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
-
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
-
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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pH Range
pH Range on EC 3.4.24.27 - thermolysin
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5 - 8.5
5.5 - 8.5
for hydrolysis of neutral substrate N-[3-(2-furyl)acryloyl]-glycyl-L-leucine amide, wild-type and mutants N112D, N112E exhibit bell-shaped pH-dependence. For hydrolysis of negatively charged substrate N-carbobenzoxy-L-Asp-L-Phe methyl ester, wild-type shows bell-shaped pH-dependence, for mutants N112D and N112E, pH-dependence of the ratio kcat/Km decreases with increase in pH from 5.5 to 8.5
additional information
additional information
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bell-shaped pH-dependence with importance of surfacecharges of thermolysin, the bell-shaped pH dependence profile of the FAGLA-hydrolyzing activity of thermolysin is shifted from pH 5.4 to pH 6.7 by the addition of 4 M NaCl