ExplorEnz: EC 3.4.24.27

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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. [DOI] [PMID: 4967801]
3.	Latt, S. A., Holmquist, B. and Vallee, B. L. Thermolysin: a zinc metalloenzyme. Biochem. Biophys. Res. Commun. 37 (1969) 333–339. [DOI] [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. [DOI] [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. [DOI] [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. [PMID: 18663848]
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]