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
-
subtilisin
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staphylococcus
-
edman
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pepsin
-
aureus
-
carboxypeptidase
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endopeptidase
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bromide
-
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
-
astacin
-
synthesis
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industry
-
nutrition
-
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
-
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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Subunits
Subunits on EC 3.4.24.27 - thermolysin
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monomer
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1 * 37000-38000, Bacillus thermoproteolyticus, SDS-PAGE, gel filtration in 6 M guanidine hydrochloride
additional information
?
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x * 22 852, propeptide of thermolysin, sequence calculation, x * 26000, mature enzyme, SDS-PAGE
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in presence of Ca2+, enzyme exhibits four autodegradation sites, one of them being Gly154-Leu155
additional information
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structure determination and molecular dynamics simulations, overview
additional information
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the enzyme consists of a beta-rich N-terminal domain and an alpha-helix C-terminal domain connected by a central alpha-helix, which is located at the bottom of the active site cleft