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
-
2-macroglobulin
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3.4.24.11
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cell-binding
- alcalase
-
ace-inhibitory
-
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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General Information
General Information on EC 3.4.24.27 - thermolysin
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evolution
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thermolysin and pseudolysin belong to subclan MA(E) of peptidases, also known as the Glu-zincins, of the matrix metalloproteinases family of zinc-containing endoproteinases with broad substrate specificity and extracellular matrix components are among the substrates
physiological function
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thermolysin family proteases are related to various diseases such as bacterial infections, cholera, gastritis and peptic ulcers, and gastric carcinoma
additional information
additional information
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life cycle of the thermolysin-like protease from Bacillus stearothermophilus in light of the calcium-dependent stability and instability of the N-terminal domain.
additional information
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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
additional information
proposed mechanism of action for the thermolysin-catalyzed synthesis of aspartame precursor carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester, overview. Residues E143, Y157, and H231 represent the catalytic triad, enzyme active site structure analysis
additional information
structure analsis using enzyme structure PDB ID 8TLN. Catalytically important residues Glu143 and His231. Important role of Asn116 in the activity and stability of thermolysin presumably by stabilizing the beta-hairpin structure. In the N-terminal domain of thermolysin, two antiparallel beta-strands, Asn112-Ala113-Phe114-Trp115 and Ser118-Gln119-Met120-Val121-Tyr122 are connected by an Asn116-Gly117 turn to form a beta-hairpin structure
additional information
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the glutamic acid of the HEXXH motif is catalytically important
additional information
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the peptide products from hydrolysis of elastin and collagen by the enzyme have an inhibitory effect on angiotensin I-converting enzyme and antihypertensive activity, overview
additional information
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the peptide products from hydrolysis of elastin and collagen by the enzyme have an inhibitory effect on angiotensin I-converting enzyme and antihypertensive activity, overview
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