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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Activating Compound
Activating Compound on EC 3.4.24.27 - thermolysin
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Ca2+
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accelerated hydrolysis of some tryptic peptides derived from bovine beta-casein in presence of Ca2+, while other peptides are not affected
Calcium
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supplementation of growth medium by calcium induces expression. Regulation by calcium ions is at posttranscriptional level
Cu2+-Cys-Gly-His-Lys
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stimulation at concentration up to 0.01 mM, inhibition at higher concentrations of 0.01-0.1 mM, binding and kinetics, overview
n-Pentanol
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saturation concentration of activation at 60%, inhibition at higher concentration
NaCl
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up to 40fold increase in activity in presence of 4 M NaCl, substrate MOCAc-PLGL(Dpa)AR. Degree of activation depends on substrate
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direct effect of organic solvents on the microenvironment of the enzyme largely depends on the molecular structure of the solvent
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additional information
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no change in hydrolysis of tryptic peptides derived from beta-casein by presence of Na+
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additional information
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microwave power output increases the level of activity of the immobilized thermolysin by 4.5fold, optimally at 40 W, overview
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