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
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thermolytic
- hydrolysates
- metalloendopeptidase
- stearothermophilus
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endoproteinase
- phosphoramidon
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i-converting
- 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
- aspartame
- thiorphan
- neprilysin
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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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Application
Application on EC 3.4.24.27 - thermolysin
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analysis
diagnostics
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thermolysin is used in the diagnosis of prion diseases ovine scrapie and bovine spongiform encephalopathy, with similar sensitivity compared to proteinase K digestion, use of a protease to distinguish PrPC from PrPSc, overview
food industry
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the enzyme can be used for production of caseicin A, an antimicrobial active peptide, from alpha-casein, for potential improvement of the safety of infant milk formula using milk-derived bioactive peptides
industry
medicine
thermolysin degrades cellular prion protein while preserving both proteinase K-sensitive and proteinase K-resistant isoforms of disease-related prion protein in both rodent and human prion strains. In variant Creutzfeldt-Jakob disease, up to 90% of total prion protein present in the brain resists degradation with thermolysin, whereas only about 15% of this material resists digestion by proteinase K
nutrition
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the enzyme is used for synthesis of N-carbobenzyloxy L-Asp-L-Phe methyl ester, a precursor of the artificial sweetener aspartam
synthesis
additional information
thermolysin degrades cellular prion protein while preserving both proteinase K-sensitive and proteinase K-resistant isoforms of disease-related prion protein in both rodent and human prion strains. In variant Creutzfeldt-Jakob disease, up to 90% of total prion protein present in the brain resists degradation with thermolysin, whereas only about 15% of this material resists digestion by proteinase K
analysis
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selective biotin tagging and thermolysin proteolysis of chloroplast outer envelope proteins reveals information on protein topology and association into complexes. Development and evaluation of a method providing information at the surface of the outer envelope membrane, based on specific tagging with biotin or proteolysis using thermolysin, a non-membrane permeable protease. Envelope, thylakoid, and stroma proteins are separated by two-dimensional electrophoresis and analyzed by immunostaining and mass spectrometry, overview
analysis
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thermolysin offers a tool for complete solubilization of cartilage prior to comprehensive glycosaminoglycans(GAG)omic analysis, and is likely applicable to other collagen-rich tissues such as ligaments, skin, and blood vessels
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the enzyme is used for synthesis of N-carbobenzyloxy L-Asp-L-Phe methyl ester, a precursor of the artificial sweetener aspartam
industry
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the enzyme is used for synthesis of N-carbobenzyloxy L-Asp-L-Phe methyl ester, a precursor of the artificial sweetener aspartam
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production of L-alpha-aspartame, which is used as a low-calorie sweetener in food, including soft drinks, table-top sweeteners, dairy products, instant mixes, dressings, jams, confectionary, toppings and in pharmaceuticals
synthesis
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hydrolysis and condensation reactions of peptides catalyzed by enzyme can be reversibly controlled by on/off ultrasound irradiation depending on its frequency region
synthesis
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immobilized enzyme catalyzes the formation of beta-cyclodextrin esters using vinyl esters of butyrate, decanoate and laurate, as acyl donors in dimethylsulfoxide. Esterification occurs exclusively at the glucose C-2 position. Enzyme also catalyzes the synthesis of alpha-, beta-, gamma- and maltosyl-beta-cyclodextrin esters with vinyl laurate as the acyl donor in dimethylsulfoxide and dimethylformamide
synthesis
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immobilized enzyme catalyzes the transesterification of vinyl laurate to several sucrose-containing tri- and tetrasaccharides. Preferred position of acylation is the 2-OH group of the alpha-D-glucopyranose moiety linked 1 to 2 to the beta-D-fructofuranose unit
synthesis
introduction of ionizing residues into the active site of enzyme as a means of modifying its pH-activity profile
synthesis
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the enzyme is used for synthesis of N-carbobenzyloxy L-Asp-L-Phe methyl ester, a precursor of the artificial sweetener aspartam
synthesis
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the enzyme is used for synthesis of N-carbobenzyloxy L-Asp-L-Phe methyl ester, a precursor of the artificial sweetener aspartam
synthesis
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thermolysin is industrially used for the synthesis of N-carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester, a precursor of an artificial sweetener aspartame, from N-carbobenzoxy-L-aspartic acid and L-phenylalanine methyl ester
synthesis
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the enzyme can be used for production of caseicin A, an antimicrobial active peptide, from alpha-casein, for potential improvement of the safety of infant milk formula using milk-derived bioactive peptides
synthesis
using the enzyme to catalyze the condensation of the chiral aspartame-precursor, carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester, from the protected amino acid substrates carbobenzoxy-L-aspartic acid and L-phenylalanine methyl ester in large scale production. Analysis of the protease mediated peptide synthesisof a precursor of the artificial sweetener aspartame, a multiton peptide synthesis catalyzed by the enzyme thermolysin. X-ray structures of thermolysin in complex with aspartame substrates separately, and after protease mediated peptide synthesis in a crystal, rationalize the reaction's substrate preferences and reveal an unexpected form of substrate inhibition that explains its sluggishness. Structure guided optimization of this and other PMPS reactions could expand the economic viability of commercial peptides beyond current high-potency, low-volume therapeutics, with substantial green chemistry advantages
synthesis
sequential hydrolysis trypsin-thermolysin of commercial hydrolysate (prepared from solubilized milk proteins) has been performed to produce bioactive peptides, mainly casein phosphopeptides. Thermolysin was the last enzyme to be used, generating the final product, with a low content of aromatic amino acids and shorter peptides
synthesis
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the enzyme is used for synthesis of N-carbobenzyloxy L-Asp-L-Phe methyl ester, a precursor of the artificial sweetener aspartam
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thermolysin crystal can be used as the stationary phase in liquid chromatography to separate D/L-phenylglycine, thermolysin crystal is useful for chiral separation
additional information
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thermolysin treatment improves the yield of human intestinal epithelial cells. The thermolysin and endothelin-3 method can be used to isolate and generate viable human intestinal epithelial cells from the human small intestine
additional information
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thermolysin powder is not acutely toxic with an oral LD50 of more than 18,000 mg/kg (2520 mg/kg thermolysin protein) in rats and more than 24,000 mg/kg (3360 mg/kg protein) in mice. Subchronic feeding studies in rats for 91 days at doses up to 1000 mg/kg (390 mg/kg protein) revealed no significant differences between treated and non-treated groups, no evidence from allergenicity sequence analysis that thermolysin is an allergen, thermolysin is safe for use in food production