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
3.4.24.27 thermolysinAdvanced search results
results (
results (Substrates Products
Substrates Products 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.
top
SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(7-methoxycoumarin-4-yl) acetyl-L-Pro-L-Leu-Gly-L-Leu-[N3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-L-Ala-L-Arg-NH2 + H2O
?
(7-methoxycoumarin-4-yl)acetyl-Arg-Pro-Pro-Gly-Phe-Ser-Ala-Phe-Lys-(2,4-dinitrophenyl)-OH + H2O
?
-
a bradykinin-like substrate
-
-
?
(7-methoxycoumarin-4yl) acetyl-L-Pro-L-Leu-Gly-L-Leu-[N3-(2,4-dinitrophenyl)-L-2,3-diamino-propionyl]-L-Ala-L-Arg-NH2 + H2O
?
-
-
-
-
?
(europium(III) complex of a modified terpyridine)-K1K1K1-GFSAK1K1K-black hole quencher 2 + H2O
?
-
thermolysin cleaves the substrates at the glycine-phenylalanine bond
-
-
?
(europium(III) complex of a modified terpyridine)-K1K2K2GFSAK2K-black hole quencher 2 + H2O
?
-
thermolysin cleaves the substrates at the glycine-phenylalanine bond
-
-
?
(europium(III) complex of a modified terpyridine)-K1K2K2GFSAK2K2K-black hole quencher 2 + H2O
?
-
thermolysin cleaves the substrates at the glycine-phenylalanine bond
-
-
?
2-hydroxy-N-(4-methyl-2-nitrophenyl)-3-nitrobenzamide + H2O
?
-
-
-
-
?
2-N-(4-[4'-N',N'-(dimethylamino)phenylazo]-benzoyl-L-serinyl-L-phenylalanylamido)-N''-ethylaminonaphthalene-5-sulfonic acid + H2O
?
-
-
-
?
5,6-carboxyfluorescein-PAGLAC(Alexa Fluor 647)-NH2 + H2O
5,6-carboxyfluorescein-PAG + LAC(Alexa Fluor 647)-NH2
-
-
-
-
?
5,6-carboxyfluorescein-PAGLAC(Cy5)-NH2 + H2O
5,6-carboxyfluorescein-PAG + LAC(Cy5)-NH2
-
-
-
-
?
5,6-carboxyfluorescein-PSVAGLAGGC(Alexa Fluor 647)-NH2 + H2O
5,6-carboxyfluorescein-PSVAG + LAGGC(Alexa Fluor 647)-NH2
-
-
-
-
?
5,6-carboxyfluorescein-PSVAGLAGGC(Cy5)-NH2 + H2O
5,6-carboxyfluorescein-PSVAG + LAGGC(Cy5)-NH2
-
-
-
-
?
5,6-carboxyfluorescein-PVAGLAGC(Cy5)-NH2 + H2O
5,6-carboxyfluorescein-PVAG + LAGC(Cy5)-NH2
-
-
-
-
?
5-bromo-N-(4-bromophenyl)-2-hydroxy-3-nitro-benzamide + H2O
?
-
-
-
-
?
Ac-Gly-Leu-Ala-methylamide + H2O
?
-
model substrate, enzyme-substrate complex, docking structures, overview
-
-
ir
alpha-1-antichymotrypsin + H2O
?
-
cleavage within the sequence LSA-LVE
-
-
?
alpha-1-antitrypsin + H2O
?
-
cleavage within the sequence AMF-LEA
-
-
?
alphaS1-casein + H2O
caseicin A + ?
-
-
antimicrobial peptide product caseicin A = IKHQGLPQE
-
?
bovine alpha-lactalbumin + H2O
?
-
reaction at 25°C and 70°C under nonreducing conditions. At 25°C, substrate undergoes limited hydrolysis leading to peptides no longer degraded. At 70°C, protein is first quickly cleaved, then unfolded, leading to the release of intermediate peptides that may be further degraded
-
-
?
bovine beta-lactoglobulin A + H2O
?
-
analysis of 25 peptides released by enzyme at 37°C, comparison with peptides relased at 25°C, 60 and 80°C. Test of peptides for angiotensin-converting enzyme inhibiting activity
-
-
?
carbobenzoxy-L-aspartic acid + L-phenylalanine methyl ester
carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester
condensation, the enzyme is enantioselective for the desired L-phenylalanine methyl ester substrate from a racemic mixture of DL-phenylalanine methyl ester. In contrast, although both enantiomers of carbobenzoxy-L-aspartic acid can bind to the enzyme, only carbobenzoxy-L-aspartic acid is used since carbobenzoxy-D-aspartic acid inhibits the enzyme, substrate carbobenzoxy-L-aspartic acid binding structures, detailed overview
precipitation as the water-insoluble Phe-OMe salt drives the overall reaction in the direction of peptide synthesis
-
?
cellular prion protein + H2O
?
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
-
-
?
DL-phenylalanine methyl ester + L-aspartic acid
D-phenylalanine methyl ester + L-alpha-aspartame
-
-
-
-
?
furylacryloyl-Gly-Leu-NH2 + H2O
furylacryloyl-Gly + Leu-NH2
-
-
-
-
?
Mca-Arg-Pro-Pro-Gly-Phe-Ser-Ala-Phe-Lys(Dnp)-OH + H2O
?
-
-
-
-
?
N,N'-diBoc-dityrosyl-(Ile-isoniazid)2 + H2O
N,N'-diBoc-dityrosyl + 2 Ile-isoniazid
-
-
-
-
?
N,N'-diBoc-dityrosyl-(Phe-isoniazid)2 + H2O
N,N'-diBoc-dityrosyl + 2 Phe-isoniazid
-
-
-
-
?
N-(2,3-dimethylphenyl)-2-hydroxy-3-nitro-benzamide + H2O
?
-
-
-
-
?
N-(2,4-dimethylphenyl)-2-hydroxy-3-nitro-benzamide + H2O
?
-
-
-
-
?
N-(2,5-dimethylphenyl)-2-hydroxy-3-nitrobenzamide + H2O
?
-
-
-
-
?
N-(2-chloro-4-nitrophenyl)-2-hydroxy-3-nitro-benzamide + H2O
?
-
-
-
-
?
N-(2-chloro-6-methylphenyl)-2-hydroxy-3-nitrobenzamide + H2O
?
-
-
-
-
?
N-(5-chloro-2-methoxyphenyl)-2-hydroxy-3-nitro-benzamide + H2O
?
-
-
-
-
?
N-(Benzyloxycarbonyl)-L-Phe + L-Phe methyl ester
N-(Benzyloxycarbonyl)-L-Phe-L-Phe methyl ester + H2O
N-benzyloxycarbonyl-Gly-L-Leu amide + H2O
N-benzyloxycarbonyl-Gly + L-Leu amide
-
-
-
-
?
N-benzyloxycarbonyl-L-Asp-L-Phe-methyl ester + H2O
N-benzyloxycarbonyl-L-Asp + L-Phe-methyl ester
-
-
-
-
?
N-carbobenzoxy-L-Asp-L-Phe-methyl ester + H2O
?
-
-
-
-
?
N-carbobenzoxy-L-Asp-L-Phe-methyl ester + H2O
N-carbobenzoxy-L-aspartic acid + L-phenylalanine methyl ester
-
-
-
-
r
N-carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester + H2O
?
-
-
-
?
N-carboxybenzoyl-L-aspartyl-L-phenylalanine methyl ester + H2O
?
-
-
-
?
N-[3-(2-furyl)acryloyl]-glycyl-L-leucine amide + H2O
N-[3-(2-furyl)acryloyl]-glycine + L-leucine amide
N-[3-(2-furyl)acryloyl]-L-leucine-L-alanine amide + H2O
?
-
i.e. FALAA
-
-
?
Nalpha-benzyloxycarbonyl-L-aspartyl-L-phenylalanine methyl ester + H2O
?
-
-
-
?
Oxidized insulin B-chain + H2O
?
-
major cleavage at the peptide bonds of His5-Leu6, His10-Leu11, Ala14-Leu15, Tyr16-Leu17, Leu17-Val18, Gly23-Phe24, Phe24-Phe25, Phe25-Tyr26
-
-
?
Pro-urokinase + H2O
?
-
thermolysin activates thrombin-inactivated pro-urokinase nearly as rapidly as it does the native zymogen, cleavage of Arg156-Phe157 and Lys158-Ile159
-
-
?
(7-methoxycoumarin-4-yl) acetyl-L-Pro-L-Leu-Gly-L-Leu-[N3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-L-Ala-L-Arg-NH2 + H2O
?
-
fluorescent substrate
-
?
(7-methoxycoumarin-4-yl) acetyl-L-Pro-L-Leu-Gly-L-Leu-[N3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-L-Ala-L-Arg-NH2 + H2O
?
-
i.e. MOCAc-PLGL(Dpa)AR, fluorescent substrate
-
-
?
3-(2-furylacryloyl)-glycyl-L-leucine amide + H2O
?
-
-
-
?
3-(2-furylacryloyl)-glycyl-L-leucine amide + H2O
?
-
-
-
?
benzyloxycarbonyl-Asp + Phe-methylester
benzyloxycarbonyl-Asp-Phe methyl ester + H2O
-
-
-
?
benzyloxycarbonyl-Asp + Phe-methylester
benzyloxycarbonyl-Asp-Phe methyl ester + H2O
-
-
-
?
casein + H2O
?
-
-
-
-
?
Collagen + H2O
?
-
collagen in solid articular cartilage at 70°C. Overnight digestion with thermolysin completely solubilized cartilage. Following thermolysin treatments, almost all glycosaminoglycans are extracted from the cartilage
-
-
?
complement component C3 + H2O
?
proteolytic activity of thermolysin against C3 is time and dose-dependent
-
-
?
complement component C3 + H2O
?
Leptospira interrogans serovar Copenhageni Fiocruz L1-130
proteolytic activity of thermolysin against C3 is time and dose-dependent
-
-
?
H-Gly-Phe-Ser-Ala-Lys-Asn-Gln-Ser-Asn-Gln-Arg-OH + H2O
?
-
-
-
?
H-Gly-Phe-Ser-Ala-Lys-Asn-Gln-Ser-Asn-Gln-Arg-OH + H2O
?
-
-
-
?
H-Gly-Phe-Ser-Ala-Lys-Asn-Gln-Ser-OH + H2O
?
-
-
-
?
N-(4-methoxyphenylazoformyl)-Leu-Leu-OH + H2O
?
-
a synthetic substrate
-
-
?
N-(4-methoxyphenylazoformyl)-Leu-Leu-OH + H2O
?
-
a synthetic substrate
-
-
?
N-(Benzyloxycarbonyl)-L-Phe + L-Phe methyl ester
N-(Benzyloxycarbonyl)-L-Phe-L-Phe methyl ester + H2O
-
-
-
?
N-(Benzyloxycarbonyl)-L-Phe + L-Phe methyl ester
N-(Benzyloxycarbonyl)-L-Phe-L-Phe methyl ester + H2O
-
-
-
?
N-carbobenzoxy-L-Asp-L-Phe methyl ester + H2O
?
-
-
-
-
?
N-carbobenzoxy-L-Asp-L-Phe methyl ester + H2O
?
-
-
-
-
?
N-carbobenzoxy-L-Asp-L-Phe-methyl ester + H2O
N-carbobenzoxy-L-Asp + L-Phe-methyl ester
-
-
-
-
?
N-carbobenzoxy-L-Asp-L-Phe-methyl ester + H2O
N-carbobenzoxy-L-Asp + L-Phe-methyl ester
-
-
-
?
N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide + H2O
?
-
-
-
-
?
N-[3-(2-furyl)acryloyl]-glycyl-L-leucine amide + H2O
?
-
-
-
r
N-[3-(2-furyl)acryloyl]-glycyl-L-leucine amide + H2O
?
-
-
-
?
N-[3-(2-furyl)acryloyl]-glycyl-L-leucine amide + H2O
?
-
i.e. FAGLA
-
-
?
N-[3-(2-furyl)acryloyl]-glycyl-L-leucine amide + H2O
?
i.e. FAGLA
-
-
?
N-[3-(2-furyl)acryloyl]-glycyl-L-leucine amide + H2O
N-[3-(2-furyl)acryloyl]-glycine + L-leucine amide
-
-
-
-
?
N-[3-(2-furyl)acryloyl]-glycyl-L-leucine amide + H2O
N-[3-(2-furyl)acryloyl]-glycine + L-leucine amide
-
-
-
-
?
additional information
?
-
-
specificity overview: various synthetic peptides
-
-
?
additional information
?
-
-
the major site for thermolysin cleavage specificity, (the S1' site), accepts large hydrophobic residues. Thermolysin preferentially cleaves at the N-terminal side of hydrophobic or bulky amino side chains such as Leu, Phe, Ile and Val. Thermolysin also cleaves bonds of Met, His, Tyr, Ala, Asn, Ser, Thr, Gly, Lys, Glu or Asp at the P1' site
-
-
?
additional information
?
-
-
autodegradation at position 154155
-
-
?
additional information
?
-
-
specificity overview: various synthetic peptides
-
-
?
additional information
?
-
-
specificity overview: oligopeptides
-
-
?
additional information
?
-
-
enzyme additionally 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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
enzyme prefers basic resiudes in P3 position
-
-
?
additional information
?
-
-
digestion of brain homogenates from healthy and scrapie-affected sheep as well as healthy and BSE-affected cattle, the PK digestion results in the amino-terminal truncation of PrPSc-producing PrP species with molecular weights of approx 17, 21, and 27 kDa that can only be detected with antibodies binding to the carboxy-terminal region of PrP, the so-called protease-resistant core or PrP27-30, overview
-
-
?
additional information
?
-
-
thermolysin is a thermostable neutral metalloproteinase and performs autocatalytic cleavage for pro-enzyme activation
-
-
?
additional information
?
-
-
thermolysin performs Co2+-stimulable autolysis
-
-
?
additional information
?
-
-
the major site for thermolysin cleavage specificity, (the S1' site), accepts large hydrophobic residues. Thermolysin preferentially cleaves at the N-terminal side of hydrophobic or bulky amino side chains such as Leu, Phe, Ile and Val. Thermolysin also cleaves bonds of Met, His, Tyr, Ala, Asn, Ser, Thr, Gly, Lys, Glu or Asp at the P1' site
-
-
?
additional information
?
-
-
isolated intact chloroplast from Spinacia oleracea are treated with thermolysin, mass spectrometric analysis and two-dimensional analysis of shedded envelope proteins, including 28 kDa ribonucleoprotein, cytosolic HSP70/Com70, translocon Tic40-like protein, ClpC, HSP70, and hexokinase 1, overview
-
-
?
additional information
?
-
binding of substrates to the active site of thermolysin, overview
-
-
?
additional information
?
-
-
synthesis and evaluation of substrates useful for the selective and sensitive assay of thermolysin, overview
-
-
?
additional information
?
-
the enzyme has low affinity for alkaline or acid P1' residues, poor activity with N-[3-(2-furyl)acryloyl]-Glu-Glu-OH , no activity with N-[3-(2-furyl)acryloyl]-Ala-Arg-OH
-
-
?
additional information
?
-
the enzyme has low affinity for alkaline or acid P1' residues, poor activity with N-[3-(2-furyl)acryloyl]-Glu-Glu-OH , no activity with N-[3-(2-furyl)acryloyl]-Ala-Arg-OH
-
-
?
additional information
?
-
-
thermolysin selectively digests the dermo-epidermal junction of epidermal sheets used for burnt persons, overview
-
-
?
additional information
?
-
-
specificity overview: hydrolyzes peptide bonds with amino groups of hydrophobic amino acids (Phe, Leu, Ala, Val, Ile but not Trp)
-
-
?
additional information
?
-
-
specificity overview: no exopeptidase activity
-
-
?
additional information
?
-
-
preferentially, peptide bonds preceding hydrophobic residues are hydrolyzed, such as I, L or F at P1' position. The enzyme less frequently also cleaves substrates with hydrophilic residues such as E, T or Q in the P1' position
-
-
?
