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
-
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
- 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
Advanced search results
Inhibitors
Inhibitors on EC 3.4.24.27 - thermolysin
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
(E)-N-(naphthalen-1-yl)-N'-(4-oxo-2-phenylquinazolin-3(4H)-yl)acetimidamide
-
low inhibitory activity
2-(4-chlorophenyl) quinazolin-4(3H)-one
-
low inhibitory activity
2-(4-methylphenyl) quinazolin-4(3H)-one
-
low inhibitory activity
2-(4-methylphenyl)-3-(1,3-thiazol-2-yl) quinazolin-4(3H)-one
-
-
2-(4-oxo-2-methylquinazolin-3(4H)-yl) guanidine
-
low inhibitory activity
2-(N-Bromoacetyl-N-hydroxyamino)-4-methylpentanonitrile
-
irreversible
2-benzamido-N-(3-(4-oxo-2-phenylquinazolin-3(4H)-yl)propyl)benzamide
-
low inhibitory activity
2-chloro-N-(2-methyl-4-oxoquinazolin-3(4H)-yl)acetamide
-
low inhibitory activity
2-hydroxy-N-(4-methyl-2-nitrophenyl)-3-nitrobenzamide
-
competitive
2-phenyl-3-(1, 3-thiazol-2-yl) quinazolin-4(3H)-one
-
low inhibitory activity
2-phenyl-3-[[(1E)-phenylmethylene] amino]-2,3-dihydroquinazolin-4(1H)-one
-
low inhibitory activity
2-[(biphenyl-4-ylsulfonyl)[2-(hydroxyamino)-2-oxoethyl]amino]-N-[2-(4-sulfamoylphenyl)ethyl]acetamide (non-preferred name)
-
-
2-[benzyl[2-(hydroxyamino)-2-oxoethyl]amino]-N-[2-(4-sulfamoylphenyl)ethyl]acetamide (non-preferred name)
-
the phenyl group of the strong binder occupies the S'2-subpocket, while a second ring system occupy the S1-subpocket in both thermolysin and pseudolysin, EC 3.4.24.27
2-[benzyl[2-(hydroxyamino)-2-oxoethyl]amino]-N-[3-(4-phenylpiperazin-1-yl)propyl]acetamide (non-preferred name)
-
the phenyl group of the strong binder occupies the S'2-subpocket, while a second ring system occupy the S1-subpocket in both thermolysin and pseudolysin, EC 3.4.24.26
2-[[2-(hydroxyamino)-2-oxoethyl][(4-methoxyphenyl)sulfonyl]amino]-N-[2-(4-sulfamoylphenyl)ethyl]acetamide (non-preferred name)
-
-
2-[[2-(hydroxyamino)-2-oxoethyl][(4-phenoxyphenyl)sulfonyl]amino]-N-[2-(4-sulfamoylphenyl)ethyl]acetamide (non-preferred name)
-
-
3-(2-aminoethyl)-2-(4-methylphenyl) quinazolin-4(3H)-one
-
low inhibitory activity
3-(2-hydroxyethyl) quinazolin-4(3H)-one
-
low inhibitory activity
3-(3-aminopropyl)-2-(4-methylphenyl) quinazolin-4(3H)-one
-
low inhibitory activity
3-(4-iodophenyl)-2-phenylquinazolin-4(3H)-one
-
low inhibitory activity
3-(isopropylideneamino)-2,2-dimethyl-2,3-dihydroquinazolin-4(1H)-one
-
potent inhibitor
3-([(1E)-[4-(dimethylamino) phenyl]methylene]amino)-2-methylquinazolin-4(3H)-one
-
-
3-([(1E)-[4-(dimethylamino) phenyl]methylene]amino)-2-phenylquinazolin-4(3H)-one
-
-
3-amino-2-(hydrazinomethyl) quinazolin-4(3H)-one
-
low inhibitory activity
3-phenyl-2-(trifluoromethyl) quinazolin-4(3H)-one
-
potent inhibitor
3-Phenylpropionyl-L-Phe
-
crystallographic study of the binding to thermolysin
3-[[(1E)-(2-hydroxynaphthalen-1-yl)methylene]amino]-2-phenylquinazolin-4(3H)-one
-
low inhibitory activity
3-[[(1E)-(3-chlorophenyl)methylene]amino]-2-phenylquinazolin-4(3H)-one
-
-
3-[[(1E)-(4-fluorophenyl)methylene]amino]-2-phenylquinazolin-4(3H)-one
-
low inhibitory activity
4-methyl-N-(2-methyl-4-oxoquinazolin-3(4H)-yl)benzamide
-
low inhibitory activity
5-bromo-N-(4-bromophenyl)-2-hydroxy-3-nitro-benzamide
-
competitive
carbobenzoxy-L-Phe
-
crystallographic study of the binding to thermolysin
carbobenzoxy-L-phenylalanine-phosphonamidate-L-leucyl-L-alanine
a potent phosphonamidate transition state analogue inhibitor
ClCH2CO-DL-(N-OH)Leu-OCH3
-
specific, irreversible, pH-dependence of inhibition
Cu2+-Cys-Gly-His-Lys
-
stimulation at concentration up to 0.01 mM, inhibition at higher concentrations of 0.01-0.1 mM, binding and kinetics, overview
ethanimidic acid N-[4-oxo-2-phenyl-3(4H)-quinazolinyl]-ethyl ester
-
-
ethyl (4-oxo-3,4-dihydroquinazolin-2-yl)acetate
-
low inhibitory activity
Hydroxamic acid inhibitors
-
binding to thermolysin suggests a pentacoordinate zinc intermediate
-
methyl 2-[(trifluoroacetyl) amino] benzoate
-
low inhibitory activity
N-(2,3-dimethylphenyl)-2-hydroxy-3-nitro-benzamide
-
competitive
N-(2,4-dimethylphenyl)-2-hydroxy-3-nitro-benzamide
-
competitive
N-(2-chloro-4-nitrophenyl)-2-hydroxy-3-nitro-benzamide
-
competitive
N-(2-chloro-6-methylphenyl)-2-hydroxy-3-nitrobenzamide
-
competitive
N-(2-methyl-4-oxoquinazolin-3(4H)-yl)acetamide
-
low inhibitory activity
N-(2-methyl-4-oxoquinazolin-3(4H)-yl)benzamide
-
low inhibitory activity
N-(2-phenyl-4-oxoquinazolin-3(4H)-yl)acetamide
-
low inhibitory activity
N-(5-chloro-2-methoxyphenyl)-2-hydroxy-3-nitro-benzamide
-
competitive
N-Benzyloxycarbonyl-L-phenylalanine
-
binding mechanism in aqueous solution, NMR and spectrophotometric analysis, overview. Substitution of Zn2+ by Co2+ decreases the binding affinity of the inhibitor, overview
N-benzyloxycarbonyl-L-tryptophan
-
binding mechanism in aqueous solution, NMR and spectrophotometric analysis, overview. Substitution of Zn2+ by Co2+ decreases the binding affinity of the inhibitor, overview. With thermolysin, a 1 M concentration of NaSCN produces an 2fold increase in its Ki value from 0.087 mM to 0.19 mM for the inhibitor N-benzyloxycarbonyl-tryptophan
n-Pentanol
-
saturation concentration of activation at 60%, inhibition at higher concentration
N-[(2R)-1-(hydroxyamino)-3-methyl-1-oxobutan-2-yl]-N-[(4-phenoxyphenyl)sulfonyl]glycine
-
-
Z-L-phenylalanine
-
enzyme binding structure and kinetics, chemical shift of the carboxylate carbon upon enzyme binding, overview. The carbobenzyloxyl protecting group and not the phenylalanyl phenyl group that is bound in the S1' specificity pocket and the alpha carboxylate group is directly coordinated to the active site zinc atom
Z-L-tryptophan
-
inhibits full length stromelysin_1-477 and truncated stromelysin_100-264, enzyme binding structure and kinetics, chemical shift of the carboxylate carbon upon enzym ebinding, overview. The tryptophan side chain can bind in the S1 specificity site of stromelysin with the tryptophan alpha carboxylate group coordinated to the active site zinc atom. L-tryptophan binds equally strongly to zinc or cobalt substituted thermolysin
[(biphenyl-4-ylmethyl)[2-(hydroxyamino)-2-oxoethyl]amino]acetic acid
-
-
[(biphenyl-4-ylsulfonyl)[2-(hydroxyamino)-2-oxoethyl]amino]acetic acid
-
-
[1-[2-(hydroxyamino)-2-oxoethyl]-2-[3-(4-phenylpiperazin-1-yl)propyl]hydrazinyl]acetic acid
-
-
[[(4-methoxyphenyl)sulfonyl](2-oxo-2-[[2-(4-sulfamoylphenyl)ethyl]amino]ethyl)amino]acetic acid
-
-
[[2-(hydroxyamino)-2-oxoethyl](4-nitrobenzyl)amino]acetic acid
-
-
[[2-(hydroxyamino)-2-oxoethyl](4-phenoxybenzyl)amino]acetic acid
-
-
[[2-(hydroxyamino)-2-oxoethyl][(4-methoxyphenyl)sulfonyl]amino]acetic acid
-
-
[[2-(hydroxyamino)-2-oxoethyl][(4-phenoxyphenyl)sulfonyl]amino]acetic acid
-
-
-
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+
-
competitive, 72% inhibition at 18 mM, partial protection or reverse effect by Ca2+ at 0.5 mM, Co2+ show partly Ca2+-sensitive and partly Ca2+-insensitive inhibition, molecular mechanism, Co21 accelerates the autolysis, overview
dipeptides
-
crystallographic study of the binding to thermolysin
N-chloroacetyl-N-hydroxyleucine methyl ester
-
irreversible inhibition
N-chloroacetyl-N-hydroxyleucyl-alanyl-glycinamide
-
irreversible inhibition
-
thermolysin-inhibitor complexes examined by NMR spectroscopy
phosphoramidon
-
i.e. N-(alpha-L-rhamnopyranosyloxyphospho)-L-Leu-L-Trp, thermolysin-inhibitor complexes examined by NMR spectroscopy
phosphoramidon
-
specific inhibitor; the OH-group is not essential for the binding to thermolysin
phosphoramidon
-
crystallographic study of the complex of phosphoramidon with thermolysin
Zn2+
zinc metalloprotease, no effect on activity by exogenous Zn2+ at 1 mM, inhibitory by 69% at 5 mM
-
the active site zinc atom is tetrahedrally coordinated when the inhibitors N-benzyloxycarbonyl-tryptophan or N-benzyloxycarbonyl-phenylalanine are bound to thermolysin. pH dependencies of inhibitors N-benzyloxycarbonyl-tryptophan or N-benzyloxycarbonyl-phenylalanine and binding to thermolysin, detailed overview
-
additional information
-
identification of inhibitors by structure based virtual screening and study of binding modes by docking
-
additional information
-
not inhibited by 2-phenyl-3-[(E)-phenyldiazenyl]-1,2,3,4-tetrahydro-10H[1,2,4]triazino[6,1b]-quinazolin-10-one, 3-mesityl-2-phenylquinazolin-4(3H)-one, 3-(2-hydroxyethyl)-2-methylquinazolin-4(3H)-one, and 3-amino-2-phenylquinazolin-4(3H)-one
-
additional information
not inhibited by 3-hydroxy-2-methylthieno[3,2-d]pyrimidine-4(3H)-one and 3-(acetylamino)-4-methylthiophene-2-carboxylic acid
-
additional information
binding of inhibitors to the active site of thermolysin, structure overview
-
additional information
-
inhibitor synthesis, docking analysis and binding structure, molecular modeling, overview. When the compounds possess two ring systems, the largest and most electron rich ring system seems to occupy the S1-subpocket. The fourth zinc coordinating ligand in the free enzyme is a water molecule. Upon inhibitor binding this water molecule is replaced by a metal binding group of the inhibitor
-
additional information
-
not inhibitory: human blood serpins alpha-1-antitrypsin and alpha-1-antichymotrypsin
-