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Literature summary extracted from

  • Adekoya, O.A.; Sylte, I.
    The thermolysin family (M4) of enzymes: therapeutic and biotechnological potential (2009), Chem. Biol. Drug Des., 73, 7-16.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.24.27 N-chloroacetyl-N-hydroxyleucine methyl ester irreversible inhibition Bacillus cereus
3.4.24.27 N-chloroacetyl-N-hydroxyleucine methyl ester irreversible inhibition Bacillus thermoproteolyticus
3.4.24.27 N-chloroacetyl-N-hydroxyleucyl-alanyl-glycinamide irreversible inhibition Bacillus cereus
3.4.24.27 N-chloroacetyl-N-hydroxyleucyl-alanyl-glycinamide irreversible inhibition Bacillus thermoproteolyticus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.24.27 Ca2+ thermolysin has four calcium ions responsible for its thermostability Bacillus cereus
3.4.24.27 Ca2+ thermolysin has four calcium ions responsible for its thermostability Bacillus thermoproteolyticus
3.4.24.27 Zn2+ contains Zn2+ Bacillus cereus
3.4.24.27 Zn2+ contains Zn2+ Bacillus thermoproteolyticus

Organism

EC Number Organism UniProt Comment Textmining
3.4.24.27 Bacillus cereus
-
-
-
3.4.24.27 Bacillus thermoproteolyticus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.27 additional information the major site for thermolysin cleavage specificity, (the S1' site), accepts large hydrophobic residues. Thermolysin preferentially cleaves at the N-terminal side of hydrophobic or bulky amino side chains such as Leu, Phe, Ile and Val. Thermolysin also cleaves bonds of Met, His, Tyr, Ala, Asn, Ser, Thr, Gly, Lys, Glu or Asp at the P1' site Bacillus cereus ?
-
 ?
3.4.24.27 additional information the major site for thermolysin cleavage specificity, (the S1' site), accepts large hydrophobic residues. Thermolysin preferentially cleaves at the N-terminal side of hydrophobic or bulky amino side chains such as Leu, Phe, Ile and Val. Thermolysin also cleaves bonds of Met, His, Tyr, Ala, Asn, Ser, Thr, Gly, Lys, Glu or Asp at the P1' site Bacillus thermoproteolyticus ?
-
 ?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.4.24.27 82
-
 the enzyme loses 50% of its activity after 30 min at 82°C Bacillus thermoproteolyticus