Information on EC 3.4.24.27 - thermolysin

Word Map on EC 3.4.24.27
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
3.4.24.27
-
RECOMMENDED NAME
GeneOntology No.
thermolysin
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
preferential cleavage: -/-Leu > -/-Phe
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
9073-78-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
antarctic bacterium
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
archaebacterium
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
Bacillus proteolyticus
-
-
-
Manually annotated by BRENDA team
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
strain MK232, genes npr and nprT
-
-
Manually annotated by BRENDA team
-
-
-
Automatic Mining of ENzyme DAta
isolated from a marine sediment of South China Sea, gene HSPA
UniProt
Manually annotated by BRENDA team
isolated from a marine sediment of South China Sea, gene HSPA
UniProt
Manually annotated by BRENDA team
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
quail
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
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
-
thermolysin family proteases are related to various diseases such as bacterial infections, cholera, gastritis and peptic ulcers, and gastric carcinoma
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
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
?
show the reaction diagram
(7-methoxycoumarin-4-yl)acetyl-Arg-Pro-Pro-Gly-Phe-Ser-Ala-Phe-Lys-(2,4-dinitrophenyl)-OH + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
-
-
-
?
(europium(III) complex of a modified terpyridine)-K1K1K1-GFSAK1K1K-black hole quencher 2 + H2O
?
show the reaction diagram
-
thermolysin cleaves the substrates at the glycine-phenylalanine bond
-
-
?
(europium(III) complex of a modified terpyridine)-K1K2K2GFSAK2K-black hole quencher 2 + H2O
?
show the reaction diagram
-
thermolysin cleaves the substrates at the glycine-phenylalanine bond
-
-
?
(europium(III) complex of a modified terpyridine)-K1K2K2GFSAK2K2K-black hole quencher 2 + H2O
?
show the reaction diagram
-
thermolysin cleaves the substrates at the glycine-phenylalanine bond
-
-
?
1-beta-D-arabinofuranosyl-N4-lauroylcytosine + H2O
?
show the reaction diagram
-
-
-
-
?
11S soy protein + H2O
?
show the reaction diagram
-
-
-
-
?
2-hydroxy-N-(4-methyl-2-nitrophenyl)-3-nitrobenzamide + H2O
?
show the reaction diagram
-
-
-
-
?
2-N-(4-[4'-N',N'-(dimethylamino)phenylazo]-benzoyl-L-serinyl-L-phenylalanylamido)-N''-ethylaminonaphthalene-5-sulfonic acid + H2O
?
show the reaction diagram
-
-
-
-
?
3-(2-furylacryloyl)-glycyl-L-leucine amide + H2O
?
show the reaction diagram
5-bromo-N-(4-bromophenyl)-2-hydroxy-3-nitro-benzamide + H2O
?
show the reaction diagram
-
-
-
-
?
7S soy protein + H2O
?
show the reaction diagram
-
-
-
-
?
Ac-Gly-Leu-Ala-methylamide + H2O
?
show the reaction diagram
-
model substrate, enzyme-substrate complex, docking structures, overview
-
-
ir
alpha-1-antichymotrypsin + H2O
?
show the reaction diagram
-
cleavage within the sequence LSA-LVE
-
-
?
alpha-1-antitrypsin + H2O
?
show the reaction diagram
-
cleavage within the sequence AMF-LEA
-
-
?
alphaS1-casein + H2O
caseicin A + ?
show the reaction diagram
-
-
antimicrobial peptide product caseicin A = IKHQGLPQE
-
?
azocasein + H2O
?
show the reaction diagram
Azocoll + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-(4-nitro)Phe-Leu-Ala + H2O
?
show the reaction diagram
-
-
-
-
-
benzyloxycarbonyl-Asp + Phe-methylester
benzyloxycarbonyl-Asp-Phe methyl ester + H2O
show the reaction diagram
benzyloxycarbonyl-Gly-(4-nitro)Phe-Leu-Ala + H2O
?
show the reaction diagram
-
-
-
-
-
benzyloxycarbonyl-Gly-Gly-(4-nitro)Phe-Leu-Ala + H2O
?
show the reaction diagram
-
-
-
-
-
benzyloxycarbonyl-Gly-Gly-Phe-Leu-Ala + H2O
?
show the reaction diagram
-
-
-
-
-
benzyloxycarbonyl-Gly-Phe-Leu-Ala + H2O
?
show the reaction diagram
-
-
-
-
-
benzyloxycarbonyl-Phe-Leu-Ala + H2O
?
show the reaction diagram
-
-
-
-
-
bovine alpha-lactalbumin + H2O
?
show the reaction diagram
-
reaction at 25C and 70C under nonreducing conditions. At 25C, substrate undergoes limited hydrolysis leading to peptides no longer degraded. At 70C, protein is first quickly cleaved, then unfolded, leading to the release of intermediate peptides that may be further degraded
-
-
?
bovine beta-lactoglobulin A + H2O
?
show the reaction diagram
-
analysis of 25 peptides released by enzyme at 37C, comparison with peptides relased at 25C, 60 and 80C. Test of peptides for angiotensin-converting enzyme inhibiting activity
-
-
?
Bovine serum albumin + H2O
?
show the reaction diagram
Carbobenzoxy-Gly-Pro-Leu-Ala-Pro + H2O
?
show the reaction diagram
-
-
-
-
-
carbobenzoxy-L-aspartic acid + L-phenylalanine methyl ester
carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester
show the reaction diagram
-
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
-
?
casein + H2O
?
show the reaction diagram
casein + H2O
L-tyrosine + ?
show the reaction diagram
cellular prion protein + H2O
?
show the reaction diagram
-
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
-
-
?
Collagen + H2O
?
show the reaction diagram
Dansyl peptides + H2O
?
show the reaction diagram
-
-
-
-
-
Dansyl-Gly-Phe-Ala + H2O
?
show the reaction diagram
-
-
-
-
-
DL-phenylalanine methyl ester + L-aspartic acid
D-phenylalanine methyl ester + L-alpha-aspartame
show the reaction diagram
Bacillus proteolyticus
-
-
-
-
-
Elastin + H2O
?
show the reaction diagram
F-Asp-PheOMe + H2O
?
show the reaction diagram
-
dipeptide synthesis
-
r
FA-glycyl-L-leucine amide + H2O
?
show the reaction diagram
-
-
-
?
feather + H2O
?
show the reaction diagram
-
-
-
?
furylacryloyl-Gly-Leu-NH2 + H2O
furylacryloyl-Gly + Leu-NH2
show the reaction diagram
-
-
-
-
-
Gelatin + H2O
?
show the reaction diagram
GFA + H2O
Phe-Ala + Gly
show the reaction diagram
-
-
-
?
GFS + H2O
Gly + Phe-Ser
show the reaction diagram
GFSA + H2O
?
show the reaction diagram
GFSA + H2O
Gly-Phe + Phe-Ser-Ala + Gly + Ser-Ala
show the reaction diagram
-
-
-
?
GFSAK + H2O
?
show the reaction diagram
GFSAKN + H2O
?
show the reaction diagram
GFSAKNQS + H2O
?
show the reaction diagram
Gly-Phe-Leu + H2O
Phe-Leu + Gly-Phe + Gly + Leu
show the reaction diagram
-
-
-
?
H-Gly-Phe-Ala-OH + H2O
?
show the reaction diagram
H-Gly-Phe-Leu-OH + H2O
?
show the reaction diagram
H-Gly-Phe-Ser-Ala-Lys-Asn-Gln-Ser-Asn-Gln-Arg-OH + H2O
?
show the reaction diagram
H-Gly-Phe-Ser-Ala-Lys-Asn-Gln-Ser-OH + H2O
?
show the reaction diagram
H-Gly-Phe-Ser-OH + H2O
?
show the reaction diagram
H-Gly-Ser-Ala-OH + H2O
?
show the reaction diagram
-
-
-
?
Hemoglobin + H2O
?
show the reaction diagram
hide powder azure + H2O
?
show the reaction diagram
-
-
-
-
?
leucine enkephalin + H2O
?
show the reaction diagram
Mca-Arg-Pro-Pro-Gly-Phe-Ser-Ala-Phe-Lys(Dnp)-OH + H2O
?
show the reaction diagram
-
-
-
-
?
N'-[3-(2-furyl)acryloyl]glycyl-L-leucinamide + H2O
?
show the reaction diagram
-
-
-
-
?
N,N'-diBoc-dityrosyl-(Ile-isoniazid)2 + H2O
N,N'-diBoc-dityrosyl + 2 Ile-isoniazid
show the reaction diagram
-
-
-
-
?
N,N'-diBoc-dityrosyl-(Phe-isoniazid)2 + H2O
N,N'-diBoc-dityrosyl + 2 Phe-isoniazid
show the reaction diagram
-
-
-
-
?
N-(2,3-dimethylphenyl)-2-hydroxy-3-nitro-benzamide + H2O
?
show the reaction diagram
-
-
-
-
?
N-(2,4-dimethylphenyl)-2-hydroxy-3-nitro-benzamide + H2O
?
show the reaction diagram
-
-
-
-
?
N-(2,5-dimethylphenyl)-2-hydroxy-3-nitrobenzamide + H2O
?
show the reaction diagram
-
-
-
-
?
N-(2-chloro-4-nitrophenyl)-2-hydroxy-3-nitro-benzamide + H2O
?
show the reaction diagram
-
-
-
-
?
N-(2-chloro-6-methylphenyl)-2-hydroxy-3-nitrobenzamide + H2O
?
show the reaction diagram
-
-
-
-
?
N-(2-ethylphenyl)-2-hydroxy-3-nitrobenzamide + H2O
?
show the reaction diagram
-
-
-
-
?
N-(4-methoxyphenylazoformyl)-Leu-Leu-OH + H2O
?
show the reaction diagram
N-(5-chloro-2-methoxyphenyl)-2-hydroxy-3-nitro-benzamide + H2O
?
show the reaction diagram
-
-
-
-
?
N-(Benzyloxycarbonyl)-L-Phe + L-Phe methyl ester
N-(Benzyloxycarbonyl)-L-Phe-L-Phe methyl ester + H2O
show the reaction diagram
N-benzyloxycarbonyl-Gly-L-Leu amide + H2O
N-benzyloxycarbonyl-Gly + L-Leu amide
show the reaction diagram
-
-
-
-
?
N-benzyloxycarbonyl-L-Asp-L-Phe-methyl ester + H2O
N-benzyloxycarbonyl-L-Asp + L-Phe-methyl ester
show the reaction diagram
-
-
-
-
?
N-carbobenzoxy-Gly-L-Leu-NH2 + H2O
?
show the reaction diagram
-
-
-
-
?
N-carbobenzoxy-L-Asp-L-Phe methyl ester + H2O
?
show the reaction diagram
N-carbobenzoxy-L-Asp-L-Phe-methyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
N-carbobenzoxy-L-Asp-L-Phe-methyl ester + H2O
N-carbobenzoxy-L-Asp + L-Phe-methyl ester
show the reaction diagram
-
-
-
-
?
N-carbobenzoxy-L-Asp-L-Phe-methyl ester + H2O
N-carbobenzoxy-L-aspartic acid + L-phenylalanine methyl ester
show the reaction diagram
-
-
-
-
r
N-carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
N-carbobenzyloxy-L-Asp-L-Phe methyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
N-carboxybenzoyl-L-aspartyl-L-phenylalanine methyl ester + H2O
?
show the reaction diagram
-
-
-
?
N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide + H2O
?
show the reaction diagram
-
-
-
-
?
N-[3-(2-furyl)acryloyl]-Gly-L-Leu-NH2 + H2O
?
show the reaction diagram
N-[3-(2-furyl)acryloyl]-Gly-Phe-NH2 + H2O
?
show the reaction diagram
-
-
-
?
N-[3-(2-furyl)acryloyl]-glycyl-L-leucine amide + H2O
?
show the reaction diagram
N-[3-(2-furyl)acryloyl]-glycyl-L-leucine amide + H2O
N-[3-(2-furyl)acryloyl]-glycine + L-leucine amide
show the reaction diagram
N-[3-(2-furyl)acryloyl]-L-leucine-L-alanine amide + H2O
?
show the reaction diagram
-
i.e. FALAA
-
-
?
N-[3-(2-furyl)acryloyl]-Phe-Ala amide + H2O
?
show the reaction diagram
-
-
-
?
N-[3-(2-furyl)acryloyl]glycyl-L-leucinamide + H2O
?
show the reaction diagram
-
-
-
-
?
Nalpha-benzyloxycarbonyl-L-aspartyl-L-phenylalanine methyl ester + H2O
?
show the reaction diagram
-
-
-
?
Oxidized insulin B-chain + H2O
?
show the reaction diagram
-
major cleavage at the peptide bonds of His5-Leu6, His10-Leu11, Ala14-Leu15, Tyr16-Leu17, Leu17-Val18, Gly23-Phe24, Phe24-Phe25, Phe25-Tyr26
-
-
-
oxyquinoline + H2O
?
show the reaction diagram
-
-
-
-
?
Pro-urokinase + H2O
?
show the reaction diagram
-
thermolysin activates thrombin-inactivated pro-urokinase nearly as rapidly as it does the native zymogen, cleavage of Arg156-Phe157 and Lys158-Ile159
-
-
-
soy protein isolate + H2O
?
show the reaction diagram
-
-
-
-
?
tryptic hydrolysate of bovine beta casein + H2O
?
show the reaction diagram
-
-
-
-
?
Tyr-Gly-Gly-Phe-Leu + H2O
?
show the reaction diagram
-
-
-
?
Z-Arg-PheOMe + H2O
?
show the reaction diagram
-
dipeptide synthesis
-
?
[3H]leucine enkephalin + H2O
?
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
N-carbobenzoxy-L-Asp-L-Phe-methyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ba2+
activates 8% at 1 mM, 15% at 5 mM
K+
-
activates, preference of monovalent cations in descending order: Na+, K+, Li+
Li+
-
activates, preference of monovalent cations in descending order: Na+, K+, Li+
Mg2+
activates 12% at 1 mM, 37% at 5 mM
Mn2+
activates 12% at 1 mM, 25% at 5 mM
NaBr
-
4 M enhances activity 13-15 times
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
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(E)-N-(naphthalen-1-yl)-N'-(4-oxo-2-phenylquinazolin-3(4H)-yl)acetimidamide
-
low inhibitory activity
1,10-phenanthroline
1-beta-D-arabinofuranosyl-N4-lauroylcytosine
-
competitive
1-butanol
1-propanol
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-(acetyloxy)-3-chlorobenzoic acid
-
-
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-butanol
2-chloro-N-(2-methyl-4-oxoquinazolin-3(4H)-yl)acetamide
-
low inhibitory activity
2-ethyl-3-hydroxyquinazolin-4(3H)-one
-
-
2-ethylquinazolin-4(3H)-one
-
-
2-hydroxy-N-(4-methyl-2-nitrophenyl)-3-nitrobenzamide
-
competitive
2-methyl-1-propanol
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-phenylpropionyl-L-phenylalanine
-
-
2-phenylpropionyl-Leu-Trp
-
-
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-(4-chlorophenyl)quinazolin-4(3H)-one
-
-
3-amino-2-(4-nitrophenyl)quinazolin-4(3H)-one
-
-
3-amino-2-(hydrazinomethyl) quinazolin-4(3H)-one
-
low inhibitory activity
3-amino-2-(trifluoromethyl) quinazolin-4(3H)-one
-
-
3-amino-2-methylquinazolin-4(3H)-one
-
-
3-hydroxy-2-isopropylquinazolin-4(3H)-one
-
-
3-hydroxy-2-methylquinazolin-4(3H)-one
-
-
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
alpha2-Macroglobulin
-
-
-
beta-phenylpropionyl-L-phenylalanine
-
-
-
Bifunctional N-carboxyalkyl dipeptides
-
-
-
carbobenzoxy-D-aspartic acid
-
-
-
carbobenzoxy-L-aspartic acid
-
substrate inhibition
-
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
-
Cbz-Gly-PSI[P(O)OH]-Leu-Leu
-
-
Cbz-Phe-PSI[P(O)OH]-Leu-Ala
-
-
ClCH2CO-DL-(N-OH)Leu-OCH3
-
specific, irreversible, pH-dependence of inhibition
Cu2+
39% inhibition at 1 mM, 52% at 5 mM
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
dimethylformamide
-
-
dipeptides
EGTA
59% inhibition at 1 mM, 98% at 5 mM
ethanimidic acid N-[4-oxo-2-phenyl-3(4H)-quinazolinyl]-ethyl ester
-
-
ethyl (4-oxo-3,4-dihydroquinazolin-2-yl)acetate
-
low inhibitory activity
Gly-D-Phe
HONH-benzylmalonyl-L-Ala-Gly-NH2
-
-
-
Hydroxamic acid inhibitors
-
binding to thermolysin suggests a pentacoordinate zinc intermediate
-
methyl 2-[(trifluoroacetyl) amino] benzoate
-
low inhibitory activity
N-(1-carboxy-3-phenyl-propyl)-L-leucyl-L-tryptophan
-
-
-
N-(1-Carboxy-3-phenylpropyl)-Leu-Trp
-
-
N-(2,3-dimethylphenyl)-2-hydroxy-3-nitro-benzamide
-
competitive
N-(2,4-dimethylphenyl)-2-hydroxy-3-nitro-benzamide
-
competitive
N-(2,5-dimethylphenyl)-2-hydroxy-3-nitrobenzamide
-
competitive
N-(2-chloro-4-nitrophenyl)-2-hydroxy-3-nitro-benzamide
-
competitive
N-(2-chloro-6-methylphenyl)-2-hydroxy-3-nitrobenzamide
-
competitive
N-(2-ethylphenyl)-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-chloroacetyl-N-hydroxyleucine methyl ester
N-chloroacetyl-N-hydroxyleucyl-alanyl-glycinamide
n-Pentanol
-
saturation concentration of activation at 60%, inhibition at higher concentration
N-Phosphoryl-Ile-Ala-OH
-
-
N-Phosphoryl-L-Leu amide
N-Phosphoryl-L-Leu-L-Trp
-
specific inhibitor
N-Phosphoryl-Leu-Phe-OH
-
-
N-Phosphoryl-Leu-Trp-OH
-
-
N-[(2R)-1-(hydroxyamino)-3-methyl-1-oxobutan-2-yl]-N-[(4-phenoxyphenyl)sulfonyl]glycine
-
-
N-[[[benzyloxycarbonyl]amino]methyl]hydroxyphosphinyl-L-Phe
-
-
Ni2+
39% inhibition at 1 mM, 87% at 5 mM
Peptide hydrazides
-
-
-
Peptide hydroxamic acids
-
-
-
Peptides containing zinc coordination ligands
-
-
-
Phosphonamidates
-
phosphoramidon
tert-butyl alcohol
-
-
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
-
Zincov
-
competitive inhibitor
[(2S)-2-sulfanyl-3-phenylpropanoyl]Gly-(5-Ph)Pro
-
-
[(2S)-2-sulfanyl-3-phenylpropanoyl]Phe-Tyr
-
-
[(2S,R)-2-sulfanylheptanoyl]Phe-Ala
-
-
[(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
-
-
[Co(acacen)(NH3)2]Cl
-
irreversible inhibition
[[(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
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
-
accelerated hydrolysis of some tryptic peptides derived from bovine beta-casein in presence of Ca2+, while other peptides are not affected
Calcium
-
supplementation of growth medium by calcium induces expression. Regulation by calcium ions is at posttranscriptional level
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
Cys-Gly-His-Lys
-
activation
n-Pentanol
-
saturation concentration of activation at 60%, inhibition at higher concentration
NaCl
-
up to 40fold increase in activity in presence of 4 M NaCl, substrate MOCAc-PLGL(Dpa)AR. Degree of activation depends on substrate
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.002
(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
-
pH and temperature not specified in the publication
0.00449
(europium(III) complex of a modified terpyridine)-K1K2K2GFSAK2K-black hole quencher 2
-
pH and temperature not specified in the publication
-
0.65 - 0.72
Benzyloxycarbonyl-(4-nitro)Phe-Leu-Ala
-
depending on mode of preparation of the form of enzyme
2.8
Benzyloxycarbonyl-Asp
-
pH 5.0 or pH 6.0
0.033 - 0.076
Benzyloxycarbonyl-Asp-Phe methyl ester
0.98 - 1.39
Benzyloxycarbonyl-Gly-Phe-Leu-Ala
-
depending on mode of preparation of the form of enzyme
0.55 - 1.52
Benzyloxycarbonyl-Phe-Leu-Ala
-
depending on mode of preparation of the form of enzyme
0.2
dansyl-Ala-Ala-Phe-Ala
-
-
2
dansyl-Ala-Leu-Ala
-
-
0.91
dansyl-Ala-Phe-Ala
-
-
13
dansyl-Gly-Gly-Leu-Gly
-
-
5
dansyl-Gly-Leu-Gly
-
-
0.69
dansyl-Gly-Leu-Phe
-
-
0.08 - 0.09
Dansyl-Gly-Phe-Ala
-
depending on assay method
0.77
dansyl-Gly-Phe-Gly
-
-
0.3
dansyl-Gly-Phe-Phe
0.6
GFA
-
pH 8.0, 37C, 5 M glycerol
0.4 - 2.5
GFL
1.3 - 3.5
GFS
0.7 - 12
GFSA
250 - 300
L-Phe methyl ester
5.8 - 12.9
L-phenylalanine methyl ester
0.2 - 1.985
leucine enkephalin
0.00395
N,N'-diBoc-dityrosyl-(Ile-isoniazid)2
-
pH 7.5, 37C
-
0.00191
N,N'-diBoc-dityrosyl-(Phe-isoniazid)2
-
pH 7.5, 37C
-
20 - 39.2
N-(Benzyloxycarbonyl)-L-Phe
12 - 20
N-benzyloxycarbonyl-Gly-L-Leu amide
0.42 - 0.57
N-benzyloxycarbonyl-L-Asp-L-Phe-methyl ester
10 - 20
N-carbobenzoxy-Gly-L-Leu-NH2
0.06 - 1.29
N-carbobenzoxy-L-Asp-L-Phe methyl ester
0.7 - 2.1
N-carbobenzoxy-L-Asp-L-Phe-methyl ester
49 - 105
N-carbobenzoxy-L-aspartic acid
0.38 - 0.49
N-carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester
-
0.77
N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
-
mutant enzyme S53D, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25C
0.62
Phe-Leu-Ala-NH(CH2)2NH-dansyl
-
-
0.2
[3H]Tyr-Gly-Gly-Phe-Leu
-
pH 8.0, 37C
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.36
(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
Bacillus thermoproteolyticus
-
pH and temperature not specified in the publication
2.6
(europium(III) complex of a modified terpyridine)-K1K2K2GFSAK2K-black hole quencher 2
Bacillus thermoproteolyticus
-
pH and temperature not specified in the publication
-
861 - 951
Benzyloxycarbonyl-(4-nitro)Phe-Leu-Ala
Bacillus thermoproteolyticus
-
depending on mode of preparation of the form of enzyme
407 - 968
Benzyloxycarbonyl-Gly-Phe-Leu-Ala
Bacillus thermoproteolyticus
-
depending on mode of preparation of the form of enzyme
362 - 605
Benzyloxycarbonyl-Phe-Leu-Ala
Bacillus thermoproteolyticus
-
depending on mode of preparation of the form of enzyme
1.4 - 1.7
Dansyl-Gly-Phe-Ala
Bacillus thermoproteolyticus
-
depending on assay method
0.06 - 0.076
GFA
0.006 - 0.045
GFL
0.035 - 0.05
GFS
0.07 - 6.08
GFSA
0.3 - 4.9
L-phenylalanine methyl ester
0.083 - 1560
leucine enkephalin
0.238
N,N'-diBoc-dityrosyl-(Ile-isoniazid)2
Bacillus thermoproteolyticus
-
pH 7.5, 37C
-
0.0463
N,N'-diBoc-dityrosyl-(Phe-isoniazid)2
Bacillus thermoproteolyticus
-
pH 7.5, 37C
-
0.556 - 1.69
N-(Benzyloxycarbonyl)-L-Phe
13.58 - 165
N-benzyloxycarbonyl-Gly-L-Leu amide
4.8 - 10.5
N-benzyloxycarbonyl-L-Asp-L-Phe-methyl ester
23.3 - 165
N-carbobenzoxy-Gly-L-Leu-NH2
1.3 - 17
N-carbobenzoxy-L-Asp-L-Phe methyl ester
1.5 - 49.4
N-carbobenzoxy-L-Asp-L-Phe-methyl ester
0.3 - 4.9
N-carbobenzoxy-L-aspartic acid
5.4 - 12
N-carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester
-
6.9
N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
Bacillus thermoproteolyticus
-
mutant enzyme S53D, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25C
additional information
additional information
-