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
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elastase
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metalloprotease
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subtilisin
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staphylococcus
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edman
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pepsin
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aureus
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carboxypeptidase
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endopeptidase
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bromide
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cyanogen
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collagenase
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proteinases
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dipeptide
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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
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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
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dispase
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aspartame
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thiorphan
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neprilysin
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s-carboxymethylated
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half-cystine
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astacin
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synthesis
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industry
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nutrition
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food industry
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diagnostics
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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
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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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Natural Substrates Products
Natural Substrates Products on EC 3.4.24.27 - thermolysin
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REACTION DIAGRAM
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autodegradation at position 154155
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additional information
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isolated intact chloroplast from Spinacia oleracea are treated with thermolysin, mass spectrometric analysis and two-dimensional analysis of shedded envelope proteins, including 28 kDa ribonucleoprotein, cytosolic HSP70/Com70, translocon Tic40-like protein, ClpC, HSP70, and hexokinase 1, overview
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additional information
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thermolysin selectively digests the dermo-epidermal junction of epidermal sheets used for burnt persons, overview
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