillus sp. (in: Bacteria)