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
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3.4.24.27
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chymotrypsin
-
elastase
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metalloprotease
-
subtilisin
-
staphylococcus
-
edman
-
pepsin
-
aureus
-
carboxypeptidase
-
endopeptidase
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bromide
-
cyanogen
-
collagenase
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proteinases
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dipeptide
-
angiotensin
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pronase
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metalloproteinases
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alpha-chymotrypsin
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thermolytic
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hydrolysates
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metalloendopeptidase
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stearothermophilus
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endoproteinase
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phosphoramidon
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i-converting
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enkephalinase
-
rhodopsin
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2-macroglobulin
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3.4.24.11
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cell-binding
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alcalase
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ace-inhibitory
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hexxh
-
dispase
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aspartame
-
thiorphan
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neprilysin
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s-carboxymethylated
-
half-cystine
-
astacin
-
synthesis
-
industry
-
nutrition
-
food industry
-
diagnostics
-
medicine
-
analysis
- 3.4.24.27
- chymotrypsin
- elastase
- metalloprotease
- subtilisin
- staphylococcus
-
edman
- pepsin
- aureus
- carboxypeptidase
- endopeptidase
- bromide
-
cyanogen
- collagenase
- proteinases
- dipeptide
- angiotensin
- pronase
- metalloproteinases
- alpha-chymotrypsin
-
thermolytic
- hydrolysates
- metalloendopeptidase
- stearothermophilus
-
endoproteinase
- phosphoramidon
-
i-converting
- enkephalinase
- rhodopsin
-
2-macroglobulin
-
3.4.24.11
-
cell-binding
- alcalase
-
ace-inhibitory
-
hexxh
-
dispase
- aspartame
- thiorphan
- neprilysin
-
s-carboxymethylated
-
half-cystine
- astacin
- synthesis
- industry
- nutrition
- food industry
- diagnostics
- medicine
- analysis
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
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Temperature Stability
Temperature Stability on EC 3.4.24.27 - thermolysin
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37
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incubation of impure enzyme at 37°C causes proteolysis of impurities, whereas the protease remains active and uncleaved
80
85
30 min, 51% remaining activity of recombinaqnt wild-type enzyme, 35-78% remaining activity of mutant enzymes
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half-life of wild-type enzyme is 18.3 min, half-lives of mutants are 25 min for L155A, 24 min for L155S, 60.8 min for L155A/I156V, 62.4 min for L155S/I156N, 93.3 for L155S/I156N, and 40 min for L155S/I156V
80
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1 h, heated enzyme has the same maximum velocity but lower affinity for substrate than the native
80
-
thermoinactivation of thermolysin at 80°C in 50% of solvents, half-lives of 3-20 min, with the increase in solvent hydrophobicity, thermal stability of the enzyme decreases, overview
80
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the rate constant (kobs) for thermal inactivation at 80°C is 84000 s-1 for the wild type enzyme
80
first-order rate constant of the thermal inactivation at 80°C in the presence of 1-100mM CaCl2