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Literature summary for 3.4.21.65 extracted from

  • Voordouw, G.; Gaucher, G.M.; Roche, R.S.
    Physiochemical properties of thermomycolase, the thermostable, extracellular, serine protease of the fungus Malbranchea pulchella (1974), Can. J. Biochem., 52, 981-990.
    View publication on PubMed
Search for more literature for 3.4.21.65

General Stability

General Stability Organism
Calcium stabilizes against autolysis Malbranchea pulchella
Extensive autolysis, especially at low calcium concentrations produces low MW peptide material Malbranchea pulchella
Freezing and freeze-drying causes a considerable loss of activity Malbranchea pulchella
Repeated freeze-drying causes insolubilization Malbranchea pulchella

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
32000 33000 Malbranchea pulchella, sedimentation equilibrium, of diisopropylphosphorylthermomycolase Malbranchea pulchella
33000
-
 x * 33000, Malbranchea pulchella var. sulfurea, SDS-PAGE Malbranchea pulchella

Organism

Organism UniProt Comment Textmining
Malbranchea pulchella
-
 var. sulfurea
-

Purification (Commentary)

Purification (Comment) Organism
-
 Malbranchea pulchella

Subunits

Subunits Comment Organism
? x * 33000, Malbranchea pulchella var. sulfurea, SDS-PAGE Malbranchea pulchella
? x * 32000-33000, Malbranchea pulchella, SDS-PAGE of diisopropylphosphorylthermomycolase Malbranchea pulchella

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
 at calcium concentrations 1 mM and 10 mM the enzyme undergoes a sharp thermal denaturation with transition temperatures at 69°C and 75°C, respectively Malbranchea pulchella
70
-
 maximal thermostability 10 mM Ca2+ Malbranchea pulchella