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3.4.24.27: thermolysin

This is an abbreviated version!
For detailed information about thermolysin, go to the full flat file.

Word Map on EC 3.4.24.27

Reaction

preferential cleavage: -/-Leu > -/-Phe =

Synonyms

Bacillus thermoproteolyticus neutral proteinase, EC 3.4.24.4, hspA, LIC13322, Neutral metalloproteinase, NprM, protease type X, proteinase type X, Proteinase, Bacillus thermoproteolyticus neutral, protex 14L, Thermoase, thermoase PC10F, Thermoase Y10, thermolysin, thermolysin-like protease, Thermostable neutral proteinase, TL, TLN, TLP, TLP-ste

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.27 thermolysin

General Stability

General Stability on EC 3.4.24.27 - thermolysin

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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
After precipitation with trichloroacetic acid the purified enzyme irreversibly loses activity and solubility at neutral pH
-
Ca2+ increases thermal stability
-
Ca2+ stablizes the enzyme
Calcium is necessary to stabilize the structure of thermolysin
-
enzyme is stable in presence of CaCl2
-
important role of Asn116 in the activity and stability of thermolysin presumably by stabilizing the beta-hairpin structure. In the N-terminal domain of thermolysin, two antiparallel beta-strands, Asn112-Ala113-Phe114-Trp115 and Ser118-Gln119-Met120-Val121-Tyr122 are connected by an Asn116-Gly117 turn to form a beta-hairpin structure