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
-
elastase
-
metalloprotease
-
subtilisin
-
staphylococcus
-
edman
-
pepsin
-
aureus
-
carboxypeptidase
-
endopeptidase
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bromide
-
cyanogen
-
collagenase
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proteinases
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dipeptide
-
angiotensin
-
pronase
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metalloproteinases
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alpha-chymotrypsin
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thermolytic
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hydrolysates
-
metalloendopeptidase
-
stearothermophilus
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endoproteinase
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phosphoramidon
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i-converting
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enkephalinase
-
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
-
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
-
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
3.4.24.27 thermolysinAdvanced search results
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results (Metals Ions
Metals Ions on EC 3.4.24.27 - thermolysin
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METALS and IONS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Ca2+
Co2+
K+
-
activates, preference of monovalent cations in descending order: Na+, K+, Li+
Li+
-
activates, preference of monovalent cations in descending order: Na+, K+, Li+
Na+
NaCl
NaSCN
-
3fold increase in catalytic activity of thermolysin when the NaSCN concentration is increased to 1 M, but decrease in catalytic activity at higher concentrations of NaSCN
Zinc
Zn2+
additional information
Ca2+
-
TLN contains one zinc ion and four calcium ions, and these ions contribute to enzymatic catalysis and structural stability
Ca2+
-
there are two adjacent calcium ions seemingly firmly bound inside the surface of the molecule by chelation to five acidic groups: Asp138, Glu177, Asp185, Glu190 and Asp191, two additional calcium binding sites are at exposed surface regions, one chelated by Asp57 and possibly also by Asp59 and the other chelated by Asp200
Ca2+
-
four Ca2+ per enzyme molecule are required for enzyme stability
Ca2+
-
four ions per enzyme molecule required for stability
Ca2+
-
thermolysin consists of four Ca2+ ligand ions necessary for stability
Ca2+
-
thermolysin has four calcium ions responsible for its thermostability
Ca2+
-
CaCl2 does not exert any significant influence on the activity of immobilized thermolysin, but stabilizes the enzyme in absence of Zn2+
Ca2+
-
protease binds calcium ions in the regions that are involved in the autolytic maturation process, at least one of the calcium ions plays a regulatory role. This calcium ion plays an important role as a switch that modulates the protease between stable and unstable states as appropriate to the biological need
Co2+
-
active zinc ion in thermolysin can be substituted by Co2+, doubles activity
Co2+
-
increases the activity 3-4fold at up to 2 mM, but inhibits at 2-18 mM, activation-and-inhibition dual effects of Co2+ ion are analysed kinetically, Co2+-dependent activation is inhibited competitively by Zn2+ ion at 0.0001-0.001 mM
Co2+
-
the active site zinc atom of thermolysin is replaced by cobalt
Na+
-
activates, preference of monovalent cations in descending order: Na+, K+, Li+, the bell-shaped pH dependence profile of the FAGLA-hydrolyzing activity of thermolysin is shifted from pH 5.4 to pH 6.7 by the addition of 4 M NaCl
Na+
-
4 M Na+ stimulates the hydrolytic activity of wild type thermolysin about 13fold
NaCl
activates the mutant enzymes at 4 M to 17-19fold of wild-type enzyme activity, overview
NaCl
-
induces enzyme activation, activation of mutant enzymes is reduced compared to the wild-type enzyme
Zinc
-
the three zinc ligands are two histidines and glutamic acid
Zn2+
-
dependent on, thermolysin is a bacterial zinc metalloproteinase. The active site zinc atom is tetrahedrally coordinated when the inhibitors N-benzyloxycarbonyl-tryptophan or N-benzyloxycarbonyl-phenylalanine are bound to thermolysin
Zn2+
-
TLN contains one zinc ion and four calcium ions, and these ions contribute to enzymatic catalysis and structural stability
Zn2+
-
a zinc metalloproteinase that contains a HEXXH motif, one Zn2+ per enzyme molecule is required for activity
Zn2+
-
one ion per enzyme molecule essential for activity, the enzyme contains the HEXXH motif constituting the zinc catalytic site
Zn2+
-
one ion per enzyme molecule required for activity
Zn2+
-
stereochemical relationships between Gln128, Glu143, Gln225, Asp226, His231 and active site Zn2+ of thermolysin, overview
Zn2+
-
zinc metalloproteinase, one ion per enzyme molecule required for activity
Zn2+
comparison of metal preferences of Escherichia coli peptide deformylase and Bacillus thermoproteolyticus thermolysin. Both enzymes catalyze via the same chemical steps, and reproduce their different preferences for zinc or iron as competent cofactors. In thermolysin, the substrate is strongly activated and can serve as the fifth coordination ligand of zinc prior to the chemical steps. When iron replaces zinc, its stronger interaction with the hydroxide ligand may lead to higher activation barrier in thermolysin
Zn2+
-
residues H142, H146, and E166 coordinate the catalytic zinc
Zn2+
-
a single catalytic Zn2+ ion is essential for hydrolytic activity
Zn2+
-
thermolysin consists of three Zn2+ ligand ions necessary for activity
Zn2+
-
the enzyme has a catalytic zinc ion at the active site cleft with a tetrahedral coordination formed by the two histidines of a HEXXH motif, and a glutamic acid located 18-72 residues C-terminal of the HEXXH motif. The fourth zinc coordinating ligand in the free enzyme is a water molecule
Zn2+
zinc metalloprotease, no efect on activity by exogenous Zn2+ at 1 mM, inhibitory at 5 mM
additional information
-
thermolysin activity as well as its stability is remarkably enhanced by high concentration of neutral salts consisting of Na+, K+, Cl-, and Br- in the synthesis and hydrolysis of N-carbobenzoxy-L-aspertyl-L-phenylalanine methyl ester and hydrolysis of N-[3-(2-furyl)acryloyl]-glycyl-L-leucine amide
