The Enzyme Database

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EC 3.4.24.27     
Accepted name: thermolysin
Reaction: Preferential cleavage: ┼Leu > ┼Phe
Other name(s): Bacillus thermoproteolyticus neutral proteinase; thermoase; thermoase Y10; TLN
Comments: 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]. Type example of peptidase family M4. Closely related but distinct enzymes are aeromonolysin, pseudolysin, bacillolysin, aureolysin and mycolysin
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9073-78-3
References:
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 (1966) 5919–5925. [PMID: 5954368]
2.  Morihara, K., Tsuzuki, H. and Oka, T. Comparison of the specificities of various neutral proteinases from microorganisms. Arch. Biochem. Biophys. 123 (1968) 572–588. [PMID: 4967801]
3.  Latt, S. A., Holmquist, B. and Vallee, B. L. Thermolysin: a zinc metalloenzyme. Biochem. Biophys. Res. Commun. 37 (1969) 333–339. [PMID: 5823940]
4.  Desmazeaud, M. J. and Hermier, J. H. Spécificité de la protéase neutre de Micrococcus caseolyticus. Eur. J. Biochem. 19 (1971) 51–55. [PMID: 5551628]
5.  Morihara, K. and Tsuzuki, H. Comparative study of various neutral proteinases from microorganisms: specificity with oligopeptides. Arch. Biochem. Biophys. 146 (1971) 291–296. [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 (1972) 35–37.
7.  Matthews, B. W. Structural basis of the action of thermolysin and related zinc peptidases. Acc. Chem. Res. 21 (1988) 333–340.
[EC 3.4.24.27 created 1972 as EC 3.4.24.4, part transferred 1992 to EC 3.4.24.27]
 
 


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