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(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
-
-
?
1-beta-D-arabinofuranosyl-N4-lauroylcytosine + H2O
?
-
-
-
-
?
11S soy protein + H2O
?
-
-
-
-
?
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
?
-
-
-
?
3-(2-furylacryloyl)-glycyl-L-leucine amide + 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
?
-
-
-
-
?
7S soy protein + 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
-
?
Azocoll + H2O
?
-
-
-
-
?
benzyloxycarbonyl-(4-nitro)Phe-Leu-Ala + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Asp + Phe-methylester
benzyloxycarbonyl-Asp-Phe methyl ester + H2O
benzyloxycarbonyl-Gly-(4-nitro)Phe-Leu-Ala + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Gly-Gly-(4-nitro)Phe-Leu-Ala + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Gly-Gly-Phe-Leu-Ala + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Gly-Phe-Leu-Ala + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Phe-Leu-Ala + H2O
?
-
-
-
-
?
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
-
-
?
Bovine serum albumin + H2O
?
Carbobenzoxy-Gly-Pro-Leu-Ala-Pro + H2O
?
-
-
-
-
?
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
-
?
casein + H2O
L-tyrosine + ?
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
-
-
?
complement component C3 + H2O
?
Dansyl peptides + H2O
?
-
-
-
-
?
dansyl-Ala-Ala-Phe-Ala + H2O
?
-
-
-
-
?
dansyl-Ala-Leu-Ala + H2O
?
-
-
-
-
?
dansyl-Ala-Phe-Ala + H2O
?
-
-
-
-
?
dansyl-Gly-Gly-Leu-Gly + H2O
?
-
-
-
-
?
dansyl-Gly-Leu-Gly + H2O
?
-
-
-
-
?
dansyl-Gly-Leu-Phe + H2O
?
-
-
-
-
?
Dansyl-Gly-Phe-Ala + H2O
?
-
-
-
-
?
dansyl-Gly-Phe-Gly + H2O
?
-
-
-
-
?
dansyl-Gly-Phe-Phe + H2O
?
-
-
-
-
?
DL-phenylalanine methyl ester + L-aspartic acid
D-phenylalanine methyl ester + L-alpha-aspartame
-
-
-
-
?
F-Asp-PheOMe + H2O
?
-
dipeptide synthesis
-
r
FA-glycyl-L-leucine amide + H2O
?
-
-
-
?
furylacryloyl-Gly-Leu-NH2 + H2O
furylacryloyl-Gly + Leu-NH2
-
-
-
-
?
GFA + H2O
Phe-Ala + Gly
-
-
-
?
GFSA + H2O
Gly-Phe + Phe-Ser-Ala + Gly + Ser-Ala
-
-
-
?
Gly-Phe-Leu + H2O
Phe-Leu + Gly-Phe + Gly + Leu
-
-
-
?
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
?
H-Gly-Ser-Ala-OH + H2O
?
-
-
-
?
hide powder azure + H2O
?
-
-
-
-
?
leucine enkephalin + H2O
?
Mca-Arg-Pro-Pro-Gly-Phe-Ser-Ala-Phe-Lys(Dnp)-OH + H2O
?
-
-
-
-
?
N'-[3-(2-furyl)acryloyl]glycyl-L-leucinamide + 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-(2-ethylphenyl)-2-hydroxy-3-nitrobenzamide + H2O
?
-
-
-
-
?
N-(3-[2-furyl]acryloyl)-Gly-Leu amide + H2O
?
-
-
-
?
N-(4-methoxyphenylazoformyl)-Leu-Leu-OH + 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-Gly-L-Leu-NH2 + 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-aspartic acid + L-phenylalanine methyl ester
-
-
-
-
r
N-carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester + H2O
?
-
-
-
?
N-carbobenzyloxy-L-Asp-L-Phe methyl ester + H2O
?
-
-
-
-
?
N-carboxybenzoyl-L-aspartyl-L-phenylalanine methyl ester + H2O
?
-
-
-
?
N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide + H2O
?
N-[3-(2-furyl)acryloyl]-Gly-L-Leu-NH2 + H2O
?
N-[3-(2-furyl)acryloyl]-Gly-Phe-NH2 + H2O
?
-
-
-
?
N-[3-(2-furyl)acryloyl]-glycyl-L-leucine amide + 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
-
-
?
N-[3-(2-furyl)acryloyl]-Phe-Ala amide + H2O
?
-
-
-
?
N-[3-(2-furyl)acryloyl]glycyl-L-leucinamide + H2O
?
-
-
-
-
?
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
-
-
?
oxyquinoline + H2O
?
-
-
-
-
?
Phe-Leu-Ala-NH(CH2)2NH-dansyl + H2O
?
-
-
-
-
?
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
-
-
?
soy protein isolate + H2O
?
-
-
-
-
?
tryptic hydrolysate of bovine beta casein + H2O
?
-
-
-
-
?
Tyr-Gly-Gly-Phe-Leu + H2O
?
-
-
?
Z-Arg-PheOMe + H2O
?
-
dipeptide synthesis
-
?
[3H]leucine enkephalin + H2O
?
[3H]Tyr-Gly-Gly-Phe-Leu + H2O
?
-
-
-
?
additional information
?
-
(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
?
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Asp + Phe-methylester
benzyloxycarbonyl-Asp-Phe methyl ester + H2O
-
-
-
?
benzyloxycarbonyl-Asp + Phe-methylester
benzyloxycarbonyl-Asp-Phe methyl ester + H2O
-
-
-
?
Bovine serum albumin + H2O
?
-
-
-
?
Bovine serum albumin + H2O
?
-
-
-
?
casein + H2O
?
-
-
-
-
?
casein + H2O
?
from bovine milk
-
-
?
casein + H2O
L-tyrosine + ?
from bovine milk
-
-
?
casein + H2O
L-tyrosine + ?
-
-
-
?
Collagen + H2O
?
-
from bovine achilles tendon
-
-
?
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
-
-
?
Collagen + H2O
?
-
from bovine achilles tendon
-
-
?
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
-
-
?
Elastin + H2O
?
-
from bovine neck ligament
-
-
?
Elastin + H2O
?
-
from bovine neck ligament
-
-
?
Gelatin + H2O
?
-
-
-
?
GFS + H2O
Gly + Phe-Ser
-
-
-
?
GFS + H2O
Gly + Phe-Ser
-
-
-
?
GFS + H2O
Gly + Phe-Ser
-
-
-
?
GFSA + H2O
?
-
-
-
?
GFSAK + H2O
?
-
-
-
?
GFSAKN + H2O
?
-
-
-
?
GFSAKNQS + H2O
?
-
-
-
?
H-Gly-Phe-Ala-OH + H2O
?
-
-
-
?
H-Gly-Phe-Ala-OH + H2O
?
-
-
-
?
H-Gly-Phe-Leu-OH + H2O
?
-
-
-
?
H-Gly-Phe-Leu-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-Asn-Gln-Arg-OH + H2O
?
-
-
-
?
H-Gly-Phe-Ser-Ala-Lys-Asn-Gln-Ser-OH + H2O
?
-
-
-
?
H-Gly-Phe-Ser-Ala-Lys-Asn-Gln-Ser-OH + H2O
?
-
-
-
?
H-Gly-Phe-Ser-OH + H2O
?
-
-
-
?
H-Gly-Phe-Ser-OH + H2O
?
-
-
-
?
Hemoglobin + H2O
?
-
-
-
?
Hemoglobin + H2O
?
-
-
-
?
leucine enkephalin + H2O
?
-
-
-
-
?
leucine enkephalin + H2O
?
-
-
-
?
leucine enkephalin + 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 + 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]-Gly-L-Leu amide + H2O
?
-
-
-
?
N-[3-(2-furyl)acryloyl]-Gly-L-Leu-NH2 + H2O
?
-
-
-
?
N-[3-(2-furyl)acryloyl]-Gly-L-Leu-NH2 + 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
-
-
-
-
?
[3H]leucine enkephalin + H2O
?
-
-
-
?
[3H]leucine enkephalin + H2O
?
-
-
-
?
additional information
?
-
-
specificity overview: various synthetic peptides
-
-
?
additional information
?
-
-
specificity overview: oligopeptides
-
-
?
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
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
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
-
-
?
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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
Ca2+
-
thermolysin has four calcium ions responsible for its thermostability
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+
required for stability
Ca2+
-
4 calcium ions required for structural stability
Ca2+
-
contains 4 structural calcium ions
Ca2+
-
four Ca2+ per enzyme molecule are required for enzyme stability
Ca2+
-
four ions per enzyme molecule required for stability
Ca2+
-
four Ca2+ ions are required for thermostability
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+
stablizes the enzyme
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
Ca2+
activates 36% at 1 mM, 48% at 5 mM
Co2+
-
2fold activation at 0.4 mM
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
-
required
NaCl
-
4 M enhances activity 13-15 times
NaCl
-
activity is remarkably enhanced by 1-5 M neutral salts
NaCl
-
induces activation
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
-
zinc metalloproteinase
Zinc
-
the three zinc ligands are two histidines and glutamic acid
Zn2+
-
contains Zn2+
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+
required for activity
Zn2+
-
active zinc ion in thermolysin
Zn2+
-
required for enzyme activity
Zn2+
-
zinc endopeptidase
Zn2+
-
zinc-containing neutral metalloendoprotease
Zn2+
-
zinc-metallopeptidase
Zn2+
-
a zinc metalloprotease
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+
a Zn2+ metalloprotease
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+
-
a zinc metalloprotease
Zn2+
-
a zinc metalloproteinase
Zn2+
zinc metalloprotease, no efect on activity by exogenous Zn2+ at 1 mM, inhibitory at 5 mM
additional information
-
mechanism of salt-induced activation
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
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(E)-N-(naphthalen-1-yl)-N'-(4-oxo-2-phenylquinazolin-3(4H)-yl)acetimidamide
-
low inhibitory activity
1-beta-D-arabinofuranosyl-N4-lauroylcytosine
-
competitive
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-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-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
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
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-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 hydroxamic acids
-
-
-
Peptides containing zinc coordination ligands
-
-
-
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
-
-
1,10-phenanthroline
85% inhibition at 1 mM, 93% at 5 mM
1,10-phenanthroline
-
5 mM, complete inhibition
1-butanol
-
-
1-propanol
-
-
2-butanol
-
-
2-methyl-1-propanol
-
-
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+
-
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
-
overview, temperature dependence, pH-dependence
dipeptides
-
crystallographic study of the binding to thermolysin
EDTA
-
-
EDTA
77% inhibition at 1 mM, 86% at 5 mM
EDTA
-
5 mM, complete inhibition
Gly-D-Phe
-
-
N-chloroacetyl-N-hydroxyleucine methyl ester
-
irreversible inhibition
N-chloroacetyl-N-hydroxyleucine methyl ester
-
irreversible inhibition
N-chloroacetyl-N-hydroxyleucyl-alanyl-glycinamide
-
irreversible inhibition
N-chloroacetyl-N-hydroxyleucyl-alanyl-glycinamide
-
irreversible inhibition
N-Phosphoryl-L-Leu amide
-
thermolysin-inhibitor complexes examined by NMR spectroscopy
N-Phosphoryl-L-Leu amide
-
-
Phosphonamidates
-
-
-
Phosphonamidates
-
overview
-
phosphoramidon
-
-
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
phosphoramidon
-
strong competitive inhibitor
thiorphan
-
-
Zn2+
-
-
Zn2+
zinc metalloprotease, no effect on activity by exogenous Zn2+ at 1 mM, inhibitory by 69% at 5 mM
additional information
-
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
no inhibition by PMSF
-
additional information
-
not inhibitory: human blood serpins alpha-1-antitrypsin and alpha-1-antichymotrypsin
-
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Acute Kidney Injury
Asymmetric dimethylarginine (ADMA) in human blood: effects of extended haemodialysis in the critically ill patient with acute kidney injury, protein binding to human serum albumin and proteolysis by thermolysin.
Bacterial Infections
Dipeptide inhibitors of thermolysin and angiotensin I-converting enzyme.
Blister
An ultrastructural comparison of dermo-epidermal separation techniques.
Bluetongue
Effects of proteolytic enzymes on the infectivity, haemagglutinating activity and protein composition of bluetongue virus type 20.
Brain Diseases
Molecular profiling of ovine prion diseases by using thermolysin-resistant PrPSc and endogenous C2 PrP fragments.
Brain Diseases
Use of thermolysin in the diagnosis of prion diseases.
Corneal Dystrophies, Hereditary
Mutation in transforming growth factor beta induced protein associated with granular corneal dystrophy type 1 reduces the proteolytic susceptibility through local structural stabilization.
Encephalitis, Tick-Borne
Protease treatment and chemical crosslinking of a flavivirus: tick borne encephalitis virus.
Encephalomyelitis, Autoimmune, Experimental
Treatment of an encephalitogenic peptide from guinea pig myelin basic protein with alpha-protease and thermolysin. Isolation of fragments and determination of cleavage sites.
Encephalopathy, Bovine Spongiform
Detection and characterization of proteinase K-sensitive disease-related prion protein with thermolysin.
Encephalopathy, Bovine Spongiform
Molecular profiling of ovine prion diseases by using thermolysin-resistant PrPSc and endogenous C2 PrP fragments.
Encephalopathy, Bovine Spongiform
Use of thermolysin in the diagnosis of prion diseases.
Hypertension
Blood Pressure Lowering Effect of a Pea Protein Hydrolysate in Hypertensive Rats and Humans.
Hypophosphatemia
Analysis of recombinant Phex: an endopeptidase in search of a substrate.
Infections
Leptospira interrogans thermolysin refolded at high pressure and alkaline pH displays proteolytic activity against complement C3.
Infections
Transient infection of freshly isolated human colorectal tumor cells by reovirus T3D intermediate subviral particles.
Influenza, Human
The sensitivity of the results of molecular docking to induced fit effects: application to thrombin, thermolysin and neuraminidase.
Influenza, Human
Thermolysin activation mutants with changes in the fusogenic region of an influenza virus hemagglutinin.
Influenza, Human
Trypsin-resistant protease activation mutants of an influenza virus.
Insulin Resistance
Enzymatic digest of whey protein and wheylin-1, a dipeptide released in the digest, increase insulin sensitivity in an Akt phosphorylation-dependent manner.
Leptospirosis
Leptospira interrogans thermolysin refolded at high pressure and alkaline pH displays proteolytic activity against complement C3.
Leukemia
Human T-cell leukemia-associated cell surface glycoprotein GP37: studies with three monoclonal antibodies and a rabbit antiserum.
Neoplasms
Anti-inflammatory effects of dulse (Palmaria palmata) resulting from the simultaneous water-extraction of phycobiliproteins and chlorophyll a.
Neoplasms
Comparison of colon-, lung-, and breast-derived carcinoembryonic antigen and cross-reacting antigens by monoclonal antibodies and fingerprint analysis.
Neoplasms
Synthesis and HPLC analysis of enzymatically cleavable linker consisting of poly(ethylene glycol) and dipeptide for the development of immunoconjugate.
Neoplasms
Synthesis of a novel duocarmycin derivative DU-257 and its application to immunoconjugate using poly(ethylene glycol)-dipeptidyl linker capable of tumor specific activation.
Neoplasms
Transient infection of freshly isolated human colorectal tumor cells by reovirus T3D intermediate subviral particles.
Neuroblastoma
Modulation of matrix adhesive responses of human neuroblastoma cells by neighboring sequences in the fibronectins.
Prion Diseases
Detection and characterization of proteinase K-sensitive disease-related prion protein with thermolysin.
Prion Diseases
Use of thermolysin in the diagnosis of prion diseases.
Sarcoma, Avian
Analysis of the catalytic domain of phosphotransferase activity of two avian sarcoma virus-transforming proteins.
Scrapie
Molecular profiling of ovine prion diseases by using thermolysin-resistant PrPSc and endogenous C2 PrP fragments.
Scrapie
Strain-specific proteolytic processing of the prion protein in prion diseases of ruminants transmitted in ovine transgenic mice.
Scrapie
Use of thermolysin in the diagnosis of prion diseases.
Tetanus
Families of zinc metalloproteases.
Tetanus
The active site structure of tetanus neurotoxin resolved by multiple scattering analysis in X-Ray absorption spectroscopy.
Tetanus
X-ray absorption spectroscopy study of zinc coordination in tetanus neurotoxin, astacin, alkaline protease and thermolysin.
Vesicular Stomatitis
Association of vesicular stomatitis virus glycoprotein with virion membrane: characterization of the lipophilic tail fragment.
Warts
Differential effect of halide anions on the hydrolysis of different dansyl substrates by thermolysin.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
0.0533
5,6-carboxyfluorescein-PAGLAC(Alexa Fluor 647)-NH2
-
pH 7.4, 30°C
-
0.0024
5,6-carboxyfluorescein-PAGLAC(Cy5)-NH2
-
pH 7.4, 30°C
0.0776
5,6-carboxyfluorescein-PSVAGLAGGC(Alexa Fluor 647)-NH2
-
pH 7.4, 30°C
-
0.0176
5,6-carboxyfluorescein-PSVAGLAGGC(Cy5)-NH2
-
pH 7.4, 30°C
0.0116
5,6-carboxyfluorescein-PVAGLAGC(Cy5)-NH2
-
pH 7.4, 30°C
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
-
-
0.91
dansyl-Ala-Phe-Ala
-
-
13
dansyl-Gly-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
-
-
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, 37°C
0.00191
N,N'-diBoc-dityrosyl-(Phe-isoniazid)2
-
pH 7.5, 37°C
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 25°C
0.62
Phe-Leu-Ala-NH(CH2)2NH-dansyl
-
-
0.2
[3H]Tyr-Gly-Gly-Phe-Leu
pH 8.0, 37°C
additional information
additional information
-
0.033
Benzyloxycarbonyl-Asp-Phe methyl ester
-
pH 5.5
0.059
Benzyloxycarbonyl-Asp-Phe methyl ester
-
pH 6.0
0.076
Benzyloxycarbonyl-Asp-Phe methyl ester
-
pH 5.0
0.3
GFA
-
pH 8.0, 37°C
0.6
GFA
-
pH 8.0, 37°C, 5 M glycerol
0.4
GFL
-
pH 8.0, 37°C, product FL
0.7
GFL
-
pH 8.0, 37°C, 5 M glycerol, product GL
1.8
GFL
-
pH 8.0, 37°C, 5 M glycerol, product FL
2.5
GFL
-
pH 8.0, 37°C, 5 M glycerol, product GF
1.3
GFS
-
pH 8.0, 37°C
3.5
GFS
-
pH 8.0, 37°C, 5 M glycerol
0.7
GFSA
-
pH 8.0, 37°C, product FSA
1.2
GFSA
-
pH 8.0, 37°C, 5 M glycerol, product GF
6.8
GFSA
-
pH 8.0, 37°C, 5 M glycerol, product FSA
12
GFSA
-
pH 8.0, 37°C, 5 M glycerol, product GF
250
L-Phe methyl ester
-
pH 5.5 or 6.0
300
L-Phe methyl ester
-
-
5.8
L-phenylalanine methyl ester
-
mutant enzyme D150E, at pH 7.5, at 25°C
7
L-phenylalanine methyl ester
-
mutant enzyme D150W, at pH 7.5, at 25°C
7.3
L-phenylalanine methyl ester
-
mutant enzyme D150A, at pH 7.5, at 25°C
8.7
L-phenylalanine methyl ester
-
wild type enzyme, at pH 7.5, at 25°C
8.8
L-phenylalanine methyl ester
-
mutant enzyme N227H, at pH 7.5, at 25°C
11.3
L-phenylalanine methyl ester
-
mutant enzyme F114A, at pH 7.5, at 25°C
12.9
L-phenylalanine methyl ester
-
mutant enzyme I168A, at pH 7.5, at 25°C
0.2
leucine enkephalin
-
pH 6.8, 37°C, wild-type
0.21
leucine enkephalin
-
pH 7.4, 37°C, wild-type
0.24
leucine enkephalin
-
pH 6.8, 37°C, mutant D170A
0.24
leucine enkephalin
-
pH 6.8, 37°C, mutant R203M
0.48
leucine enkephalin
-
pH 7.4, 37°C, mutant Y157F
1.985
leucine enkephalin
-
pH 7.4, 37°C, mutant D226A
20
N-(benzyloxycarbonyl)-L-Phe
-
-
39.2
N-(benzyloxycarbonyl)-L-Phe
-
-
12
N-benzyloxycarbonyl-Gly-L-Leu amide
-
recombinant mutant L155S/I156N, pH 7.0, 37°C
12
N-benzyloxycarbonyl-Gly-L-Leu amide
-
recombinant mutant L155S/I156V, pH 7.0, 37°C
13
N-benzyloxycarbonyl-Gly-L-Leu amide
-
recombinant mutant L155A/I156N, pH 7.0, 37°C
13
N-benzyloxycarbonyl-Gly-L-Leu amide
-
recombinant mutant L155A/I156V, pH 7.0, 37°C
13
N-benzyloxycarbonyl-Gly-L-Leu amide
-
recombinant mutant L155S, pH 7.0, 37°C
14
N-benzyloxycarbonyl-Gly-L-Leu amide
-
recombinant wild-type enzyme, pH 7.0, 37°C
20
N-benzyloxycarbonyl-Gly-L-Leu amide
-
recombinant mutant L155A, pH 7.0, 37°C
0.42
N-benzyloxycarbonyl-L-Asp-L-Phe-methyl ester
-
recombinant wild-type enzyme, pH 7.5, 25°C
0.44
N-benzyloxycarbonyl-L-Asp-L-Phe-methyl ester
-
recombinant mutant G117E, pH 7.5, 25°C
0.5
N-benzyloxycarbonyl-L-Asp-L-Phe-methyl ester
-
recombinant mutant G117R, pH 7.5, 25°C
0.57
N-benzyloxycarbonyl-L-Asp-L-Phe-methyl ester
-
recombinant mutant G117K, pH 7.5, 25°C
10
N-carbobenzoxy-Gly-L-Leu-NH2
-
mutant L155G, 37°C, pH 7.0
13
N-carbobenzoxy-Gly-L-Leu-NH2
-
mutant L155S, 37°C, pH 7.0
14
N-carbobenzoxy-Gly-L-Leu-NH2
-
wild-type, 37°C, pH 7.0
17
N-carbobenzoxy-Gly-L-Leu-NH2
-
mutant L155F, 37°C, pH 7.0
20
N-carbobenzoxy-Gly-L-Leu-NH2
-
mutant L155A, 37°C, pH 7.0
0.06
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
pH 7.0, 25°C, recombinant mutant L144S
0.1
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
pH 7.0, 25°C, recombinant mutant G8C/N60C/S65P/L144S
0.16
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
mutant enzyme L144S/D150E/S53D, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
0.17
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
mutant enzyme L144S/D150E, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
0.18
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
pH 7.0, 25°C, recombinant mutant G8C/N60C/S65P
0.18
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
mutant enzyme D150E/I168A, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
0.19
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
mutant enzyme L144S, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
0.24
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
pH 7.5, 25°C, recombinant mutant Q225V
0.28
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
pH 7.5, 25°C, recombinant mutant Q128A
0.29
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
pH 7.5, 25°C, recombinant mutant Q225A
0.3
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
pH 7.5, 25°C, recombinant mutants Q128K and Q225R
0.33
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
pH 7.0, 25°C, recombinant wild-type enzyme
0.33
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
pH 7.5, 25°C, recombinant mutant Q128E
0.34
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
pH 7.5, 25°C, recombinant mutant Q225D
0.39
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
pH 7.5, 25°C, recombinant mutant Q225K
0.4
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
pH 7.5, 25°C, recombinant enzyme
0.4
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
pH 7.5, 25°C, recombinant wild-type enzyme
0.45
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
pH 7.5, 25°C, recombinant wild-type enzyme
0.46
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
mutant enzyme I168A, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
0.5
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
mutant enzyme D150E, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
0.52
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
pH 7.5, 25°C, native enzyme
0.52
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
pH 7.5, 25°C, native wild-type enzyme
0.54
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
mutant enzyme G8C/N60C/S65P, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
0.55
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
mutant enzyme S53D/L155A/G8C/N60C/S65P, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
0.63
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
pH 7.5, 25°C, recombinant mutant Q225E
0.63
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
wild type enzyme, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
0.69
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
mutant enzyme S53D/L155A, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
0.83
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
mutant enzyme L155A/G8C/N60C/S65P, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
0.94
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
mutant enzyme S53D/G8C/N60C/S65P, in the absence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
1.29
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
mutant enzyme L155A, in the absence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
0.7
N-carbobenzoxy-L-Asp-L-Phe-methyl ester
-
mutant enzyme D150E, at pH 7.5, at 25°C
0.8
N-carbobenzoxy-L-Asp-L-Phe-methyl ester
-
mutant enzyme I168A, at pH 7.5, at 25°C
1
N-carbobenzoxy-L-Asp-L-Phe-methyl ester
-
mutant enzyme F114A, at pH 7.5, at 25°C
1
N-carbobenzoxy-L-Asp-L-Phe-methyl ester
-
wild type enzyme, at pH 7.5, at 25°C
1.3
N-carbobenzoxy-L-Asp-L-Phe-methyl ester
-
mutant enzyme N227H, at pH 7.5, at 25°C
2.1
N-carbobenzoxy-L-Asp-L-Phe-methyl ester
-
mutant enzyme D150A, at pH 7.5, at 25°C
2.1
N-carbobenzoxy-L-Asp-L-Phe-methyl ester
-
mutant enzyme D150W, at pH 7.5, at 25°C
49
N-carbobenzoxy-L-aspartic acid
-
mutant enzyme F114A, at pH 7.5, at 25°C
54
N-carbobenzoxy-L-aspartic acid
-
mutant enzyme D150W, at pH 7.5, at 25°C
57
N-carbobenzoxy-L-aspartic acid
-
mutant enzyme D150A, at pH 7.5, at 25°C
60
N-carbobenzoxy-L-aspartic acid
-
mutant enzyme D150E, at pH 7.5, at 25°C
62
N-carbobenzoxy-L-aspartic acid
-
wild type enzyme, at pH 7.5, at 25°C
70
N-carbobenzoxy-L-aspartic acid
-
mutant enzyme N227H, at pH 7.5, at 25°C
105
N-carbobenzoxy-L-aspartic acid
-
mutant enzyme I168A, at pH 7.5, at 25°C
0.38
N-carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester
purified recombinant mutant N116Q, pH 7.5, 25°C
0.39
N-carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester
purified recombinant wild-type enzyme, pH 7.5, 25°C
0.41
N-carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester
purified recombinant mutant N116A, pH 7.5, 25°C
0.48
N-carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester
purified recombinant mutant N116D, pH 7.5, 25°C
0.49
N-carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester
purified recombinant mutant N116T, pH 7.5, 25°C
additional information
additional information
-
-
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
overview: Km of synthetic oligopeptides
-
additional information
additional information
-
effect of various n-pentanal concentrations of Km
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
thermodynamics of wild-type and mutant enzymes
-
additional information
additional information
-
Michaelis-Menten kinetics, overview
-
additional information
additional information
-
Michaelis-Menten kinetics, overview
-
additional information
additional information
steady-state kinetics, overview
-
additional information
additional information
-
kinetics and thermodynamics of wild-type and mutant enzymes in absence or presence of salt, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
pH and temperature not specified in the publication
2.6
(europium(III) complex of a modified terpyridine)-K1K2K2GFSAK2K-black hole quencher 2
-
pH and temperature not specified in the publication
-
0.7
5,6-carboxyfluorescein-PAGLAC(Alexa Fluor 647)-NH2
-
pH 7.4, 30°C
-
0.37
5,6-carboxyfluorescein-PAGLAC(Cy5)-NH2
-
pH 7.4, 30°C
5.7
5,6-carboxyfluorescein-PSVAGLAGGC(Alexa Fluor 647)-NH2
-
pH 7.4, 30°C
-
7.82
5,6-carboxyfluorescein-PSVAGLAGGC(Cy5)-NH2
-
pH 7.4, 30°C
2.96
5,6-carboxyfluorescein-PVAGLAGC(Cy5)-NH2
-
pH 7.4, 30°C
861 - 951
Benzyloxycarbonyl-(4-nitro)Phe-Leu-Ala
-
depending on mode of preparation of the form of enzyme
407 - 968
Benzyloxycarbonyl-Gly-Phe-Leu-Ala
-
depending on mode of preparation of the form of enzyme
362 - 605
Benzyloxycarbonyl-Phe-Leu-Ala
-
depending on mode of preparation of the form of enzyme
1.4 - 1.7
Dansyl-Gly-Phe-Ala
-
depending on assay method
0.3 - 4.9
L-phenylalanine methyl ester
0.083 - 1560
leucine enkephalin
0.238
N,N'-diBoc-dityrosyl-(Ile-isoniazid)2
-
pH 7.5, 37°C
0.0463
N,N'-diBoc-dityrosyl-(Phe-isoniazid)2
-
pH 7.5, 37°C
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
-
mutant enzyme S53D, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
additional information
additional information
-
0.06
GFA
-
pH 8.0, 37°C
0.076
GFA
-
pH 8.0, 37°C, 5 M glycerol
0.006
GFL
-
pH 8.0, 37°C, 5 M glycerol, product GF
0.013
GFL
-
pH 8.0, 37°C, product GF
0.026
GFL
-
pH 8.0, 37°C, 5 M glycerol, product FL
0.045
GFL
-
pH 8.0, 37°C, product FL
0.035
GFS
-
pH 8.0, 37°C
0.05
GFS
-
pH 8.0, 37°C, 5 M glycerol
0.07
GFSA
-
pH 8.0, 37°C, product FSA
0.173
GFSA
-
pH 8.0, 37°C, 5 M glycerol, product FSA
0.3
GFSA
-
pH 8.0, 37°C, product GF
0.591
GFSA
-
pH 8.0, 37°C, 5 M glycerol, product GF
6.08
GFSA
-
pH 8.0, 37°C, 5 M glycerol, product GF
0.3
L-phenylalanine methyl ester
-
mutant enzyme F114A, at pH 7.5, at 25°C
1.3
L-phenylalanine methyl ester
-
wild type enzyme, at pH 7.5, at 25°C
2.1
L-phenylalanine methyl ester
-
mutant enzyme D150A, at pH 7.5, at 25°C
2.3
L-phenylalanine methyl ester
-
mutant enzyme N227H, at pH 7.5, at 25°C
2.5
L-phenylalanine methyl ester
-
mutant enzyme D150E, at pH 7.5, at 25°C
3.2
L-phenylalanine methyl ester
-
mutant enzyme D150W, at pH 7.5, at 25°C
4.9
L-phenylalanine methyl ester
-
mutant enzyme I168A, at pH 7.5, at 25°C
0.083
leucine enkephalin
-
pH 6.8, 37°C, mutant R203M
2.94
leucine enkephalin
-
pH 6.8, 37°C, mutant D170A
2.94
leucine enkephalin
-
pH 7.4, 37°C, mutant Y157F
155.5
leucine enkephalin
-
pH 7.4, 37°C, wild-type
156
leucine enkephalin
-
pH 7.4, 37°C, wild-type
1555
leucine enkephalin
-
pH 6.8, 37°C, wild-type
1560
leucine enkephalin
-
pH 6.8, 37°C, wild-type
0.556
N-(benzyloxycarbonyl)-L-Phe
-
-
1.69
N-(benzyloxycarbonyl)-L-Phe
-
-
13.58
N-benzyloxycarbonyl-Gly-L-Leu amide
-
recombinant mutant L155A/I156V, pH 7.0, 37°C
26.67
N-benzyloxycarbonyl-Gly-L-Leu amide
-
recombinant mutant L155A/I156N, pH 7.0, 37°C
48.33
N-benzyloxycarbonyl-Gly-L-Leu amide
-
recombinant mutant L155S/I156N, pH 7.0, 37°C
51.67
N-benzyloxycarbonyl-Gly-L-Leu amide
-
recombinant wild-type enzyme, pH 7.0, 37°C
80
N-benzyloxycarbonyl-Gly-L-Leu amide
-
recombinant mutant L155A, pH 7.0, 37°C
105
N-benzyloxycarbonyl-Gly-L-Leu amide
-
recombinant mutant L155S/I156V, pH 7.0, 37°C
165
N-benzyloxycarbonyl-Gly-L-Leu amide
-
recombinant mutant L155S, pH 7.0, 37°C
4.8
N-benzyloxycarbonyl-L-Asp-L-Phe-methyl ester
-
recombinant mutant G117R, pH 7.5, 25°C
7.9
N-benzyloxycarbonyl-L-Asp-L-Phe-methyl ester
-
recombinant wild-type enzyme, pH 7.5, 25°C
8.4
N-benzyloxycarbonyl-L-Asp-L-Phe-methyl ester
-
recombinant mutant G117K, pH 7.5, 25°C
10.5
N-benzyloxycarbonyl-L-Asp-L-Phe-methyl ester
-
recombinant mutant G117E, pH 7.5, 25°C
23.3
N-carbobenzoxy-Gly-L-Leu-NH2
-
mutant L155F, 37°C, pH 7.0
51.6
N-carbobenzoxy-Gly-L-Leu-NH2
-
wild-type, 37°C, pH 7.0
80
N-carbobenzoxy-Gly-L-Leu-NH2
-
mutant L155A, 37°C, pH 7.0
150
N-carbobenzoxy-Gly-L-Leu-NH2
-
mutant L155G, 37°C, pH 7.0
165
N-carbobenzoxy-Gly-L-Leu-NH2
-
mutant L155S, 37°C, pH 7.0
1.3
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
pH 7.5, 25°C, recombinant mutant Q225A
1.6
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
pH 7.5, 25°C, recombinant mutant Q225V
3.3
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
pH 7.0, 25°C, recombinant mutant G8C/N60C/S65P
3.3
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
pH 7.5, 25°C, recombinant mutant Q225D
3.3
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
mutant enzyme S53D/L155A/G8C/N60C/S65P, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
3.4
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
pH 7.0, 25°C, recombinant wild-type enzyme
3.6
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
pH 7.5, 25°C, recombinant mutant Q225R
3.7
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
pH 7.5, 25°C, recombinant mutant Q128K
3.8
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
pH 7.5, 25°C, recombinant enzyme
3.8
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
pH 7.5, 25°C, recombinant wild-type enzyme
3.8
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
pH 7.5, 25°C, recombinant mutant Q128A
4.3
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
pH 7.5, 25°C, native enzyme
4.3
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
pH 7.5, 25°C, native wild-type enzyme
4.3
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
pH 7.5, 25°C, recombinant mutants Q128E and Q225E
4.7
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
pH 7.5, 25°C, recombinant wild-type enzyme and mutant Q225K
5.4
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
mutant enzyme G8C/N60C/S65P, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
5.9
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
wild type enzyme, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
6.3
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
mutant enzyme L155A/G8C/N60C/S65P, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
6.4
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
mutant enzyme S53D/L155A, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
6.7
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
pH 7.0, 25°C, recombinant mutant L144S
7
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
pH 7.0, 25°C, recombinant mutant G8C/N60C/S65P/L144S
7.4
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
mutant enzyme S53D/G8C/N60C/S65P, in the absence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
7.7
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
mutant enzyme I168A, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
8.7
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
mutant enzyme L155A, in the absence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
9.4
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
mutant enzyme L144S, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
15.5
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
mutant enzyme D150E/I168A, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
15.6
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
mutant enzyme L144S/D150E/S53D, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
16.5
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
mutant enzyme D150E, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
17
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
mutant enzyme L144S/D150E, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
1.5
N-carbobenzoxy-L-Asp-L-Phe-methyl ester
-
mutant enzyme F114A, at pH 7.5, at 25°C
9.5
N-carbobenzoxy-L-Asp-L-Phe-methyl ester
-
wild type enzyme, at pH 7.5, at 25°C
12.3
N-carbobenzoxy-L-Asp-L-Phe-methyl ester
-
mutant enzyme I168A, at pH 7.5, at 25°C
17.1
N-carbobenzoxy-L-Asp-L-Phe-methyl ester
-
mutant enzyme N227H, at pH 7.5, at 25°C
20.5
N-carbobenzoxy-L-Asp-L-Phe-methyl ester
-
mutant enzyme D150E, at pH 7.5, at 25°C
24.4
N-carbobenzoxy-L-Asp-L-Phe-methyl ester
-
mutant enzyme D150A, at pH 7.5, at 25°C
49.4
N-carbobenzoxy-L-Asp-L-Phe-methyl ester
-
mutant enzyme D150W, at pH 7.5, at 25°C
0.3
N-carbobenzoxy-L-aspartic acid
-
mutant enzyme F114A, at pH 7.5, at 25°C
1.3
N-carbobenzoxy-L-aspartic acid
-
wild type enzyme, at pH 7.5, at 25°C
2.1
N-carbobenzoxy-L-aspartic acid
-
mutant enzyme D150A, at pH 7.5, at 25°C
2.3
N-carbobenzoxy-L-aspartic acid
-
mutant enzyme N227H, at pH 7.5, at 25°C
2.5
N-carbobenzoxy-L-aspartic acid
-
mutant enzyme D150E, at pH 7.5, at 25°C
3.2
N-carbobenzoxy-L-aspartic acid
-
mutant enzyme D150W, at pH 7.5, at 25°C
4.9
N-carbobenzoxy-L-aspartic acid
-
mutant enzyme I168A, at pH 7.5, at 25°C
5.4
N-carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester
purified recombinant mutant N116T, pH 7.5, 25°C
6.7
N-carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester
purified recombinant mutant N116A, pH 7.5, 25°C
7.1
N-carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester
purified recombinant mutant N116Q, pH 7.5, 25°C
7.7
N-carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester
purified recombinant wild-type enzyme, pH 7.5, 25°C
12
N-carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester
purified recombinant mutant N116D, pH 7.5, 25°C
additional information
additional information
-
effect of various n-pentanal concentrations of turnover number
-
additional information
additional information
-
overview: turnover number of synthetic oligopeptides
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
13.1
5,6-carboxyfluorescein-PAGLAC(Alexa Fluor 647)-NH2
-
pH 7.4, 30°C
-
154.2
5,6-carboxyfluorescein-PAGLAC(Cy5)-NH2
-
pH 7.4, 30°C
73.5
5,6-carboxyfluorescein-PSVAGLAGGC(Alexa Fluor 647)-NH2
-
pH 7.4, 30°C
-
444.3
5,6-carboxyfluorescein-PSVAGLAGGC(Cy5)-NH2
-
pH 7.4, 30°C
255.2
5,6-carboxyfluorescein-PVAGLAGC(Cy5)-NH2
-
pH 7.4, 30°C
60.3
N,N'-diBoc-dityrosyl-(Ile-isoniazid)2
-
pH 7.5, 37°C
24.3
N,N'-diBoc-dityrosyl-(Phe-isoniazid)2
-
pH 7.5, 37°C
1.03 - 12.67
N-benzyloxycarbonyl-Gly-L-Leu amide
9.6 - 23.9
N-benzyloxycarbonyl-L-Asp-L-Phe-methyl ester
6 - 99
N-carbobenzoxy-L-Asp-L-Phe methyl ester
1.5 - 27.6
N-carbobenzoxy-L-Asp-L-Phe-methyl ester
11 - 27
N-carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester
0.23 - 11.7
N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
15 - 117
N-[3-(2-furyl)acryloyl]-glycyl-L-leucine amide
1.03
N-benzyloxycarbonyl-Gly-L-Leu amide
-
recombinant mutant L155A/I156V, pH 7.0, 37°C
2
N-benzyloxycarbonyl-Gly-L-Leu amide
-
recombinant mutant L155A/I156N, pH 7.0, 37°C
3.67
N-benzyloxycarbonyl-Gly-L-Leu amide
-
recombinant wild-type enzyme, pH 7.0, 37°C
4
N-benzyloxycarbonyl-Gly-L-Leu amide
-
recombinant mutant L155A, pH 7.0, 37°C
4
N-benzyloxycarbonyl-Gly-L-Leu amide
-
recombinant mutant L155S/I156N, pH 7.0, 37°C
12
N-benzyloxycarbonyl-Gly-L-Leu amide
-
recombinant mutant L155S/I156V, pH 7.0, 37°C
12.67
N-benzyloxycarbonyl-Gly-L-Leu amide
-
recombinant mutant L155S, pH 7.0, 37°C
9.6
N-benzyloxycarbonyl-L-Asp-L-Phe-methyl ester
-
recombinant mutant G117R, pH 7.5, 25°C
14.7
N-benzyloxycarbonyl-L-Asp-L-Phe-methyl ester
-
recombinant mutant G117K, pH 7.5, 25°C
18.8
N-benzyloxycarbonyl-L-Asp-L-Phe-methyl ester
-
recombinant wild-type enzyme, pH 7.5, 25°C
23.9
N-benzyloxycarbonyl-L-Asp-L-Phe-methyl ester
-
recombinant mutant G117E, pH 7.5, 25°C
6
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
mutant enzyme S53D/L155A/G8C/N60C/S65P, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
6.7
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
mutant enzyme L155A, in the absence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
7.5
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
mutant enzyme L155A/G8C/N60C/S65P, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
7.9
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
mutant enzyme S53D/G8C/N60C/S65P, in the absence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
9.2
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
mutant enzyme S53D/L155A, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
9.4
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
wild type enzyme, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
10
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
mutant enzyme G8C/N60C/S65P, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
16.8
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
mutant enzyme I168A, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
33.1
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
mutant enzyme D150E, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
49.7
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
mutant enzyme L144S, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
96.2
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
mutant enzyme L144S/D150E/S53D, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
99
N-carbobenzoxy-L-Asp-L-Phe methyl ester
-
mutant enzyme L144S/D150E, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
1.5
N-carbobenzoxy-L-Asp-L-Phe-methyl ester
-
mutant enzyme F114A, at pH 7.5, at 25°C
9.3
N-carbobenzoxy-L-Asp-L-Phe-methyl ester
-
wild type enzyme, at pH 7.5, at 25°C
11.7
N-carbobenzoxy-L-Asp-L-Phe-methyl ester
-
mutant enzyme D150A, at pH 7.5, at 25°C
13.7
N-carbobenzoxy-L-Asp-L-Phe-methyl ester
-
mutant enzyme N227H, at pH 7.5, at 25°C
16
N-carbobenzoxy-L-Asp-L-Phe-methyl ester
-
mutant enzyme I168A, at pH 7.5, at 25°C
23
N-carbobenzoxy-L-Asp-L-Phe-methyl ester
-
mutant enzyme D150W, at pH 7.5, at 25°C
27.6
N-carbobenzoxy-L-Asp-L-Phe-methyl ester
-
mutant enzyme D150E, at pH 7.5, at 25°C
11
N-carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester
purified recombinant mutant N116T, pH 7.5, 25°C
16
N-carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester
purified recombinant mutant N116A, pH 7.5, 25°C
19
N-carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester
purified recombinant mutant N116Q, pH 7.5, 25°C
20
N-carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester
purified recombinant wild-type enzyme, pH 7.5, 25°C
27
N-carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester
purified recombinant mutant N116D, pH 7.5, 25°C
0.23
N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
-
mutant enzyme S53D/L155A/G8C/N60C/S65P, in the absence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
0.26
N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
-
mutant enzyme L155A, in the absence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
0.29
N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
-
mutant enzyme G8C/N60C/S65P, in the absence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
0.29
N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
-
wild type enzyme, in the absence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
0.31
N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
-
mutant enzyme S53D/G8C/N60C/S65P, in the absence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
0.32
N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
-
mutant enzyme S53D, in the absence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
0.33
N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
-
mutant enzyme S53D/L155A, in the absence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
0.34
N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
-
mutant enzyme L155A/G8C/N60C/S65P, in the absence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
0.62
N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
-
mutant enzyme I168A, in the absence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
0.79
N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
-
mutant enzyme D150E, in the absence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
1.82
N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
-
mutant enzyme L144S, in the absence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
2.04
N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
-
mutant enzyme L144S/D150E, in the absence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
2.1
N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
-
mutant enzyme L155A, in the presence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
2.49
N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
-
mutant enzyme L144S/D150E/S53D, in the absence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
3
N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
-
mutant enzyme I168A, in the presence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
3.2
N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
-
mutant enzyme S53D/L155A, in the presence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
3.3
N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
-
mutant enzyme S53D/L155A/G8C/N60C/S65P, in the presence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
3.5
N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
-
mutant enzyme G8C/N60C/S65P, in the presence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
3.8
N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
-
wild type enzyme, in the presence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
3.9
N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
-
mutant enzyme S53D, in the presence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
4
N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
-
mutant enzyme D150E, in the presence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
4
N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
-
mutant enzyme S53D/G8C/N60C/S65P, in the presence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
4.3
N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
-
mutant enzyme L155A/G8C/N60C/S65P, in the presence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
6
N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
-
mutant enzyme L144S/D150E, in the presence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
6.6
N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
-
mutant enzyme L144S, in the presence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
9
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 25°C
11.7
N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
-
mutant enzyme L144S/D150E/S53D, in the presence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C
15
N-[3-(2-furyl)acryloyl]-glycyl-L-leucine amide
-
recombinant mutant G117R, pH 7.5, 25°C
16
N-[3-(2-furyl)acryloyl]-glycyl-L-leucine amide
-
recombinant mutant G117K, pH 7.5, 25°C
26
N-[3-(2-furyl)acryloyl]-glycyl-L-leucine amide
purified recombinant mutant N116T, pH 7.5, 25°C
31
N-[3-(2-furyl)acryloyl]-glycyl-L-leucine amide
purified recombinant mutant N116A, pH 7.5, 25°C
33
N-[3-(2-furyl)acryloyl]-glycyl-L-leucine amide
-
recombinant mutant G117E, pH 7.5, 25°C
37
N-[3-(2-furyl)acryloyl]-glycyl-L-leucine amide
purified recombinant mutant N116Q, pH 7.5, 25°C
37
N-[3-(2-furyl)acryloyl]-glycyl-L-leucine amide
purified recombinant wild-type enzyme, pH 7.5, 25°C
40
N-[3-(2-furyl)acryloyl]-glycyl-L-leucine amide
-
recombinant wild-type enzyme, pH 7.5, 25°C
117
N-[3-(2-furyl)acryloyl]-glycyl-L-leucine amide
purified recombinant mutant N116D, pH 7.5, 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.000000064
1-beta-D-arabinofuranosyl-N4-lauroylcytosine
-
25°C, pH 7.5
35
1-Pentanol
-
pH 7.5, 25°C
0.0593
2-(4-methylphenyl)-3-(1,3-thiazol-2-yl) quinazolin-4(3H)-one
-
at pH 7.0 and 25°C
0.57
2-(acetyloxy)-3-chlorobenzoic acid
in 100 mM Tris/HCl, pH 7.5, 2 mM CaCl2, 4% (v/v) DMSO, at 25°C
0.315
2-ethyl-3-hydroxyquinazolin-4(3H)-one
in 100 mM Tris/HCl, pH 7.5, 2 mM CaCl2, 4% (v/v) DMSO, at 25°C
0.00125
2-ethylquinazolin-4(3H)-one
-
at pH 7.0 and 25°C
2.06
2-hydroxy-N-(4-methyl-2-nitrophenyl)-3-nitrobenzamide
-
25°C, pH 7.5
41 - 380
2-methyl-1-propanol
1.6
2-phenylpropionyl-L-phenylalanine
-
pH 8.6, temperature not specified in the publication
0.000015
2-phenylpropionyl-Leu-Trp
-
pH 7.2, temperature not specified in the publication
0.000243
3-(isopropylideneamino)-2,2-dimethyl-2,3-dihydroquinazolin-4(1H)-one
-
at pH 7.0 and 25°C
0.0183
3-([(1E)-[4-(dimethylamino) phenyl]methylene]amino)-2-methylquinazolin-4(3H)-one
-
at pH 7.0 and 25°C
0.042
3-([(1E)-[4-(dimethylamino) phenyl]methylene]amino)-2-phenylquinazolin-4(3H)-one
-
at pH 7.0 and 25°C
10100
3-amino-2-(4-chlorophenyl)quinazolin-4(3H)-one
-
at pH 7.0 and 25°C
3.12
3-amino-2-(4-nitrophenyl)quinazolin-4(3H)-one
-
at pH 7.0 and 25°C
0.0379
3-amino-2-(trifluoromethyl) quinazolin-4(3H)-one
-
at pH 7.0 and 25°C
0.0549
3-amino-2-methylquinazolin-4(3H)-one
-
at pH 7.0 and 25°C
0.128
3-hydroxy-2-isopropylquinazolin-4(3H)-one
in 100 mM Tris/HCl, pH 7.5, 2 mM CaCl2, 4% (v/v) DMSO, at 25°C
0.93
3-hydroxy-2-methylquinazolin-4(3H)-one
in 100 mM Tris/HCl, pH 7.5, 2 mM CaCl2, 4% (v/v) DMSO, at 25°C
1.7
3-methylaspirin
in 100 mM Tris/HCl, pH 7.5, 2 mM CaCl2, 4% (v/v) DMSO, at 25°C
0.0000115
3-phenyl-2-(trifluoromethyl) quinazolin-4(3H)-one
-
at pH 7.0 and 25°C
4
3-[[(1E)-(3-chlorophenyl)methylene]amino]-2-phenylquinazolin-4(3H)-one
-
at pH 7.0 and 25°C
4.81
5-bromo-N-(4-bromophenyl)-2-hydroxy-3-nitro-benzamide
-
25°C, pH 7.5
1.6
beta-phenylpropionyl-L-phenylalanine
-
pH 6.8, 25°C, enzyme contains Zn2+
0.000000068
carbobenzoxy-L-phenylalanine-phosphonamidate-L-leucyl-L-alanine
pH and temperature not specified in the publication
0.0016
CGS-28,106
pH 8.0, 37°C
7.63
dimethylformamide
-
pH 7.5, 25°C
106
ethanimidic acid N-[4-oxo-2-phenyl-3(4H)-quinazolinyl]-ethyl ester
-
at pH 7.0 and 25°C
100
ethanol
-
pH 7.5, 25°C
0.25
Isopropanol
-
pH 7.5, 25°C
430
methanol
-
pH 7.5, 25°C
0.00005
N-(1-carboxy-3-phenyl-propyl)-L-leucyl-L-tryptophan
pH and temperature not specified in the publication
294
N-(2,3-dimethylphenyl)-2-hydroxy-3-nitro-benzamide
-
25°C, pH 7.5
161
N-(2,4-dimethylphenyl)-2-hydroxy-3-nitro-benzamide
-
25°C, pH 7.5
1.45
N-(2,5-dimethylphenyl)-2-hydroxy-3-nitrobenzamide
-
25°C, pH 7.5
697
N-(2-chloro-4-nitrophenyl)-2-hydroxy-3-nitro-benzamide
-
25°C, pH 7.5
0.047
N-(2-chloro-6-methylphenyl)-2-hydroxy-3-nitrobenzamide
-
25°C, pH 7.5
2.95
N-(2-ethylphenyl)-2-hydroxy-3-nitrobenzamide
-
25°C, pH 7.5
8.14
N-(5-chloro-2-methoxyphenyl)-2-hydroxy-3-nitro-benzamide
-
25°C, pH 7.5
0.008 - 0.37
N-Benzyloxycarbonyl-L-phenylalanine
0.007 - 0.21
N-benzyloxycarbonyl-L-tryptophan
0.18
n-Propanol
-
pH 7.5, 25°C
0.214
oxyquinoline
-
25°C, pH 7.5
0.000015
P-Leu-Trp
-
pH 7.2, 25°C, enzyme contains Zn2+
0.00003 - 0.0047
phosphoramidon
0.0008 - 0.16
Retrothiorphan
110
tert-amylalcohol
-
pH 7.5, 25°C
190
tert-butyl alcohol
-
pH 7.5, 25°C
0.008 - 0.37
Z-L-phenylalanine
0.007 - 0.087
Z-L-tryptophan
0.000012 - 0.00023
Zincov
0.0012
[(2S)-2-sulfanyl-3-phenylpropanoyl]Gly-(5-Ph)Pro
pH 8.0, 37°C
0.000042
[(2S)-2-sulfanyl-3-phenylpropanoyl]Phe-Tyr
pH 8.0, 37°C
0.000048
[(2S,R)-2-sulfanylheptanoyl]Phe-Ala
pH 8.0, 37°C
additional information
additional information
-
50
1-butanol
-
pH 7.5, 25°C
460
1-butanol
-
pH 7.5, 25°C
38
1-propanol
-
pH 7.5, 25°C
65
1-propanol
-
pH 7.5, 25°C
280
1-propanol
-
pH 7.5, 25°C
40
2-butanol
-
pH 7.5, 25°C
370
2-butanol
-
pH 7.5, 25°C
41
2-methyl-1-propanol
-
pH 7.5, 25°C
380
2-methyl-1-propanol
-
pH 7.5, 25°C
0.0031
HACBO-Gly
-
pH 7.4, 37°C, wild-type
0.019
HACBO-Gly
-
pH 7.4, 37°C, mutant D226A
0.031
HACBO-Gly
-
pH 7.4, 37°C, mutant Y157F
0.008
N-Benzyloxycarbonyl-L-phenylalanine
-
pH 5.0, 37°C, Co2+-bound enzyme
0.012
N-Benzyloxycarbonyl-L-phenylalanine
-
pH 5.1, 37°C, Zn2+-bound enzyme
0.16
N-Benzyloxycarbonyl-L-phenylalanine
-
pH 7.1, 37°C, Co2+-bound enzyme
0.37
N-Benzyloxycarbonyl-L-phenylalanine
-
pH 7.0, 37°C, Zn2+-bound enzyme
0.007
N-benzyloxycarbonyl-L-tryptophan
-
pH 5.0, 37°C, Co2+-bound enzyme
0.008
N-benzyloxycarbonyl-L-tryptophan
-
pH 5.0, 37°C, Zn2+-bound enzyme
0.087
N-benzyloxycarbonyl-L-tryptophan
-
pH 7.0, 37°C, Zn2+-bound enzyme
0.19
N-benzyloxycarbonyl-L-tryptophan
-
pH 7.0, 37°C, Zn2+-bound enzyme, in presence of 1 M NaSCN
0.21
N-benzyloxycarbonyl-L-tryptophan
-
pH 7.0, 37°C, Co2+-bound enzyme, in presence of 1 M NaSCN
0.00003
phosphoramidon
-
pH 7.2, temperature not specified in the publication
0.00003
phosphoramidon
-
pH 7.2, 25°C, enzyme contains Zn2+
0.000031
phosphoramidon
-
pH 7.4, 37°C, mutant Y157F
0.000032
phosphoramidon
-
pH 7.2, 25°C
0.00006
phosphoramidon
-
pH 6.8, 37°C, wild-type
0.00006
phosphoramidon
-
pH 7.4, 37°C, wild-type
0.00019
phosphoramidon
-
pH 7.4, 37°C, mutant D226A
0.0047
phosphoramidon
-
pH 6.8, 37°C, mutant R203M
0.0008
Retrothiorphan
-
pH 6.8, 37°C, wild-type
0.16
Retrothiorphan
-
pH 6.8, 37°C, mutant R203M
0.0016
thiorphan
pH 8.0, 37°C
0.0016
thiorphan
-
pH 6.8, 37°C, wild-type
0.0016
thiorphan
-
pH 7.4, 37°C, wild-type
0.0033
thiorphan
-
pH 6.8, 37°C, mutant D170A
0.0076
thiorphan
-
pH 7.4, 37°C, mutant Y157F
0.013
thiorphan
-
pH 7.4, 37°C, mutant D226A
0.16
thiorphan
-
pH 6.8, 37°C, mutant R203M
0.008
Z-L-phenylalanine
-
pH 5.0, 25°C, enzyme contains Co2+
0.16
Z-L-phenylalanine
-
pH 7.1, 25°C, enzyme contains Co2+
0.37
Z-L-phenylalanine
-
pH 7.0, 25°C, enzyme contains Zn2+
0.007
Z-L-tryptophan
-
pH 5.0, 25°C, enzyme contains Co2+
0.008
Z-L-tryptophan
-
pH 5.0, 25°C, enzyme contains Zn2+
0.012
Z-L-tryptophan
-
pH 5.1, 25°C, enzyme contains Zn2+
0.019
Z-L-tryptophan
-
pH 5.0, 25°C, enzyme contains Zn2+, presence of 1 M NaSCN
0.021
Z-L-tryptophan
-
pH 5.0, 25°C, enzyme contains Co2+, presence of 1 M NaSCN
0.087
Z-L-tryptophan
-
pH 7.0, 25°C, enzyme contains Zn2+
0.000012
Zincov
-
pH 7.5, 25°C, cobalt-substituted thermolysin
0.00023
Zincov
-
pH 7.5, 25°C
additional information
additional information
-
detailed inhibition kinetics with Co2+ and Zn2+, overview
-
additional information
additional information
-
inhibition kinetics with Co2+ and Ca2+, overview
-
additional information
additional information
-
organic solvent inhibition kinetics, overview
-
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0.07685
2-(4-methylphenyl)-3-(1,3-thiazol-2-yl) quinazolin-4(3H)-one
Bacillus thermoproteolyticus
-
at pH 7.0 and 25°C
0.00125
2-ethylquinazolin-4(3H)-one
Bacillus thermoproteolyticus
-
at pH 7.0 and 25°C
0.067
2-[(biphenyl-4-ylsulfonyl)[2-(hydroxyamino)-2-oxoethyl]amino]-N-[2-(4-sulfamoylphenyl)ethyl]acetamide (non-preferred name)
Bacillus thermoproteolyticus
-
pH 7.5, 37°C
0.012
2-[benzyl[2-(hydroxyamino)-2-oxoethyl]amino]-N-[2-(4-sulfamoylphenyl)ethyl]acetamide (non-preferred name)
Bacillus thermoproteolyticus
-
pH 7.5, 37°C
0.008
2-[benzyl[2-(hydroxyamino)-2-oxoethyl]amino]-N-[3-(4-phenylpiperazin-1-yl)propyl]acetamide (non-preferred name)
Bacillus thermoproteolyticus
-
pH 7.5, 37°C
0.164
2-[[2-(hydroxyamino)-2-oxoethyl][(4-methoxyphenyl)sulfonyl]amino]-N-[2-(4-sulfamoylphenyl)ethyl]acetamide (non-preferred name)
Bacillus thermoproteolyticus
-
pH 7.5, 37°C
0.16
2-[[2-(hydroxyamino)-2-oxoethyl][(4-phenoxyphenyl)sulfonyl]amino]-N-[2-(4-sulfamoylphenyl)ethyl]acetamide (non-preferred name)
Bacillus thermoproteolyticus
-
pH 7.5, 37°C
0.0002477
3-(isopropylideneamino)-2,2-dimethyl-2,3-dihydroquinazolin-4(1H)-one
Bacillus thermoproteolyticus
-
at pH 7.0 and 25°C
0.01832
3-([(1E)-[4-(dimethylamino) phenyl]methylene]amino)-2-methylquinazolin-4(3H)-one
Bacillus thermoproteolyticus
-
at pH 7.0 and 25°C
0.04203
3-([(1E)-[4-(dimethylamino) phenyl]methylene]amino)-2-phenylquinazolin-4(3H)-one
Bacillus thermoproteolyticus
-
at pH 7.0 and 25°C
12.74
3-amino-2-(4-chlorophenyl)quinazolin-4(3H)-one
Bacillus thermoproteolyticus
-
at pH 7.0 and 25°C
3.118
3-amino-2-(4-nitrophenyl)quinazolin-4(3H)-one
Bacillus thermoproteolyticus
-
at pH 7.0 and 25°C
0.03786
3-amino-2-(trifluoromethyl) quinazolin-4(3H)-one
Bacillus thermoproteolyticus
-
at pH 7.0 and 25°C
0.05489
3-amino-2-methylquinazolin-4(3H)-one
Bacillus thermoproteolyticus
-
at pH 7.0 and 25°C
0.0000115
3-phenyl-2-(trifluoromethyl) quinazolin-4(3H)-one
Bacillus thermoproteolyticus
-
at pH 7.0 and 25°C
4.002
3-[[(1E)-(3-chlorophenyl)methylene]amino]-2-phenylquinazolin-4(3H)-one
Bacillus thermoproteolyticus
-
at pH 7.0 and 25°C
122.6
ethanimidic acid N-[4-oxo-2-phenyl-3(4H)-quinazolinyl]-ethyl ester
Bacillus thermoproteolyticus
-
at pH 7.0 and 25°C
1
N-[(2R)-1-(hydroxyamino)-3-methyl-1-oxobutan-2-yl]-N-[(4-phenoxyphenyl)sulfonyl]glycine
Bacillus thermoproteolyticus
-
pH 7.5, 37°C
1
[(biphenyl-4-ylmethyl)[2-(hydroxyamino)-2-oxoethyl]amino]acetic acid
Bacillus thermoproteolyticus
-
pH 7.5, 37°C
0.44
[(biphenyl-4-ylsulfonyl)[2-(hydroxyamino)-2-oxoethyl]amino]acetic acid
Bacillus thermoproteolyticus
-
pH 7.5, 37°C
1
[1-[2-(hydroxyamino)-2-oxoethyl]-2-[3-(4-phenylpiperazin-1-yl)propyl]hydrazinyl]acetic acid
Bacillus thermoproteolyticus
-
pH 7.5, 37°C
0.637
[[(4-methoxyphenyl)sulfonyl](2-oxo-2-[[2-(4-sulfamoylphenyl)ethyl]amino]ethyl)amino]acetic acid
Bacillus thermoproteolyticus
-
pH 7.5, 37°C
0.755
[[2-(hydroxyamino)-2-oxoethyl](4-nitrobenzyl)amino]acetic acid
Bacillus thermoproteolyticus
-
pH 7.5, 37°C
0.524
[[2-(hydroxyamino)-2-oxoethyl](4-phenoxybenzyl)amino]acetic acid
Bacillus thermoproteolyticus
-
pH 7.5, 37°C
0.27
[[2-(hydroxyamino)-2-oxoethyl][(4-methoxyphenyl)sulfonyl]amino]acetic acid
Bacillus thermoproteolyticus
-
pH 7.5, 37°C
0.114
[[2-(hydroxyamino)-2-oxoethyl][(4-phenoxyphenyl)sulfonyl]amino]acetic acid
Bacillus thermoproteolyticus
-
pH 7.5, 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.34
-
mutant F114H, substrate casein, 25°C, pH 7.5
0.55
-
mutant N227A, substrate casein, 25°C, pH 7.5
0.62
-
mutant D150W, substrate casein, 25°C, pH 7.5
0.68
-
mutant I168A, substrate casein, 25°C, pH 7.5
0.84
-
mutant D150H, substrate casein, 25°C, pH 7.5
0.93
-
mutant D150E, substrate casein, 25°C, pH 7.5
1.08
-
wild-type, substrate casein, 25°C, pH 7.5
1.14
-
mutant F114A, substrate casein, 25°C, pH 7.5
1.18
-
mutant N227H, substrate casein, 25°C, pH 7.5
10.2
-
purified mutant enzyme S53D/L155A, using casein as substrate, at pH 7.5 and 25°C
10.5
-
purified mutant enzyme D150E, using casein as substrate, at pH 7.5 and 25°C
11.3
-
purified mutant enzyme S53D, using casein as substrate, at pH 7.5 and 25°C
11.9
-
purified mutant enzyme S53D/G8C/N60C/S65P, using casein as substrate, at pH 7.5 and 25°C
11000
-
recombinant wild-type enzyme, substrate casein, pH 7.5, 25°C
1468
purified native enzyme, pH 8.0, 30°C, substrate bovine serum albumin
2000
-
recombinant mutant G117D, substrate casein, pH 7.5, 25°C
2899
purified native enzyme, pH 8.0, 30°C, substrate gelatin
2900
-
recombinant mutant G117R, substrate casein, pH 7.5, 25°C
3.5
-
purified mutant enzyme L144S/D150E, using casein as substrate, at pH 7.5 and 25°C
3.6
-
purified mutant enzyme L144S, using casein as substrate, at pH 7.5 and 25°C
3077
purified native enzyme, pH 8.0, 30°C, substrate casein
3200
-
recombinant mutant G117K, substrate casein, pH 7.5, 25°C
373
purified native enzyme, pH 8.0, 30°C, substrate feather
489
purified native enzyme, pH 8.0, 30°C, substrate elastin
5300
purified recombinant mutant N116A, pH 7.5, 25°C, substrate N-[3-(2-furyl)acryloyl]-glycyl-L-leucine amide
5400
purified recombinant mutant N116T, pH 7.5, 25°C, substrate N-[3-(2-furyl)acryloyl]-glycyl-L-leucine amide
6.7
-
purified mutant enzyme L155A, using casein as substrate, at pH 7.5 and 25°C
6800
purified recombinant mutant N116Q, pH 7.5, 25°C, substrate N-[3-(2-furyl)acryloyl]-glycyl-L-leucine amide
697
purified native enzyme, pH 8.0, 30°C, substrate hemoglobin
7.5
-
purified mutant enzyme D150E/I168A, using casein as substrate, at pH 7.5 and 25°C
7.9
-
purified mutant enzyme S53D/L155A/G8C/N60C/S65P, using casein as substrate, at pH 7.5 and 25°C
7900
purified recombinant mutant N116D, pH 7.5, 25°C, substrate N-[3-(2-furyl)acryloyl]-glycyl-L-leucine amide
8.1
-
purified mutant enzyme L155A/G8C/N60C/S65P, using casein as substrate, at pH 7.5 and 25°C
855
purified native enzyme, pH 8.0, 30°C, substrate collagen
9.6
-
purified mutant enzyme I168A, using casein as substrate, at pH 7.5 and 25°C
9340
-
pH and temperature not specified in the publication
0.42
-
mutant I168H, substrate casein, 25°C, pH 7.5
0.42
-
mutant S234A, substrate casein, 25°C, pH 7.5
0.89
-
mutant D150A, substrate casein, 25°C, pH 7.5
0.89
-
mutant S169A, substrate casein, 25°C, pH 7.5
10.8
-
purified mutant enzyme G8C/N60C/S65P, using casein as substrate, at pH 7.5 and 25°C
10.8
-
purified wild type enzyme, using casein as substrate, at pH 7.5 and 25°C
12000
-
recombinant mutant G117E, substrate casein, pH 7.5, 25°C
12000
purified recombinant wild-type enzyme, pH 7.5, 25°C, substrate N-[3-(2-furyl)acryloyl]-glycyl-L-leucine amide
additional information
-
catalytic efficiency of wild-type and mutant enzymes in absence or presence of 4 M NaCl, overview
additional information
one proteolytic unit is defined as the amount which liberates a quantity of acid-soluble peptides that corresponds to an increase in A275 of 0.0074 (A275 of 1 mg of tyrosine)/min
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L155A
-
site-directed mutagenesis, the mutation abolishes the autodegradation activity, mutant thermostability at 80°C is slightly enhanced compared to the wild-type enzyme
L155A/I156N
-
site-directed mutagenesis, the mutation abolishes the autodegradation activity, mutant thermostability at 80°C is enhanced compared to the wild-type enzyme
L155A/I156V
-
site-directed mutagenesis, the mutation abolishes the autodegradation activity, mutant thermostability at 80°C is enhanced compared to the wild-type enzyme
L155S
-
site-directed mutagenesis, the mutation abolishes the autodegradation activity, mutant thermostability at 80°C is slightly enhanced compared to the wild-type enzyme
L155S/I156N
-
site-directed mutagenesis, the mutation abolishes the autodegradation activity, mutant thermostability at 80°C is enhanced compared to the wild-type enzyme
L155S/I156V
-
site-directed mutagenesis, the mutation abolishes the autodegradation activity, mutant thermostability at 80°C is enhanced compared to the wild-type enzyme
A113D
-
complete loss of activity
A113E
-
complete loss of activity
A113H
-
complete loss of activity
A113K
-
complete loss of activity
A113R
-
complete loss of activity
A4T/G8C/T56A/G58A/N60C/T63F/S65P/A69P
-
the mutant shows altered thermodynamics
A4T/T56A/G58A/T63F/S65P/A69P
-
the mutant shows altered thermodynamics
D150H
-
105% residual activity with casein, 37% residual activity with substrate N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide. Thermal inactivation at 80°C is greatly suppressed
D150K
-
51% residual activity with casein, no residual activity with substrate N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
D150R
-
44% residual activity with casein, no residual activity with substrate N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
D170E
-
complete loss of activity
D170H
-
complete loss of activity
D170K
-
complete loss of activity
D170R
-
complete loss of activity
D226A
-
site-directed mutagenesis
DELTA127
-
absence of CaCl2, 18% of wild-type activity, presence of 5 mM CaCl2, 71% of wild-type activity. Decrease in amount of enzyme secreted compared to wild-type
E143A
-
site-directed mutagenesis, E143A might exist as a complex with the propetide in the supernatant, inactive mutant, the autocatalytic activity is affected
F114D
-
complete loss of activity
F114E
-
complete loss of activity
F114H
-
18% residual activity with casein, 20% residual activity with substrate N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
F114K
-
complete loss of activity
F114R
-
complete loss of activity
G117D
-
site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type
G117E
-
site-directed mutagenesis, the mutant enzyme shows increased activity compared to the wild-type enzyme, the kcat/Km value is 80% of wild-type level with N-[3-(2-furyl)acryloyl]-glycyl-L-leucine amide, but 130% with N-benzyloxycarbonyl-L-Asp-L-Phe-methyl ester
G117K
-
site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type, the kcat/Km value is 40% of wild-type level with N-[3-(2-furyl)acryloyl]-glycyl-L-leucine amide, but 80% with N-benzyloxycarbonyl-L-Asp-L-Phe-methyl ester
G117R
-
site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type, the kcat/Km value is 40% of wild-type level with N-[3-(2-furyl)acryloyl]-glycyl-L-leucine amide and N-benzyloxycarbonyl-L-Asp-L-Phe-methyl ester
G162A
-
complete loss of activity
G162D
-
complete loss of activity
G162E
-
complete loss of activity
G162H
-
complete loss of activity
G162K
-
complete loss of activity
G162R
-
complete loss of activity
G8C/N60C
-
the mutant shows altered thermodynamics
H231A
-
the mutant shows 500fold decreased catalytic efficiency compared to the wild-type enzyme
I168D
-
complete loss of activity
I168E
-
complete loss of activity
I168H
-
13% residual activity with casein, 35% residual activity with substrate N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide. Thermal inactivation at 80°C is greatly suppressed
I168K
-
complete loss of activity
I168R
-
complete loss of activity
L144S/D150E
-
the mutation yields the most significant increase in the hydrolytic activities for N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide and N-carbobenzoxy-L-Asp-L-Phe methyl ester and shows about 30% casein-hydrolytic activity compared to the wild type enzyme
L144S/D150E/I168A/S53D/L155A/G8C/N60C/S65P
-
inactive
L144S/D150E/L155A
-
inactive
L144S/D150E/S53D
-
the triple mutant shows improved activity and stability with about 30% casein-hydrolytic activity compared to the wild type enzyme
L144S/D150E/S53D/L155A
-
inactive
L144S/D150W/N227H
-
the mutant shows 10fold decreased catalytic efficiency compared to the wild-type enzyme
L144S/I168A
-
the mutation abolishes the hydrolytic activities for N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide and N-carbobenzoxy-L-Asp-L-Phe methyl ester
L155A/G8C/N60C/S65P
-
the mutant shows about 80% casein-hydrolytic activity compared to the wild type enzyme
L155F
-
thermostability at 80°C increases with amino acid substitutions at L155 in the order of wild-type, Gly, Ser, Phe, Ala. Autodegradation site shifts from G154-L155 to F155-I156 and the bond I164-D165 is newly recognized as an autodegradation site
L155G
-
thermostability at 80°C increases with amino acid substitutions at L155 in the order of wild-type, Gly, Ser, Phe, Ala. Autodegradation site shifts from G154-L155 to G155-I156 and the bond I164-D165 is newly recognized as an autodegradation site
M205P
-
absence of CaCl2, 0.52% of wild-type activity, presence of 5 mM CaCl2, 48% of wild-type activity. Decrease in amount of enzyme secreted compared to wild-type
N116A
site-directed mutagenesis, the mutant shows slightly decreased activity compared to the wild-type enzyme
N116D
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
N116D/Q119R/D150Q/Q225R
-
the mutant shows 4fold decreased catalytic efficiency compared to the wild-type enzyme
N116Q
site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
N116T
site-directed mutagenesis, the mutant shows slightly decreased activity compared to the wild-type enzyme
N227A
-
72% residual activity with casein , 28% residual activity with substrate N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide. Thermal inactivation at 80°C is greatly suppressed
N227D
-
11% residual activity with casein, no residual activity with substrate N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
N227E
-
36% residual activity with casein, no residual activity with substrate N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
N227K
-
29% residual activity with casein, no residual activity with substrate N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
N227R
-
55% residual activity with casein, no residual activity with substrate N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
P208H
-
absence of CaCl2, 0.61% of wild-type activity, presence of 5 mM CaCl2, 61% of wild-type activity. Decrease in amount of enzyme secreted compared to wild-type
Q128A
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
Q128E
-
site-directed mutagenesis, the mutant shows similar activity compared to the wild-type enzyme
Q128K
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Q225A
-
site-directed mutagenesis, the mutant shows altered pKa value and stimulation of activity by NaCl and reduced activity with the negatively charged substrate N-carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester substrate compared to the wild-type enzyme
Q225D
-
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
Q225E
-
site-directed mutagenesis, the mutant shows similar activity compared to the wild-type enzyme
Q225K
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
Q225R
-
site-directed mutagenesis, the mutant shows similar activity compared to the wild-type enzyme
Q225V
-
site-directed mutagenesis, the mutant shows altered pKa value and stimulation of activity by NaCl and reduced activity with the negatively charged substrate N-carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester substrate compared to the wild-type enzyme
R203A
-
the mutant shows 5fold decreased catalytic efficiency compared to the wild-type enzyme
S103A
-
the mutant shows 3fold decreased catalytic efficiency compared to the wild-type enzyme
S169A
-
112% residual activity with casein, 64% residual activity with substrate N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
S169D
-
complete loss of activity
S169E
-
complete loss of activity
S169H
-
complete loss of activity
S169K
-
complete loss of activity
S169R
-
complete loss of activity
S198D
site directed mutagenesis, the mutant shows similar activity compared to the wild-type enzyme
S218D
site directed mutagenesis, the mutant shows similar activity compared to the wild-type enzyme
S234A
-
88% residual activity with casein, 17% residual activity with substrate N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide. Thermal inactivation at 80°C is greatly suppressed
S234D
-
5% residual activity with casein, no residual activity with substrate N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
S234E
-
4% residual activity with casein, 7% residual activity with substrate N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
S234H
-
32% residual activity with casein, no residual activity with substrate N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
S234K
-
complete loss of activity
S234R
-
complete loss of activity
S254D
site directed mutagenesis, the mutant shows similar activity compared to the wild-type enzyme
S25D
site directed mutagenesis, the catalytic activity is of the mutant enzyme is similar to the wild-type in absence of NaCl, but increased in presence of 4 M NaCl
S53D/G8C/N60C/S65P
-
the mutant shows about 110% casein-hydrolytic activity compared to the wild type enzyme
S53D/L155A
-
the mutation yields the greatest increase in the thermal stability and shows about 90% casein-hydrolytic activity compared to the wild type enzyme
S53D/L155A/G8C/N60C/S65P
-
the mutant shows about 70% casein-hydrolytic activity compared to the wild type enzyme
S65D
site directed mutagenesis, the catalytic activity is of the mutant enzyme is similar to the wild-type in absence of NaCl, but increased in presence of 4 M NaCl, increased thermostability in presence of 10 mM CaCl2
V230A
-
17% residual activity with casein, no residual activity with substrate N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
V230D
-
complete loss of activity
V230E
-
complete loss of activity
V230H
-
complete loss of activity
V230K
-
3% residual activity with casein, no residual activity with substrate N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
V230R
-
6% residual activity with casein, 12% residual activity with substrate N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
W115A
-
complete loss of activity
W115D
-
complete loss of activity
W115E
-
complete loss of activity
W115H
-
complete loss of activity
W115K
-
complete loss of activity
W115R
-
complete loss of activity
Y157A
-
11% residual activity with casein, no residual activity with substrate N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
Y157D
-
1% residual activity with casein, no residual activity with substrate N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
Y157E
-
13% residual activity with casein, no residual activity with substrate N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
Y157F
-
site-directed mutagenesis
Y157H
-
24% residual activity with casein, no residual activity with substrate N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
Y157K
-
7% residual activity with casein, no residual activity with substrate N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
Y157R
-
complete loss of activity
D170A
-
site-directed mutagenesis
-
R203M
-
site-directed mutagenesis
-
D150A
-
131% residual activity with casein, 81% residual activity with substrate N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
D150A
-
mutant with improved activity, the mutant has higher kcat values in N-carbobenzoxy-L-Asp-L-Phe-methyl ester synthesis than wild type
D150E
-
128% residual activity with casein, 228% residual activity with substrate N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
D150E
-
mutant with improved activity, the mutant has higher kcat values in N-carbobenzoxy-L-Asp-L-Phe-methyl ester synthesis than wild type
D150E
-
the mutation increases the activity of thermolysin
D150W
-
81% residual activity with casein, 60% residual activity with substrate N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide. Thermal inactivation at 80°C is greatly suppressed
D150W
-
mutant with improved activity, the mutant has higher kcat values in N-carbobenzoxy-L-Asp-L-Phe-methyl ester synthesis than wild type
D170A
-
complete loss of activity
D170A
-
site-directed mutagenesis
F114A
-
mutant with reduced activity
F114A
-
28% residual activity with casein, 8% residual activity with substrate N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide
G8C/N60C/S65P
-
site-directed mutagenesis, the mutant shows a similar catalytic efficiency compared tot he wild-type enzyme
G8C/N60C/S65P
-
the mutation increases the stability of thermolysin
G8C/N60C/S65P
-
the triple mutation increases the stability of thermolysin as high as the individual mutations do
G8C/N60C/S65P/L144S
-
site-directed mutagenesis, the mutant shows about 6fold increased catalytic effiency compared to the wild-type enzyme
G8C/N60C/S65P/L144S
-
the mutant is more active and stable than wild type thermolysin
I168A
-
69% residual activity with casein, 125% residual activity with substrate N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide. Thermal inactivation at 80°C is greatly suppressed
I168A
-
mutant with improved activity, the mutant has higher kcat values in N-carbobenzoxy-L-Asp-L-Phe-methyl ester synthesis than wild type
I168A
-
the mutation increases the activity of thermolysin and shows about 90% casein-hydrolytic activity compared to the wild type enzyme
L144S
-
site-directed mutagenesis, the mutant shows about 10fold increased catalytic effiency compared to the wild-type enzyme
L144S
-
the mutation increases the activity of thermolysin and shows about 30% casein-hydrolytic activity compared to the wild type enzyme
L155A
-
absence of CaCl2, 87% of wild-type activity, presence of 5 mM CaCl2, 83% of wild-type activity. Amount of enzyme secreted is about the same level as wild-type
L155A
-
thermostability at 80°C increases with amino acid substitutions at L155 in the order of wild-type, Gly, Ser, Phe, Ala. Autodegradation site shifts from G154-L155 to A155-I156 and the bond I164-D165 is newly recognized as an autodegradation site
L155A
-
the mutation increases the stability of thermolysin and shows about 60% casein-hydrolytic activity compared to the wild type enzyme
L155S
-
thermostability at 80°C increases with amino acid substitutions at L155 in the order of wild-type, Gly, Ser, Phe, Ala. Autodegradation site shifts from G154-L155 to S155-I156 and the bond I164-D165 is newly recognized as an autodegradation site
L155S
-
the mutant shows increased stability at 80°C compared to the wild-type enzyme
N112A
no enzymic activity in supernatant of cells expressing mutant
N112A
-
site-directed mutagenesis, inactive mutant, the autocatalytic activity is affected
N112D
supernatants of cells expressing mutant show 18% of wild-type activity
N112D
-
site-directed mutagenesis, the autocatalytic activity is affected
N112D
-
the mutant shows an altered pKa value
N112E
supernatants of cells expressing mutant show 5% of wild-type activity
N112E
-
site-directed mutagenesis, the autocatalytic activity is affected
N112H
no enzymic activity in supernatant of cells expressing mutant
N112H
-
site-directed mutagenesis, inactive mutant, the autocatalytic activity is affected
N112K
no enzymic activity in supernatant of cells expressing mutant
N112K
-
site-directed mutagenesis, inactive mutant, the autocatalytic activity is affected
N112R
no enzymic activity in supernatant of cells expressing mutant
N112R
-
site-directed mutagenesis, inactive mutant, the autocatalytic activity is affected
N227H
-
19% residual activity with casein, 19% residual activity with substrate N-[3-(2-furyl)acryloyl]-Gly-L-Leu amide. Thermal inactivation at 80°C is greatly suppressed
N227H
-
mutant with improved activity, the mutant has higher kcat values in N-carbobenzoxy-L-Asp-L-Phe-methyl ester synthesis than wild type
R203M
-
site-directed mutagenesis
R203M
-
the mutant shows 2300fold decreased catalytic efficiency compared to the wild-type enzyme
S53D
site directed mutagenesis, the catalytic activity is of the mutant enzyme is similar to the wild-type in absence of NaCl, but increased in presence of 4 M NaCl, increased thermostability in presence of 10 mM CaCl2
S53D
-
the mutation increases the stability of thermolysin
additional information
-
a mutant thermolysin is affected by its autocatalytic digestion activity
additional information
-
generation of an engineered enzyme with a higher activity in the synthesis of N-carbobenzyloxy L-Asp-L-Phe methyl ester
additional information
-
evaluation of an efficient method for the immobilization of thermolysin using sodium chloride salting-in and consecutive microwave irradiation, overview. 4.6% of the relative activity for the immobilized thermolysin is detected when the immobilization mixture contains no salts, including ZnCl2, CaCl2 or NaCl
additional information
-
evaluation of an efficient method for the immobilization of thermolysin using sodium chloride salting-in and consecutive microwave irradiation, overview. 4.6% of the relative activity for the immobilized thermolysin is detected when the immobilization mixture contains no salts, including ZnCl2, CaCl2 or NaCl
-
additional information
-
generation of an engineered enzyme with a higher activity in the synthesis of N-carbobenzyloxy L-Asp-L-Phe methyl ester
additional information
-
generation of an engineered enzyme with a higher activity in the synthesis of N-carbobenzyloxy L-Asp-L-Phe methyl ester
-
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diagnostics
-
thermolysin is used in the diagnosis of prion diseases ovine scrapie and bovine spongiform encephalopathy, with similar sensitivity compared to proteinase K digestion, use of a protease to distinguish PrPC from PrPSc, overview
food industry
-
the enzyme can be used for production of caseicin A, an antimicrobial active peptide, from alpha-casein, for potential improvement of the safety of infant milk formula using milk-derived bioactive peptides
medicine
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
nutrition
-
the enzyme is used for synthesis of N-carbobenzyloxy L-Asp-L-Phe methyl ester, a precursor of the artificial sweetener aspartam
analysis
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
analysis
-
selective biotin tagging and thermolysin proteolysis of chloroplast outer envelope proteins reveals information on protein topology and association into complexes. 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
analysis
-
thermolysin offers a tool for complete solubilization of cartilage prior to comprehensive glycosaminoglycans(GAG)omic analysis, and is likely applicable to other collagen-rich tissues such as ligaments, skin, and blood vessels
industry
-
the enzyme is used for synthesis of N-carbobenzyloxy L-Asp-L-Phe methyl ester, a precursor of the artificial sweetener aspartam
industry
-
the enzyme is used for synthesis of N-carbobenzyloxy L-Asp-L-Phe methyl ester, a precursor of the artificial sweetener aspartam
-
synthesis
-
production of L-alpha-aspartame, which is used as a low-calorie sweetener in food, including soft drinks, table-top sweeteners, dairy products, instant mixes, dressings, jams, confectionary, toppings and in pharmaceuticals
synthesis
-
hydrolysis and condensation reactions of peptides catalyzed by enzyme can be reversibly controlled by on/off ultrasound irradiation depending on its frequency region
synthesis
-
immobilized 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
synthesis
-
immobilized enzyme 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
synthesis
introduction of ionizing residues into the active site of enzyme as a means of modifying its pH-activity profile
synthesis
-
the enzyme is used for synthesis of N-carbobenzyloxy L-Asp-L-Phe methyl ester, a precursor of the artificial sweetener aspartam
synthesis
-
the enzyme is used for synthesis of N-carbobenzyloxy L-Asp-L-Phe methyl ester, a precursor of the artificial sweetener aspartam
synthesis
-
thermolysin is industrially used for the synthesis of N-carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester, a precursor of an artificial sweetener aspartame, from N-carbobenzoxy-L-aspartic acid and L-phenylalanine methyl ester
synthesis
-
the enzyme can be used for production of caseicin A, an antimicrobial active peptide, from alpha-casein, for potential improvement of the safety of infant milk formula using milk-derived bioactive peptides
synthesis
using the enzyme to catalyze the condensation of the chiral aspartame-precursor, carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester, from the protected amino acid substrates carbobenzoxy-L-aspartic acid and L-phenylalanine methyl ester in large scale production. Analysis of the protease mediated peptide synthesisof a precursor of the artificial sweetener aspartame, a multiton peptide synthesis catalyzed by the enzyme thermolysin. X-ray structures of thermolysin in complex with aspartame substrates separately, and after protease mediated peptide synthesis in a crystal, rationalize the reaction's substrate preferences and reveal an unexpected form of substrate inhibition that explains its sluggishness. Structure guided optimization of this and other PMPS reactions could expand the economic viability of commercial peptides beyond current high-potency, low-volume therapeutics, with substantial green chemistry advantages
synthesis
sequential hydrolysis trypsin-thermolysin of commercial hydrolysate (prepared from solubilized milk proteins) has been performed to produce bioactive peptides, mainly casein phosphopeptides. Thermolysin was the last enzyme to be used, generating the final product, with a low content of aromatic amino acids and shorter peptides
synthesis
-
the enzyme is used for synthesis of N-carbobenzyloxy L-Asp-L-Phe methyl ester, a precursor of the artificial sweetener aspartam
-
additional information
-
thermolysin crystal can be used as the stationary phase in liquid chromatography to separate D/L-phenylglycine, thermolysin crystal is useful for chiral separation
additional information
-
thermolysin treatment improves the yield of human intestinal epithelial cells. The thermolysin and endothelin-3 method can be used to isolate and generate viable human intestinal epithelial cells from the human small intestine
additional information
-
thermolysin powder is not acutely toxic with an oral LD50 of more than 18,000 mg/kg (2520 mg/kg thermolysin protein) in rats and more than 24,000 mg/kg (3360 mg/kg protein) in mice. Subchronic feeding studies in rats for 91 days at doses up to 1000 mg/kg (390 mg/kg protein) revealed no significant differences between treated and non-treated groups, no evidence from allergenicity sequence analysis that thermolysin is an allergen, thermolysin is safe for use in food production