EC - Thermolysin

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IntEnz Enzyme Nomenclature


Accepted name:
Other names:
Bacillus thermoproteolyticus neutral proteinase
thermoase Y10
Systematic name:




A thermostable extracellular metalloendopeptidase containing four calcium ions. Enzymes that may be species variants of thermolysin are reported from Micrococcus caseolyticus [4] and Aspergillus oryzae [5]. Formerly included in EC Type example of peptidase family M4. Closely related but distinct enzymes are aeromonolysin, pseudolysin, bacillolysin, aureolysin and mycolysin.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , MEROPS , NIST 74 , UniPathway
Protein domains and families: PROSITE:PDOC00129
Structural data: CSA , EC2PDB
CAS Registry Number: 9073-78-3


  1. Ohta, Y. Ogura, Y. and Wada, A.
    Thermostable protease from thermophilic bacteria. I. Thermostability, physicochemical properties, and amino acid composition.
    J. Biol. Chem. 241: 5919-5925 (1966). [PMID: 5954368]
  2. Morihara, K., Tsuzuki, H. and Oka, T.
    Comparison of the specificities of various neutral proteinases from microorganisms.
    Arch. Biochem. Biophys. 123: 572-588 (1968). [PMID: 4967801]
  3. Latt, S. A., Holmquist, B. and Vallee, B. L.
    Thermolysin: a zinc metalloenzyme.
    Biochem. Biophys. Res. Commun. 37: 333-339 (1969). [PMID: 5823940]
  4. Desmazeaud, M. J. and Hermier, J. H.
    Spécificité de la protéase neutre de Micrococcus caseolyticus.
    Eur. J. Biochem. 19: 51-55 (1971). [PMID: 5551628]
  5. Morihara, K.and Tsuzuki, H.
    Comparative study of various neutral proteinases from microorganisms: specificity with oligopeptides.
    Arch. Biochem. Biophys. 146: 291-296 (1971). [PMID: 5004124]
  6. Titani, K., Hermodson, M. A., Ericson, L. H., Walsh, K. A. and Neurath, H.
    Amino-acid sequence of thermolysin.
    Nature New Biol. 238: 35-37 (1972).
  7. Matthews, B. W.
    Structural basis of the action of thermolysin and related zinc peptidases.
    Acc. Chem. Res. 21: 333-340 (1988).

[EC created 1972 as EC, part transferred 1992 to EC]