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Literature summary for 3.4.24.27 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

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

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Bacillus cereus
-
-
-
Bacillus thermoproteolyticus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
-
?
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]

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