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
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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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Posttranslational Modification
Posttranslational Modification on EC 3.4.24.27 - thermolysin
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proteolytic modification
proteolytic modification
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the pre-pro-enzyme contains a signal peptide and a prosequence, the prosequence acts as an intramolecular chaperone for autocatalytic cleavage of the linking peptide bond
proteolytic modification
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thermolysin is synthesized as inactive pre-proenzyme and receives autocatalytic cleavage of the peptide bond linking the pro- and mature sequences, overview
proteolytic modification
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thermolysin performs Co2+-stimulable autolysis
proteolytic modification
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the pre-pro-enzyme contains a signal peptide and a prosequence, the prosequence acts as an intramolecular chaperone for autocatalytic cleavage of the linking peptide bond
proteolytic modification
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autolytic processing. Secreted proteases are produced as prepro-proteins. The pre-peptide is cleaved-off during Sec-controlled secretion, and the active protease emerges outside the cell after folding of the proprotein and autolytic removal of the pro-peptide. The protein is translocated through the membrane at the expense of ATP and the pre-peptide is cleaved off by a type I signal peptidase. The pro-part plays two roles in this process: it facilitates folding by acting as an intra-molecular chaperone and it inhibits protease activity of the folded pro-enzyme
proteolytic modification
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the pre-pro-enzyme contains a signal peptide and a prosequence, the prosequence acts as an intramolecular chaperone for autocatalytic cleavage of the linking peptide bond
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proteolytic modification
thermolysin encoded by LIC13322 has a signal peptide for secretion, a fungalin/thermolysin propeptide (FTP) domain, a propeptide (PepSY) domain, and a catalytic domain M4 that includes peptidase_M4 and peptidase_M4_C
proteolytic modification
Leptospira interrogans serovar Copenhageni Fiocruz L1-130
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thermolysin encoded by LIC13322 has a signal peptide for secretion, a fungalin/thermolysin propeptide (FTP) domain, a propeptide (PepSY) domain, and a catalytic domain M4 that includes peptidase_M4 and peptidase_M4_C
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