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Literature summary for 3.4.24.27 extracted from

  • Wladyka, B.; Bista, M.; Sabat, A.J.; Bonar, E.; Grzeszczuk, S.; Hryniewicz, W.; Dubin, A.
    A novel member of the thermolysin family, cloning and biochemical characterization of metalloprotease from Staphylococcus pseudintermedius (2008), Acta Biochim. Pol., 55, 525-536.
    View publication on PubMed
Search for more literature for 3.4.24.27

Activating Compound

Activating Compound Comment Organism Structure
Calcium supplementation of growth medium by calcium induces expression. Regulation by calcium ions is at posttranscriptional level Staphylococcus pseudintermedius

General Stability

General Stability Organism
enzyme is stable in presence of CaCl2 Staphylococcus pseudintermedius

Inhibitors

Inhibitors Comment Organism Structure
1,10-phenanthroline 5 mM, complete inhibition Staphylococcus pseudintermedius
alpha2-Macroglobulin
-
 Staphylococcus pseudintermedius
EDTA 5 mM, complete inhibition Staphylococcus pseudintermedius
additional information not inhibitory: human blood serpins alpha-1-antitrypsin and alpha-1-antichymotrypsin Staphylococcus pseudintermedius

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular supplementation of growth medium by calcium induces expression. Regulation by calcium ions is at posttranscriptional level Staphylococcus pseudintermedius
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
35000
-
 x * 35000, SDS-PAGE, x * 55170, calculated Staphylococcus pseudintermedius
55170
-
 x * 35000, SDS-PAGE, x * 55170, calculated Staphylococcus pseudintermedius

Organism

Organism UniProt Comment Textmining
Staphylococcus pseudintermedius
-
-
-

Purification (Commentary)

Purification (Comment) Organism
incubation of impure enzyme at 37°C causes proteolysis of impurities, whereas the protease remains active and uncleaved Staphylococcus pseudintermedius

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alpha-1-antichymotrypsin + H2O cleavage within the sequence LSA-LVE Staphylococcus pseudintermedius ?
-
 ?
alpha-1-antitrypsin + H2O cleavage within the sequence AMF-LEA Staphylococcus pseudintermedius ?
-
 ?
azocasein + H2O
-
 Staphylococcus pseudintermedius ?
-
 ?
Azocoll + H2O
-
 Staphylococcus pseudintermedius ?
-
 ?
hide powder azure + H2O
-
 Staphylococcus pseudintermedius ?
-
 ?
additional information preferentially, peptide bonds preceding hydrophobic residues are hydrolyzed, such as I, L or F at P1' position. The enzyme less frequently also cleaves substrates with hydrophilic residues such as E, T or Q in the P1' position Staphylococcus pseudintermedius ?
-
 ?

Subunits

Subunits Comment Organism
? x * 35000, SDS-PAGE, x * 55170, calculated Staphylococcus pseudintermedius

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
37
-
 incubation of impure enzyme at 37°C causes proteolysis of impurities, whereas the protease remains active and uncleaved Staphylococcus pseudintermedius