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Enzyme - EC 3.4.24.27
DFBP ID DFBPENZY0031
EC Number EC 3.4.24.27
Term Thermolysin
Introduction
DFBP ID DFBPENZY0031
EC Number EC 3.4.24.27
Accepted Name

Accepted name:
     • Thermolysin
Alternative name(s):
     • Bacillus thermoproteolyticus neutral proteinase

Cleavage sites
Number
Pn------
P4
P3
P2
P1
Cleavage sites
P1'
P2'
------Pm'
site.1------
-
--
not D or E-|-A, F, I, L, M or V-
------
Cross-references
Database(s)
ExPASy - ENZYMEEC 3.4.24.27
MEROPS databaseEnzyme ID M04.001
ExplorEnz databaseEC 3.4.24.27
Reference(s)
Literature(s)

[1] Keil, B. Specificity of proteolysis. Springer-Verlag Berlin-Heidelberg-NewYork, pp.335. (1992)
[2] Keil, B., Tong T.N. LYSIS. Springer-Verlag Berlin-Heidelberg-NewYork, diskette set. (1992)
[3] 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]
[4] 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]
[5] Latt, S. A., Holmquist, B. and Vallee, B. L. Thermolysin: a zinc metalloenzyme. Biochem. Biophys. Res. Commun. 37 (1969) 333–339. [DOI] [PMID: 5823940]
[6] 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]
[7] 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]
[8] 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]
[9] Matthews, B. W. Structural basis of the action of thermolysin and related zinc peptidases. Acc. Chem. Res. 21 (1988) 333–340.

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