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(R,S)-2-benzyl-3-(tert-butylsulfonyl)propionic acid + H2O
(R)-2-benzyl-3-(tert-butylsulfonyl)propionic ethyl ester + (S)-2-benzyl-3-(tert-butylsulfonyl)propionic acid + ethanol
-
-
-
-
?
(R,S)-2-benzyl-3-[[1-methyl-1-((morpholin-4-yl)-carbonyl)ethyl]sulfonyl]propionic acid + H2O
(S)-2-benzyl-3-[[1-methyl-1-((morpholin-4-yl)-carbonyl)ethyl]sulfonyl]propionic acid + (R)-2-benzyl-3-[[1-methyl-1-((morpholin-4-yl)-carbonyl)ethyl]sulfonyl]propionic acid-ethyl ester + ethanol
-
-
-
-
?
(R/S)-(2-methylpropyl)butanedioic acid diethyl ester + H2O
(S)-(2-methylpropyl)butanedioic acid diethyl ester + (R)-(2-methylpropyl)butanedioic acid 4-ethyl ester + ethanol
-
-
-
-
?
1-phenylethanol + trifluoroethyl butyrate
?
-
-
-
-
?
1-propanol + N-acetyl phenylalanine ethyl ester
?
-
-
-
-
?
2 rac-1-(4-chlorophenyl)ethan-1-ol + vinyl butyrate
(1S)-1-(4-chlorophenyl)ethyl butyrate + (1R)-1-(4-chlorophenyl)ethan-1-ol + ?
-
-
-
?
2 rac-1-(4-methoxyphenyl)ethan-1-ol + vinyl butyrate
(1S)-1-(4-methoxyphenyl)ethyl butyrate + (1R)-1-(4-methoxyphenyl)ethan-1-ol + ?
substrate only of mutant G165L/M221F, not of the wild-type enzyme
-
-
?
2 rac-1-(4-methylphenyl)ethan-1-ol + vinyl butyrate
(1S)-1-(4-methylphenyl)ethyl butyrate + (1R)-1-(4-methylphenyl)ethan-1-ol + ?
substrate only of mutant G165L/M221F, not of the wild-type enzyme
-
-
?
2 rac-1-phenylbutan-1-ol + vinyl butyrate
(S)-1-phenylbutyl butyrate + (R)-1-phenylbutan-1-ol + ?
substrate only of mutant G165L/M221F, not of the wild-type enzyme
-
-
?
2 rac-1-phenylethanol + vinyl butyrate
(S)-1-phenylethyl butyrate + (R)-1-phenylethanol + ?
-
-
-
?
2 rac-1-phenylheptan-1-ol + vinyl butyrate
(S)-1-phenylheptyl butyrate + (R)-1-phenylheptan-1-ol + ?
substrate only of mutant G165L/M221F, not of the wild-type enzyme
-
-
?
2 rac-1-phenylpentan-1-ol + vinyl butyrate
(S)-1-phenylpentyl butyrate + (R)-1-phenylpentan-1-ol + ?
substrate only of mutant G165L/M221F, not of the wild-type enzyme
-
-
?
2 rac-1-phenylpropan-1-ol + vinyl butyrate
(S)-1-phenylpropyl butyrate + (R)-1-phenylpropan-1-ol + ?
substrate only of mutant G165L/M221F, not of the wild-type enzyme
-
-
?
2 rac-N-tert-butoxycarbonylphenylalanine ethyl thioester + 1-phenylmethanamine + tert-butanol
N-benzyl-Nalpha-(tert-butoxycarbonyl)-L-phenylalaninamide + (R)-N-tert-butoxycarbonylphenylalanine ethyl thioester + ?
-
continuous-flow cascade reactor system for subtilisin A-catalyzed dynamic kinetic resolution (DKR). The continuous-mode DKR of the racemic thioester in a serial cascade system of six biocatalyst-filled columns at 50°C for KR and five grafted silica gel-filled columns at 150°C for racemization results in the formation of the (S)-benzylamide in 79% conversion, 8.17 g/l/h volumetric productivity and 98% enantiomeric excess. Method evaluation, overview
-
-
?
67 kDa gamma-glutamyl transpeptidase + H2O
30 kDa gamma-glutamyl transpeptidase + ?
-
proteolytic digestion of 67 kDa gamma-glutamyl transpeptidase from Bacillus licheniformis ER-15 by subtilisin to the 30 kDa form, which in turn remains associated with subtilisin as a heterodimeric protein
-
-
?
Aalpha chain of fibrinogen + H2O
?
-
-
-
-
?
acetyl-L-Ala-L-Ala-L-Ala-4-nitroanilide + H2O
?
-
-
-
-
?
acetyl-L-Phe + ethanol
acetyl-L-Phe ethyl ester + H2O
acetyl-L-Phe ethyl ester + H2O
acetyl-L-Phe + ethanol
acetyl-L-Tyr + ethanol
acetyl-L-Tyr ethyl ester + H2O
-
-
-
-
r
acetyl-L-Tyr ethyl ester + H2O
acetyl-L-Tyr + ethanol
acid casein + H2O
?
-
purified caseins from animal's milk from cow, sheep, goat and water buffalo used as substrate for subtilisin, cow acid casein is the best substrate
-
?
Ala-Ala-Phe 7-amido-4-methylcoumarin + H2O
?
Ala-Ala-Pro-Leu-4-nitroanilide + H2O
Ala-Ala-Pro-Leu + 4-nitroaniline
low activity
-
-
?
Ala-Ala-Pro-Lys-4-nitroanilide + H2O
Ala-Ala-Pro-Lys + 4-nitroaniline
low activity
-
-
?
Ala-Ala-Pro-Met-4-nitroanilide + H2O
Ala-Ala-Pro-Met + 4-nitroaniline
low activity
-
-
?
Ala-Ala-Pro-Nle-4-nitroanilide + H2O
Ala-Ala-Pro-Nle + 4-nitroaniline
low activity
-
-
?
Ala-Ala-Pro-Phe 4-nitroanilide + H2O
?
Ala-Ala-Pro-Phe-4-nitroanilide + H2O
Ala-Ala-Pro-Phe + 4-nitroaniline
low activity
-
-
?
Ala-Ala-Val-Ala-4-nitroanilide + H2O
Ala-Ala-Val-Ala + 4-nitroaniline
low activity
-
-
?
Benzoyl-Arg ethyl ester + H2O
?
benzoyl-L-Arg + ethanol
benzoyl-L-Arg ethyl ester + H2O
-
-
-
-
r
Benzoyl-L-Arg ethyl ester + H2O
Benzoyl-L-Arg + ethanol
Benzyloxycarbonyl-Ala-Ala-Leu 4-nitroanilide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Gly-4-nitroanilide + H2O
benzyloxycarbonyl-Gly + 4-nitroaniline
-
-
-
-
?
Benzyloxycarbonyl-Gly-Gly-L-Leu-NH2 + H2O
?
-
-
-
-
?
Benzyloxycarbonyl-Gly-L-Leu-NH2 + H2O
?
-
-
-
-
?
Benzyloxycarbonyl-Gly-L-Tyr-NH2 + H2O
?
-
-
-
-
?
Benzyloxycarbonyl-glycyl-L-tyrosinamide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-L-Ala ethyl ester + butanol
benzyloxycarbonyl-L-Ala butyl ester + ethanol
-
in isooctane, preferential use of L-enantiomer. Comparison with enantioselectivity in water and DMSO
-
-
?
benzyloxycarbonyl-L-Ala-L-Ala-L-Leu-4-nitroanilide + H2O
benzyloxycarbonyl-L-Ala-L-Ala-L-Leu + 4-nitroaniline
benzyloxycarbonyl-L-Asp methyl ester + serine amide
benzyloxycarbonyl-L-Asp-L-Ser-NH2 + methanol
-
-
-
-
?
beta subunit of haemoglobin + H2O
?
-
-
-
-
?
Bovine serum albumin + H2O
?
Carboxybenzoyl-Gly-Ala-NH2 + H2O
Carboxybenzoyl-Gly-Ala + NH3
-
subtilisin BPN'
subtilisin BPN'
?
Carboxybenzoyl-Gly-Leu-NH2 + H2O
Carboxybenzoyl-Gly-Leu + NH3
-
subtilisin BPN'
subtilisin BPN'
?
Carboxybenzoyl-Gly-Pro-Leu-Gly-Pro-OH + H2O
Carboxybenzoyl-Gly-Pro-Leu + Gly-Pro-OH
-
subtilisin BPN'
subtilisin BPN'
?
chicken-feather keratin + H2O
?
-
-
-
-
?
Clupein + H2O
?
-
-
-
-
?
D-Val-Leu-Lys p-nitroanilide + H2O
D-Val-Leu-Lys + p-nitroaniline
-
-
-
?
eglin-c + H2O
?
-
proteinase inhibitor, subtilisin DY hydrolyses the peptide bond between residues 45 and 46 in the reactive centre of eglin-c
-
?
ethyl 2-(4-ethylphenoxy)propionate + butanol
butyl 2-(4-ethylphenoxy)propanoate + propanol
-
in isooctane, preferential use of S-enantiomer. Comparison with enantioselectivity in water and DMSO
-
-
?
Glp-Ala-Ala-Leu-p-nitroanilide + H2O
?
glutaryl-Ala-Ala-Pro-Leu-p-nitroanilide + H2O
glutaryl-Ala-Ala-Pro-Leu + p-nitroaniline
relative hydrolysis rate is 22%
-
-
?
Hammarsten casein + H2O
?
Human fibrinogen + H2O
?
-
fibrinolytic activity is determined using the fibrin plate method
-
-
?
human fibronectin + H2O
?
-
-
-
-
?
insoluble elastin + H2O
?
-
-
-
-
?
IvaP I9 domain + H2O
?
a temporary inhibitor and substrate of purified IvaP
-
-
?
kappa casein + H2O
?
-
purified caseins from animal's milk from cow, sheep, goat and water buffalo used as substrate for subtilisin
-
?
L-Ala-L-Ala-L-Ala-L-Ala-L-Pro-L-Phe + H2O
?
-
-
-
-
?
L-Ala-L-Ala-L-Phe-L-Ala-L-Ala-L-Phe + H2O
?
-
-
-
-
?
L-Ala-L-Ala-L-Pro-L-Ala + H2O
?
-
-
-
-
?
L-Ala-L-Ala-L-Pro-L-Phe + H2O
?
-
-
-
-
?
L-Ala-L-Ala-L-Val-L-Ala + H2O
?
-
-
-
-
?
L-Lys-L-His-L-Asp-L-Arg-L-Lys-L-Asp + H2O
?
-
-
-
-
?
L-Phe-L-Ala-L-Ala-L-Phe + H2O
?
-
-
-
-
?
L-phenylalanine-isopropylester + H2O
L-phenylalanine + isopropanol
-
-
-
-
?
L-Tyr-L-Val-L-Ala-L-Asp + H2O
?
-
-
-
-
?
lactate dehydrogenase + H2O
?
poor substrate in native form, but can be digested in heat-denatured form
-
-
?
malate dehydrogenase + H2O
?
poor substrate in native form, but can be digested in heat-denatured form
-
-
?
MeO-succinyl-Ala-Ala-Phe 4-nitroanilide + H2O
?
methoxysuccinyl-Ala-Ile-Pro-Met-p-nitroanilide + H2O
methoxysuccinyl-Ala-Ile-Pro-Met + p-nitroaniline
is the most favorable substrate, relative hydrolysis rate is 100%
-
-
?
methyl mandelate + butanol
butyl mandelate + methanol
-
in isooctane, preferential use of S-enantiomer. Comparison with enantioselectivity in water and DMSO
-
-
?
N-Acetyl-Ala methyl ester + H2O
?
-
subtilisin BPN'
-
-
?
N-Acetyl-Gly ethyl ester + H2O
?
-
subtilisin BPN'
-
-
?
N-Acetyl-L-norvaline ethyl ester + H2O
?
-
subtilisin BPN'
-
-
?
N-acetyl-L-phenylalanine ethyl ester
?
-
-
-
-
?
N-acetyl-L-phenylalanine ethyl ester + 1-butanol
?
-
transesterification catalyzed by poly(ethylene glycol)-modified subtilisin
-
-
?
N-acetyl-L-phenylalanine ethyl ester + H2O
?
-
-
-
-
?
N-Acetyl-Leu methyl ester + H2O
?
-
subtilisin BPN'
-
-
?
N-Acetyl-Lys methyl ester + H2O
?
-
subtilisin BPN'
-
-
?
N-Acetyl-Phe ethyl ester + H2O
?
-
subtilisin BPN'
-
-
?
N-Acetyl-Phe methyl ester + H2O
?
N-Acetyl-Trp ethyl ester + H2O
?
-
subtilisin BPN'
-
-
?
N-Acetyl-Trp methyl ester + H2O
?
N-Acetyl-Tyr ethyl ester + H2O
?
N-acetyl-Tyr ethyl ester + H2O
N-acetyl-Tyr + ethanol
-
-
-
?
N-Acetyl-Tyr methyl ester + H2O
?
N-Acetyl-Val methyl ester + H2O
?
N-acetylglucosamine + H2O
?
N-CBZ-Gly-Gly-Leu p-nitroanilide + H2O
?
-
-
-
-
?
N-methoxysuccinyl-Ala-Ala-Pro-Val-4-nitroanilide + H2O
N-methoxysuccinyl-Ala-Ala-Pro-Val + 4-nitroaniline
-
-
-
-
?
N-methoxysuccinyl-Ala-Ala-Pro-Val-p-nitroanilide + H2O
N-methoxysuccinyl-Ala-Ala-Pro-Val + p-nitroaniline
N-Succ-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-Succ-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
N-succinyl-Ala-Ala-Pro-Leu-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Leu + 4-nitroaniline
-
-
-
?
N-succinyl-Ala-Ala-Pro-Met-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Met + p-nitroaniline
relative hydrolysis rate is 39%
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
?
-
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
N-succinyl-Ala-Ala-Val-Ala-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Val-Ala + 4-nitroaniline
-
-
-
?
N-succinyl-L-Ala-L-Ala-L-L-Ala-4-nitroanilide + H2O
?
N-succinyl-L-Ala-L-Ala-L-Pro-L-Leu-4-nitroanilide + H2O
?
N-succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-nitroanilide + H2O
?
N-succinyl-L-Ala-L-Ala-L-Val-4-nitroanilide + H2O
?
N-tosyl-L-Arg methyl ester + H2O
N-tosyl-L-Arg + methanol
N-trans-cinnamoyl imidazole + H2O
(E)-cinnamate + imidazole
-
-
-
-
?
Nalpha-benzoyl-DL-Arg-4-nitroanilide + H2O
Nalpha-benzoyl-DL-Arg + 4-nitroaniline
-
-
-
-
?
Nalpha-Benzoyl-L-Arg ethyl ester + H2O
?
-
-
-
-
?
Oxidized insulin B-chain + H2O
?
oxidized insulin chain B + H2O
?
-
is cleaved by subtilisin-like serine protease at multiple sites, preferably at the C-termini of the hydrophobic residues, such as Tyr, Phe, Leu, Val and Ala. This peptide is also cleaved by subtilisin at the C-termini of the hydrophobic residues, but at more specific sites
-
-
?
p-nitrophenyl butyrate + H2O
p-nitrophenol
-
catalyzed by native subtilisin
-
-
?
peanut flour + H2O
?
-
6 h alcalase hydrolysate
-
-
?
peptidyl-4-nitroanilide + H2O
?
-
-
-
?
Phe-Ala-Ala-Phe-4-nitroanilide + H2O
Phe-Ala-Ala-Phe + 4-nitroaniline
highly preferred substrate
-
-
?
porcine brain tubulin + H2O
peptides
-
MALDI-mass spectrum of the carboxy-terminal peptides released by subtilisin treatment. Polyglutamylated peptides from the beta subunit and from both the tyrosinated and detyrosinated forms of the alpha subunit are observed. The fragments removed by subtilisin are in the range of 1.6 kDa. Post-translational modifications can be directly identified in the mixture of peptides resulting from limited subtilisin treatment
-
-
?
proPhrA + H2O
PhrA
-
-
-
-
?
sec-phenethyl alcohol + vinyl butyrate
?
-
-
-
-
?
serum albumin + H2O
?
-
-
-
-
?
silk fibroin + H2O
?
-
-
-
-
?
Spirulina platensis powder + H2O
?
-
-
-
-
?
strobilurin fungicide + H2O
?
-
-
-
-
?
Suc-Ala-Ala-Pro-Phe-4-methyl-coumaryl-7-amide + H2O
?
-
-
-
-
?
Suc-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
Suc-Ala-Ala-Pro-Phe + 4-nitroaniline
succinyl-AAPA-p-nitroanilide + H2O
?
succinyl-AAPE-p-nitroanilide + H2O
?
-
-
-
?
succinyl-AAPF-4-nitroanilide + H2O
succinyl-AAPF + 4-nitroaniline
-
-
-
?
succinyl-AAPF-p-nitroanilide + H2O
succinyl-AAPF + p-nitroaniline
succinyl-AAPR-p-nitroanilide + H2O
?
-
-
-
?
Succinyl-Ala-Ala 4-nitroanilide + H2O
?
Succinyl-Ala-Ala-Ala 4-nitroanilide + H2O
?
succinyl-Ala-Ala-Ala-Ala-Ala-p-nitroanilide + H2O
succinyl-AAAAA + p-nitroaniline
-
-
-
?
succinyl-Ala-Ala-Ala-p-nitroanilide + H2O
succinyl-AAA + p-nitroaniline
-
-
-
?
succinyl-Ala-Ala-p-nitroanilide + H2O
succinyl-Ala-Ala + p-nitroaniline
-
-
-
?
succinyl-Ala-Ala-Phe-4-nitroanilide + H2O
succinyl-Ala-Ala-Phe + 4-nitroaniline
-
-
-
-
?
succinyl-Ala-Ala-Pro-Ala-p-nitroanilide + H2O
succinyl-AAPA + p-nitroaniline
-
-
-
?
succinyl-Ala-Ala-Pro-Leu-p-nitroanilide + H2O
succinyl-AAPL + p-nitroaniline
-
-
-
?
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
succinyl-Ala-Ala-Pro-Phe-7-amido-4-methylcoumarin + H2O
succinyl-Ala-Ala-Pro-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
-
-
-
-
?
succinyl-Ala2-Phe-4-methylcoumarin 7-amide + H2O
?
-
-
-
?
succinyl-L-Ala-L-Ala-L-Ala-4-nitroanilide + H2O
?
-
-
-
-
?
succinyl-L-Ala-L-Ala-L-Phe-7-amido-4-methylcoumarin + H2O
succinyl-L-Ala-L-Ala-L-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-L-Ala-L-Ala-L-Pro-Gly-4-nitroanilide + H2O
succinyl-L-Ala-L-Ala-L-Pro-Gly + 4-nitroaniline
-
-
-
-
?
succinyl-L-Ala-L-Ala-L-Pro-L-Ala-4-nitroanilide + H2O
succinyl-L-Ala-L-Ala-L-Pro-L-Ala + 4-nitroaniline
-
-
-
-
?
succinyl-L-Ala-L-Ala-L-Pro-L-Lys-4-nitroanilide + H2O
succinyl-L-Ala-L-Ala-L-Pro-L-Lys + 4-nitroaniline
-
-
-
-
?
succinyl-L-Ala-L-Ala-L-Pro-L-Met-4-nitroanilide + H2O
succinyl-L-Ala-L-Ala-L-Pro-L-Met + 4-nitroaniline
-
-
-
-
?
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-methyl-coumaryl-7-amide + H2O
succinyl-L-Ala-L-Ala-L-Pro-L-Phe + 7-amino-4-methylcoumarin
-
-
-
?
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-nitroanilide + H2O
?
-
-
-
-
?
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-nitroanilide + H2O
succinyl-L-Ala-L-Ala-L-Pro-L-Phe + 4-nitroaniline
-
-
-
-
?
succinyl-L-Ala-L-Ala-L-Pro-L-Tyr-4-nitroanilide + H2O
succinyl-L-Ala-L-Ala-L-Pro-L-Tyr + 4-nitroaniline
-
-
-
-
?
succinyl-L-Asp-L-Val-L-Arg-L-Ala-L-Phe-7-amido-4-methylcoumarin + H2O
succinyl-L-Asp-L-Val-L-Arg-L-Ala-L-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
Succinyl-Leu-Leu-Val-Tyr 4-methylcoumarin 7-amide + H2O
?
succinyl-Phe-Ala-Ala-Phe-p-nitroanilide + H2O
succinyl-Phe-Ala-Ala-Phe + p-nitroaniline
-
-
-
?
Toluenesulfonyl-Arg methyl ester + H2O
?
-
subtilisin Carlsberg, subtilisin Novo
-
-
?
type I keratin + H2O
?
-
-
-
-
?
Urea-denatured hemoglobin + H2O
?
vinyl butyrate + H2O
?
-
-
-
-
?
Z-Ala-Ala-Leu-OCH3 + H2O
?
-
-
-
-
?
Z-Ala-Ala-Leu-OMe + Phe-p-nitroanilide
Z-Ala-Ala-Leu-Phe-p-nitroanilide + methanol
-
-
-
-
?
Z-Ala-Ala-Leu-p-nitroanilide + H2O
?
Z-Ala-Phe-OMe + H2O
Z-Ala-Phe-NH2 + methanol
-
enzymatic method for the synthesis of free terminal amides of peptides, by ammonolysis of peptide methyl esters using ammonium carbamate and subtilisin A from Bacillus licheniformis in polar organic solvents with low water content is developed. Enzyme is very stable and active in a mixture of t-BuOH and DMF 82.5:17.5 (v/v), containing 0.2% water. Optimum conditions for Z-Ala-Phe-NH2 synthesis are molar ratio ammonium carbamate to Z-Ala-Phe-OMe 10, in t-BuOH/DMF, 82.5:17.5 (v/v) containing 0.2% (v) water, at 30°C for 21 h with the maximum yield of 87%
-
-
?
Z-Thr-Ala-Thr-OCH3 + Asp-p-nitroanilide
Z-Thr-Ala-Thr-Asp-p-nitroanilide + methanol
-
-
-
-
?
additional information
?
-
acetyl-L-Phe + ethanol
acetyl-L-Phe ethyl ester + H2O
-
-
-
-
r
acetyl-L-Phe + ethanol
acetyl-L-Phe ethyl ester + H2O
-
-
-
-
r
acetyl-L-Phe ethyl ester + H2O
acetyl-L-Phe + ethanol
-
-
-
-
r
acetyl-L-Phe ethyl ester + H2O
acetyl-L-Phe + ethanol
-
-
-
-
r
acetyl-L-Tyr ethyl ester + H2O
acetyl-L-Tyr + ethanol
-
-
-
-
r
acetyl-L-Tyr ethyl ester + H2O
acetyl-L-Tyr + ethanol
-
-
-
-
r
Ala-Ala-Phe 7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
Ala-Ala-Phe 7-amido-4-methylcoumarin + H2O
?
-
-
-
?
Ala-Ala-Phe 7-amido-4-methylcoumarin + H2O
?
-
-
-
?
Ala-Ala-Pro-Phe 4-nitroanilide + H2O
?
-
-
-
-
?
Ala-Ala-Pro-Phe 4-nitroanilide + H2O
?
-
-
-
-
?
alpha-casein + H2O
?
-
SES7 clleavage pattern, overview
-
-
?
alpha-casein + H2O
?
-
SES7 clleavage pattern, overview
-
-
?
azocasein + H2O
?
-
-
-
?
azocasein + H2O
?
-
-
-
?
azocasein + H2O
?
-
-
-
?
azocasein + H2O
?
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
Benzoyl-Arg ethyl ester + H2O
?
-
subtilisin Carlsberg, subtilisin Novo
-
-
?
Benzoyl-Arg ethyl ester + H2O
?
-
subtilisin BPN', subtilisin Amylosacchariticus
-
-
?
Benzoyl-L-Arg ethyl ester + H2O
Benzoyl-L-Arg + ethanol
-
-
-
-
r
Benzoyl-L-Arg ethyl ester + H2O
Benzoyl-L-Arg + ethanol
-
-
-
-
r
benzyloxycarbonyl-L-Ala-L-Ala-L-Leu-4-nitroanilide + H2O
benzyloxycarbonyl-L-Ala-L-Ala-L-Leu + 4-nitroaniline
-
-
-
-
?
benzyloxycarbonyl-L-Ala-L-Ala-L-Leu-4-nitroanilide + H2O
benzyloxycarbonyl-L-Ala-L-Ala-L-Leu + 4-nitroaniline
-
-
-
-
?
beta-casein + H2O
?
-
SES7 clleavage pattern, overview
-
-
?
beta-casein + H2O
?
-
SES7 clleavage pattern, overview
-
-
?
beta-casein + H2O
?
-
-
-
-
?
beta-casein + H2O
?
-
from bovine milk
-
-
?
beta-casein + H2O
?
-
-
-
-
?
beta-casein + H2O
?
-
from bovine milk
-
-
?
Bovine serum albumin + H2O
?
-
-
-
-
?
Bovine serum albumin + H2O
?
poor substrate in native form, but can be digested in heat-denatured form
-
-
?
Bovine serum albumin + H2O
?
-
-
-
-
?
Bovine serum albumin + H2O
?
-
-
-
?
Bovine serum albumin + H2O
?
-
-
-
?
Bovine serum albumin + H2O
?
-
-
-
-
?
Bovine serum albumin + H2O
?
-
-
-
-
?
casein + H2O
?
38% activity relative to gelatin as substrate. Also purified AcpII-C and AcpII-C-DELTAPA act well on casein
-
-
?
casein + H2O
?
38% activity relative to gelatin as substrate. Also purified AcpII-C and AcpII-C-DELTAPA act well on casein
-
-
?
casein + H2O
?
-
caseinolytic activity is determined using the casein plate method
-
-
?
chitin + H2O
?
-
-
-
-
?
Collagen + H2O
?
81% activity relative to gelatin as substrate. Also purified AcpII-C and AcpII-C-DELTAPA act well on collagen
-
-
?
Collagen + H2O
?
81% activity relative to gelatin as substrate. Also purified AcpII-C and AcpII-C-DELTAPA act well on collagen
-
-
?
cuticle + H2O
?
-
Pr1-like activity on host and non-host cuticle. In KV01 cultures, at 16 h, similar Pr1-like activity on both aphid and locust cuticle
-
-
?
cuticle + H2O
?
-
Pr1-like activity on host and non-host cuticle. In KV71 cultures, at 16 and 24 h, similar Pr1-like activity on both aphid and locust cuticle. Filtrates from KV71 and KV42 cultures, that contain cocktails of cuticle-degrading enzymes, hydrolyse 3-4fold more protein from aphid than locust cuticle
-
-
?
Cytochrome c + H2O
?
-
from equine heart
-
-
?
Cytochrome c + H2O
?
-
from equine heart
-
-
?
Elastin + H2O
?
7% activity relative to gelatin as substrate
-
-
?
Elastin + H2O
?
-
-
-
-
?
Elastin + H2O
?
-
-
-
-
?
Fibrin + H2O
?
-
strain DJ-4
-
?
Fibrin + H2O
?
-
strain DJ-4
-
?
Fibrinogen + H2O
?
rapid hydrolysis of Aalpha-, Bbeta- and gamma-chains. At very low concentration, no cleavage of gamma-chain
-
-
?
Fibrinogen + H2O
?
rapid hydrolysis of Aalpha-, Bbeta- and gamma-chains. At very low concentration, no cleavage of gamma-chain
-
-
?
Fibrinogen + H2O
?
-
-
-
?
Fibrinogen + H2O
?
-
-
-
?
Gelatin + H2O
?
best substrate for AcpII. Also purified AcpII-C and AcpII-C-DELTAPA act well on gelatin
-
-
?
Gelatin + H2O
?
best substrate for AcpII. Also purified AcpII-C and AcpII-C-DELTAPA act well on gelatin
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Glp-Ala-Ala-Leu-p-nitroanilide + H2O
?
-
-
-
-
?
Glp-Ala-Ala-Leu-p-nitroanilide + H2O
?
-
-
-
-
?
Glp-Ala-Ala-Leu-p-nitroanilide + H2O
?
-
-
-
-
?
Hammarsten casein + H2O
?
-
activation energy for hydrolysis 10.59 kcal per mol
-
-
?
Hammarsten casein + H2O
?
-
activation energy for hydrolysis 10.59 kcal per mol
-
-
?
Hemoglobin + H2O
?
-
-
-
-
?
Hemoglobin + H2O
?
-
denatured
-
-
?
Hemoglobin + H2O
?
-
-
-
-
?
Hemoglobin + H2O
?
-
-
-
-
?
intelectin + H2O
?
-
-
-
?
intelectin + H2O
?
enzyme IvaP is able to cleave purified intelectin, which inhibits intelectin binding to Vibrio cholerae
-
-
?
intelectin + H2O
?
-
-
-
?
intelectin + H2O
?
enzyme IvaP is able to cleave purified intelectin, which inhibits intelectin binding to Vibrio cholerae
-
-
?
intelectin + H2O
?
Vibrio cholerae serotype O1 C6706
-
-
-
?
intelectin + H2O
?
Vibrio cholerae serotype O1 C6706
enzyme IvaP is able to cleave purified intelectin, which inhibits intelectin binding to Vibrio cholerae
-
-
?
intelectin + H2O
?
-
-
-
?
intelectin + H2O
?
enzyme IvaP is able to cleave purified intelectin, which inhibits intelectin binding to Vibrio cholerae
-
-
?
Keratin + H2O
?
1.5% activity relative to gelatin as substrate
-
-
?
Keratin + H2O
?
1.5% activity relative to gelatin as substrate
-
-
?
Keratin + H2O
?
-
-
-
-
?
KOH chitin + H2O
?
-
-
-
-
?
KOH chitin + H2O
?
-
-
-
-
?
MeO-succinyl-Ala-Ala-Phe 4-nitroanilide + H2O
?
-
-
-
-
?
MeO-succinyl-Ala-Ala-Phe 4-nitroanilide + H2O
?
-
-
-
-
?
N-Acetyl-Phe methyl ester + H2O
?
-
subtilisin Amylosacchariticus
-
-
?
N-Acetyl-Phe methyl ester + H2O
?
-
subtilisin Carlsberg, subtilisin Novo
-
-
?
N-Acetyl-Trp methyl ester + H2O
?
-
subtilisin Amylosacchariticus
-
-
?
N-Acetyl-Trp methyl ester + H2O
?
-
subtilisin Carlsberg, subtilisin Novo
-
-
?
N-Acetyl-Tyr ethyl ester + H2O
?
-
-
-
-
?
N-Acetyl-Tyr ethyl ester + H2O
?
-
subtilisin Carlsberg, subtilisin Novo
-
-
?
N-Acetyl-Tyr ethyl ester + H2O
?
-
subtilisin BPN'
-
-
?
N-Acetyl-Tyr methyl ester + H2O
?
-
subtilisin Amylosacchariticus
-
-
?
N-Acetyl-Tyr methyl ester + H2O
?
-
subtilisin Carlsberg, subtilisin Novo
-
-
?
N-Acetyl-Val methyl ester + H2O
?
-
subtilisin Carlsberg, subtilisin Novo
-
-
?
N-Acetyl-Val methyl ester + H2O
?
-
subtilisin BPN'
-
-
?
N-acetylglucosamine + H2O
?
-
N-acetylglucosamine has little effect on subtilisin production by KV01 (11% of that on cuticle)
-
-
?
N-acetylglucosamine + H2O
?
-
restricted feeding of N-acetylglucosamine (the monomer of chitin) to biomass of KV71 induces protease to 61% of that on cuticle
-
-
?
N-methoxysuccinyl-Ala-Ala-Pro-Val-p-nitroanilide + H2O
N-methoxysuccinyl-Ala-Ala-Pro-Val + p-nitroaniline
-
-
-
?
N-methoxysuccinyl-Ala-Ala-Pro-Val-p-nitroanilide + H2O
N-methoxysuccinyl-Ala-Ala-Pro-Val + p-nitroaniline
-
-
-
?
N-methoxysuccinyl-Ala-Ala-Pro-Val-p-nitroanilide + H2O
N-methoxysuccinyl-Ala-Ala-Pro-Val + p-nitroaniline
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
Vibrio cholerae serotype O1 C6706
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
relative hydrolysis rate is 94%
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
-
-
-
-
?
N-succinyl-L-Ala-L-Ala-L-L-Ala-4-nitroanilide + H2O
?
-
3.8% of the activity with N-succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-nitroanilide
-
-
?
N-succinyl-L-Ala-L-Ala-L-L-Ala-4-nitroanilide + H2O
?
-
3.8% of the activity with N-succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-nitroanilide
-
-
?
N-succinyl-L-Ala-L-Ala-L-Pro-L-Leu-4-nitroanilide + H2O
?
-
19% of the activity with N-succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-nitroanilide
-
-
?
N-succinyl-L-Ala-L-Ala-L-Pro-L-Leu-4-nitroanilide + H2O
?
-
19% of the activity with N-succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-nitroanilide
-
-
?
N-succinyl-L-Ala-L-Ala-L-Pro-L-Leu-4-nitroanilide + H2O
?
-
-
-
-
?
N-succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-nitroanilide + H2O
?
-
-
-
-
?
N-succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-nitroanilide + H2O
?
-
-
-
-
?
N-succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-nitroanilide + H2O
?
-
-
-
-
?
N-succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-nitroanilide + H2O
?
-
-
-
-
?
N-succinyl-L-Ala-L-Ala-L-Val-4-nitroanilide + H2O
?
-
2.2% of the activity with N-succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-nitroanilide
-
-
?
N-succinyl-L-Ala-L-Ala-L-Val-4-nitroanilide + H2O
?
-
2.2% of the activity with N-succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-nitroanilide
-
-
?
N-tosyl-L-Arg methyl ester + H2O
N-tosyl-L-Arg + methanol
-
-
-
-
?
N-tosyl-L-Arg methyl ester + H2O
N-tosyl-L-Arg + methanol
-
subtilisin Carlsberg, subtilisin Novo, subtilisin Amylosacchariticus
-
-
?
Oxidized insulin B-chain + H2O
?
-
enzyme primarily hydrolyzes Leu15-Tyr16 bond and secondarily Gln4-His5, Ser9-His10, Phe24-Phe25 and Lys29-Ala30
-
-
?
Oxidized insulin B-chain + H2O
?
-
enzyme primarily hydrolyzes Leu15-Tyr16 bond and secondarily Gln4-His5, Ser9-His10, Phe24-Phe25 and Lys29-Ala30
-
-
?
proCSF + H2O
CSF
-
-
-
-
?
proCSF + H2O
CSF
-
-
-
-
?
Suc-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
Suc-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
Suc-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
Suc-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
Suc-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
Suc-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
Suc-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
Suc-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
succinyl-AAPA-p-nitroanilide + H2O
?
-
-
-
-
?
succinyl-AAPA-p-nitroanilide + H2O
?
-
-
-
?
succinyl-AAPF-p-nitroanilide + H2O
succinyl-AAPF + p-nitroaniline
-
-
-
?
succinyl-AAPF-p-nitroanilide + H2O
succinyl-AAPF + p-nitroaniline
-
-
-
?
succinyl-AAPF-p-nitroanilide + H2O
succinyl-AAPF + p-nitroaniline
-
-
-
?
succinyl-AAPF-p-nitroanilide + H2O
succinyl-AAPF + p-nitroaniline
-
-
-
?
succinyl-AAPF-p-nitroanilide + H2O
succinyl-AAPF + p-nitroaniline
-
-
?
Succinyl-Ala-Ala 4-nitroanilide + H2O
?
-
-
-
-
?
Succinyl-Ala-Ala 4-nitroanilide + H2O
?
-
-
-
-
?
Succinyl-Ala-Ala-Ala 4-nitroanilide + H2O
?
-
-
-
-
?
Succinyl-Ala-Ala-Ala 4-nitroanilide + H2O
?
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
Succinyl-Leu-Leu-Val-Tyr 4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
Succinyl-Leu-Leu-Val-Tyr 4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
ubiquitin + H2O
?
-
from bovine blood cells
-
-
?
ubiquitin + H2O
?
-
from bovine blood cells
-
-
?
Urea-denatured hemoglobin + H2O
?
-
-
-
-
?
Urea-denatured hemoglobin + H2O
?
-
-
-
-
?
Z-Ala-Ala-Leu-p-nitroanilide + H2O
?
-
-
-
-
?
Z-Ala-Ala-Leu-p-nitroanilide + H2O
?
-
-
-
-
?
Z-Ala-Ala-Leu-p-nitroanilide + H2O
?
-
-
-
-
?
additional information
?
-
substrate specificity, substrate docking simulations, overview. No activity with Ala-Ala-Pro-Glu-4-nitroanilide and Tyr-Val-Ala-Asp-4-nitroanilide. Substrate specificity and the role of stress signals such as divalent metal ions play roles in defining the proteolytic activity of Bacillus clausii intracellular subtilisin protease, molecular basis, overview. The enzyme unfolds under stress conditions. Heat-denatured whole proteins are found to be better substrates for the enzyme than the native forms
-
-
?
additional information
?
-
-
substrate specificity, substrate docking simulations, overview. No activity with Ala-Ala-Pro-Glu-4-nitroanilide and Tyr-Val-Ala-Asp-4-nitroanilide. Substrate specificity and the role of stress signals such as divalent metal ions play roles in defining the proteolytic activity of Bacillus clausii intracellular subtilisin protease, molecular basis, overview. The enzyme unfolds under stress conditions. Heat-denatured whole proteins are found to be better substrates for the enzyme than the native forms
-
-
?
additional information
?
-
N-succinyl-Ala-Ala-Val-Ala-p-nitroanilide and keratin are poor substrates for AcpII, with relative hydrolysis rates of 1-1.5% of the activity toward N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide or gelatin, respectively
-
-
?
additional information
?
-
-
N-succinyl-Ala-Ala-Val-Ala-p-nitroanilide and keratin are poor substrates for AcpII, with relative hydrolysis rates of 1-1.5% of the activity toward N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide or gelatin, respectively
-
-
?
additional information
?
-
N-succinyl-Ala-Ala-Val-Ala-p-nitroanilide and keratin are poor substrates for AcpII, with relative hydrolysis rates of 1-1.5% of the activity toward N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide or gelatin, respectively
-
-
?
additional information
?
-
-
N-succinyl-Ala-Ala-Val-Ala-p-nitroanilide and keratin are poor substrates for AcpII, with relative hydrolysis rates of 1-1.5% of the activity toward N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide or gelatin, respectively
-
-
?
additional information
?
-
-
reactions catalyzed: 1. peptide bond hydrolysis, 2. ester bond hydrolysis, 3. transesterification, 4. transpeptidation
-
-
?
additional information
?
-
-
reactions catalyzed: 1. peptide bond hydrolysis, 2. ester bond hydrolysis, 3. transesterification, 4. transpeptidation
-
-
?
additional information
?
-
-
alteration of substrate specificity by protein engineering
-
-
?
additional information
?
-
-
substrates bind in a less catalytically favorable conformation after the enzyme has been exposed to organic media for several hours
-
-
?
additional information
?
-
besides ester hydrolysis the enzyme also performs ester perhydrolysis reacting an ester and a hydroperpxide, residue Gl165 in the S1 binding pocket of the enzyme is involved. Perhydrolysis reaction analysis and kinetcis, overview
-
-
?
additional information
?
-
-
ionic-surfactant-coated Bacillus licheniformis subtilisin (ISCBLS) is a catalyst for the dynamic kinetic resolution of secondary alcohols. The engineered enzyme ISCBCL displays 9300fold enhanced activity relative to its native counterpart in the transesterificaion of N-acetyl phenylalanine ethyl ester with 1-propanol in hexane and 12800fold enhanced activity in the transesterification of trifluoroethyl butyrate with 1-phenylethanol in tetrahydrofuran. 50 secondary alcohols are evaluated as substrates for kinetic resolution in presence of trifluoroethyl butyrate, product determination and analysis, overview. The engineered enzyme displays enantioselectivity for most of the secondary alcohols tested
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additional information
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low catalytic activity of subtilisin Carlsberg (SC) for transacylation reactions with secondary alcohols in organic solvent, tetrahedral intermediates of the model reaction, enzyme with bound (S)-alpha-methylbenzyl butyrate or (R)-alpha-methylbenzyl butyrate, overview. The alkyl chain of the acyl donor, vinyl butyrate, is coordinated into the S1 binding pocket. The alkyl chain of the secondary alcohol is directed into the S1' binding pocket, and the phenyl group is directed towards the solvent. G165 is located in the bottom of the S1 pocket. Enantioselectivities of immobilized wild-type and mutants of subtilisin Carlsberg in the transacylation of racemic 1-phenylethanol and vinyl butyrate in tetrahydrofuran. Molecular modeling
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additional information
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random mutagenesis to enhance the activity of subtilisin in organic solvents
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additional information
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under relatively non-aqueous conditions, immobilized subtilisin is able to synthesize phenylacetic acid ethyl ester
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additional information
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high elastolytic acitivity
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additional information
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preferentially hydrolyzes the ester bond of Ala, but significant hydrolysis is observed with other aliphatic (Gly, Leu) and aromatic (Tyr) amino acids
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additional information
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reactions catalyzed: 1. peptide bond hydrolysis, 2. ester bond hydrolysis, 3. transesterification, 4. transpeptidation
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additional information
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reactions catalyzed: 1. peptide bond hydrolysis, 2. ester bond hydrolysis, 3. transesterification, 4. transpeptidation
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additional information
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little or no reaction with Glu-Phe-p-nitroanilide, benzyloxycarbonyl-Phe-p-nitroanilide, Suc-Phe-p-nitroanilide, acetyl-Phe-p-nitroanilide, Phe-p-nitroanilide, Gly-p-nitroanilide and Ala-p-nitroanilide at 75°C, and Val-Leu-Lys-p-nitroanilide, benzoyl-Arg-p-nitroanilide, Suc-Ala-Ala-p-nitroanilide, benzoyl-Tyr-p-nitroanilide, benzyloxycarbonyl-Lys-Arg-p-nitroanilide, and benzyloxycarbonyl-Arg-p-nitroanilide at 40°C
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additional information
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biosynthesis of subtilisin requires participation of an N-terminal prodomain
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additional information
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little or no reaction with Glu-Phe-p-nitroanilide, benzyloxycarbonyl-Phe-p-nitroanilide, Suc-Phe-p-nitroanilide, acetyl-Phe-p-nitroanilide, Phe-p-nitroanilide, Gly-p-nitroanilide and Ala-p-nitroanilide at 75°C, and Val-Leu-Lys-p-nitroanilide, benzoyl-Arg-p-nitroanilide, Suc-Ala-Ala-p-nitroanilide, benzoyl-Tyr-p-nitroanilide, benzyloxycarbonyl-Lys-Arg-p-nitroanilide, and benzyloxycarbonyl-Arg-p-nitroanilide at 40°C
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additional information
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high elastolytic acitivity
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additional information
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preferentially hydrolyzes the ester bond of Ala, but significant hydrolysis is observed with other aliphatic (Gly, Leu) and aromatic (Tyr) amino acids
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additional information
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random mutagenesis to enhance the activity of subtilisin in organic solvents
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additional information
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influence of substrate structure of N-protected peptide nitroanilides of the types: benzyloxycarbonyl-A2-A1 4-nitroanilide, benzyloxycarbonyl-A3-A2-A1 4-nitroanilide, benzyloxycarbonyl-A4-A3-A2-A1 4-nitroanilide, subsite S1 is of broad selectivity: preference for hydrophobic amino acid residues (i.e. leucine and phenylalanine) the beta-branched and the basic amino acid residues cannot interact with the S1 subsite and the hydrolysis of the corresponding peptides occurs exclusively at the A2-A1 bond. If S1/A1 interactions are weak (Ala, norvaline, norleucine) the amino acid residue A1 can interact with subsites S1 and S1' resulting in the hydrolysis of two bonds (A1 4-nitroanilide and A2-A1). The subsite S2 reveals a preference for small amino acid residues
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additional information
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reactions catalyzed: 1. peptide bond hydrolysis, 2. ester bond hydrolysis, 3. transesterification, 4. transpeptidation
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additional information
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does not cleave proPhrE
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additional information
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the enzyme shows activity towards complex substrates, e.g. skimmed milk
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additional information
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the enzyme shows activity towards complex substrates, e.g. skimmed milk
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additional information
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performance of a thrombolytic activity assay
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additional information
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the wild-type enzyme performs autoproteolysis, while the enzyme mutant S221C does not. The cleavage patterns of SES7 is determined by hydrolysates peptide profile, it prefers amino acids Q, T, P, or L at P3, P, V and Q at P2, K, L, N, Q, or F at P1, and F, S, or A at P1'
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additional information
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influence of substrate structure of N-protected peptide nitroanilides of the types: benzyloxycarbonyl-A2-A1 4-nitroanilide, benzyloxycarbonyl-A3-A2-A1 4-nitroanilide, benzyloxycarbonyl-A4-A3-A2-A1 4-nitroanilide, subsite S1 is of broad selectivity: preference for hydrophobic amino acid residues (i.e. leucine and phenylalanine) the beta-branched and the basic amino acid residues cannot interact with the S1 subsite and the hydrolysis of the corresponding peptides occurs exclusively at the A2-A1 bond. If S1/A1 interactions are weak (Ala, norvaline, norleucine) the amino acid residue A1 can interact with subsites S1 and S1' resulting in the hydrolysis of two bonds (A1 4-nitroanilide and A2-A1). The subsite S2 reveals a preference for small amino acid residues
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additional information
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random mutagenesis to enhance the activity of subtilisin in organic solvents
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additional information
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the wild-type enzyme performs autoproteolysis, while the enzyme mutant S221C does not. The cleavage patterns of SES7 is determined by hydrolysates peptide profile, it prefers amino acids Q, T, P, or L at P3, P, V and Q at P2, K, L, N, Q, or F at P1, and F, S, or A at P1'
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additional information
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performance of a thrombolytic activity assay
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additional information
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enzymes prefers cleaving after hydrophobic residues (and in particular P1 leucine)
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the Fusarium equiseti Fe protease has a broad substrate specificity, almost all amino acid residues are accepted at position P1, even though it shows some preference for cleavage at the C-terminal side of asparagine and histidine residues. The S4 subsite of Fe protease favors aspartic acid and threonine, substrate specificity and comprison to other subtilisin and selected fungal subtilisin-like proteases, overview
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additional information
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the Fe protease is active against beta-casein, while it shows poor activity with cytochrome c and ubiquitin. beta-Casein is fully digested, while cytochrome c and ubiquitin are not. Autoproteolytic degradation (autoproteolysis) of the purified recombinant Fe protease. The Fe protease has a broad substrate specificity: almost all amino acid residues are accepted at positions P1-4 and P1'-P4'. The protease has a slight preference for His and Asn in position P1. There are only two amino acids, Pro and Asp, which are rarely found in position P1. Hydrophobic amino acids are overrepresented in position P2, but Gly, Asp, and the aromatic amino acids Phe and Tyr are rarely found in P2. Gly and Thr are favored in position P3 and Thr and Asp in position P4. Tyrosine is common in the P1' position, unlike Phe which is rarely found in position P1'. Compared to other proteases, the Fe protease has unique cleavage site specificity
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additional information
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the Fe protease is active against beta-casein, while it shows poor activity with cytochrome c and ubiquitin. beta-Casein is fully digested, while cytochrome c and ubiquitin are not. Autoproteolytic degradation (autoproteolysis) of the purified recombinant Fe protease. The Fe protease has a broad substrate specificity: almost all amino acid residues are accepted at positions P1-4 and P1'-P4'. The protease has a slight preference for His and Asn in position P1. There are only two amino acids, Pro and Asp, which are rarely found in position P1. Hydrophobic amino acids are overrepresented in position P2, but Gly, Asp, and the aromatic amino acids Phe and Tyr are rarely found in P2. Gly and Thr are favored in position P3 and Thr and Asp in position P4. Tyrosine is common in the P1' position, unlike Phe which is rarely found in position P1'. Compared to other proteases, the Fe protease has unique cleavage site specificity
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additional information
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the Fusarium equiseti Fe protease has a broad substrate specificity, almost all amino acid residues are accepted at position P1, even though it shows some preference for cleavage at the C-terminal side of asparagine and histidine residues. The S4 subsite of Fe protease favors aspartic acid and threonine, substrate specificity and comprison to other subtilisin and selected fungal subtilisin-like proteases, overview
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displays preference for cleavage after Glu
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Sub2 undergoes self-digestion at high concentrations
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enzyme is able to hydrolyze a range of fluorogenic substrates, including AFC derivatives of VEID, VAD, YVAD, IETD, VDVAD and LEHD
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additional information
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enzyme is able to hydrolyze a range of fluorogenic substrates, including AFC derivatives of VEID, VAD, YVAD, IETD, VDVAD and LEHD
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degrades protein components of both nematode (Meloidogyne sp.) and insect (Phthorimaea opercullella) eggs
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contains the catalytic triad characteristic of subtilisin family proteinases: motif I (Asp200), motif II (His239), and motif III (Ser568). Has the Gram-positive cell wall anchoring motif (Leu-Pro-X-Thr-Gly) at the carboxy-terminus, which is followed by a hydrophobic domain
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additional information
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contains the catalytic triad characteristic of subtilisin family proteinases: motif I (Asp200), motif II (His239), and motif III (Ser568). Has the Gram-positive cell wall anchoring motif (Leu-Pro-X-Thr-Gly) at the carboxy-terminus, which is followed by a hydrophobic domain
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autoprocessing of Pro-subtilisin-like serine protease
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Ser361 contributes to IvaP autoprocessing in stationary-phase cultures
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enzyme IvaP performs autoprocessing involving residue Ser361. Identification of the N-terminal enzyme IvaP cleavage sequence AAQDNV
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Ser361 contributes to IvaP autoprocessing in stationary-phase cultures
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additional information
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enzyme IvaP performs autoprocessing involving residue Ser361. Identification of the N-terminal enzyme IvaP cleavage sequence AAQDNV
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Vibrio cholerae serotype O1 C6706
Ser361 contributes to IvaP autoprocessing in stationary-phase cultures
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additional information
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Vibrio cholerae serotype O1 C6706
enzyme IvaP performs autoprocessing involving residue Ser361. Identification of the N-terminal enzyme IvaP cleavage sequence AAQDNV
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additional information
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Ser361 contributes to IvaP autoprocessing in stationary-phase cultures
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additional information
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enzyme IvaP performs autoprocessing involving residue Ser361. Identification of the N-terminal enzyme IvaP cleavage sequence AAQDNV
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(dimethylamino)-1-naphthalenesulfonyl fluoride
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100% inhibition of enzyme activity with N-trans cinnamoyl imidazole as substrate, during prolonged exposure to organic solvents the active-site fluorescent label inhibitor adopts a different binding conformation
1,10-phenanthroline
at 37°C and pH of 7.5, 0.1 mM inhibits prosubtilisin JB1 by 40%
2,2'-[[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphoryl]bis(oxybenzene-4,1-diyl)]diacetic acid
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2,2'-[[(1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphoryl]bis(oxybenzene-4,1-diyl)]diacetic acid
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2,2'-[[(1-[[1-(tert-butoxycarbonyl)-L-prolyl]amino]-3-methylbutyl)phosphoryl]bis(oxybenzene-3,1-diyl)]diacetic acid
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2-phenylethaneboronic acid
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2-phenylethanesulfonic acid
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3,4-dichloroisocoumarin
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4-(2-aminoethyl)-benzenesulfonyl fluoride
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4-(2-aminoethyl)benzenesulfonyl fluoride
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4-(4'-Aminophenylazo)phenylarsonic acid
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4-bromophenacyl bromide
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5-Dimethylaminonaphthalene-1-sulfonate
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circular-dichroism and fluorescence studies of 5-dimethylaminonaphthalene-1-sulfonyl derivative of subtilisin indicate a closely similar structure to that of native subtilisin
acetonitril
high concentrations of acetonitrile significantly decrease the enzyme activity by over 60%, most likely due to disrupting the enzyme structural integrity
alpha2-Macroglobulin
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inhibits alkaline proteolytic activity of purified Arp by 80%
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angiotensin-converting enzyme
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IC50 is 0.067 mg/ml
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Benzyloxycarbonyl-(Ala)n-PheCH2Cl
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benzyloxycarbonyl-(Ala)2-PheCH2Cl is the best inhibitor
Benzyloxycarbonyl-Ala-XaaCH2Cl
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Xaa : Gly, Val, Ala, Leu, Phe
Benzyloxycarbonyl-L-phenylalanylbromomethane
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reactivity is about an order of magnitude less than that of subtilisins BPN' and Carlsberg
bis(2,3,5-trimethylphenyl) (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
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bis(2,3-dimethylphenyl) (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
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bis(2,3-dimethylphenyl) (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
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bis(2,5-dimethylphenyl) (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
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bis(2-methylphenyl) (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
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bis(2-methylphenyl) (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
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bis(3,4,5-trimethylphenyl) (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
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bis(3,4,5-trimethylphenyl) (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
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bis(3,4-dimethylphenyl) (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
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bis(3,4-dimethylphenyl) (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
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bis(3-chlorophenyl) (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
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bis(3-chlorophenyl) (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
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bis(3-methoxyphenyl) (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
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bis(4-chlorophenyl) (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
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bis(4-chlorophenyl) (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
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bis(4-ethylphenyl) (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
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bis(4-ethylphenyl) (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
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bis(4-methoxyphenyl) (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
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bis(4-methylphenyl) (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
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bis(4-tert-butylphenyl) (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
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bis(4-tert-butylphenyl) (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
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bis[4-(methylsulfonyl)phenyl] (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
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bis[4-(propan-2-yl)phenyl] (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
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bis[4-(propan-2-yl)phenyl] (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
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bis[4-(sulfanylmethyl)phenyl] (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
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bis[4-(sulfanylmethyl)phenyl] (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
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Brij 35
at 37°C and pH of 7.5, 0.01% reduces prosubtilisin JB1 relative activity to 30% and 0.05% reduces prosubtilisin JB1 relative activity to 70%
Broad bean extract
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subtilisin BPN'
Ca2+
at 37°C and pH of 7.5, 1 mM reduces prosubtilisin JB1 relative activity to 57% and 5 mM reduces prosubtilisin JB1 relative activity to 45%
Chiral amine- and aminoalcohol-derivatives
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Chymotrypsin I inhibitor from potato
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subtilisin Carlsberg, subtilisin BPN'
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chymotrypsin inhibitor 2
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chymotrypsin inhibitor 2 mutant M59A
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chymotrypsin inhibitor 2 mutant M59F
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chymotrypsin inhibitor 2 mutant M59G
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chymotrypsin inhibitor 2 mutant M59K
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chymotrypsin inhibitor 2 mutant M59Y
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chymotrypsin inhibitor 2 mutant Y61A
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Co2+
at 37°C and pH of 7.5, 1 mM reduces prosubtilisin JB1 relative activity to 14% and 5 mM reduces prosubtilisin JB1 relative activity to 24%
CrSPI-1
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Kazal-type inhibitor from the hepatopancreas of the Carcinoscorpius rotundicauda, potently inhibits subtilisin
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diisopropyl fluorophosphate
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diisopropylphosphofluoridate
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Dipeptidyl chloromethyl ketones
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diphenyl (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
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diphenyl (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
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E-64c
at 37°C and pH of 7.5, 0.1 mM inhibits prosubtilisin JB1 by 25%
EGTA
at 37°C and pH of 7.5, 0.1 mM inhibits prosubtilisin JB1 by 34%
EPI1a
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four-cysteine atypical Kazal-domain of protease inhibitor EPI1 from Phytophthora infestans. 80% inhibition at 0.00015 mM
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EPI1b
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typical Kazal-domain of protease inhibitor EPI1 from Phytophthora infestans, little inhibitory effect
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fungal protease inhibitor F
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specific inhibitor toward subtilisin-type protease. P1 residue most signficantly affects inhibitory specificity. Mutant T29M has stronger subtilisin-inhibitory activity than the wild-type, mutants T29E and T29R are relatively weaker inhibitors. Inhibitory activities of mutants T29F and T29L are as strong as that of the wild-type
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guanidine hydrochloride
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at 2 M inhibits subtilisin-like serine protease by 35% and at 4 M almost completely, whereas it has no inhibitory effect on subtilisin
guanidinium hydrochloride
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H2O2
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the enzyme activity is reduced to 68% after a 20-min incubation with 0.33% hydrogen peroxide at 25°C in Tris buffer, substrate suc-Ala-Ala-Pro-Phe-4-nitroanilide, recombinant enzyme
Hg+
at 37°C and pH of 7.5, 1 mM reduces prosubtilisin JB1 relative activity to 33% and 5 mM reduces prosubtilisin JB1 relative activity to 22%
human LEKTI
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noncompetitive inhibition
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human proteinase inhibitor 9
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PI9, serine proteinase inhibitor
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Inhibitor from Dolichos biflorus
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purification and properties
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Inhibitor from egg white
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Inhibitor from seeds of Canavalia lineata
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Inhibitor from seeds of Setaria italica
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purification and characterization
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Inhibitor from Streptomyces sp.
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Inhibitor from Streptomyces virginiae
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primary structure
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Inhibitor from Vigna unguiculata subsp. cylindrica
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Inhibitor of Amaranthus caudatus seeds
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Inhibitor of trypsin from soybean
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IvaP I9 domain
the N-terminal propeptide of enzyme IvaP, the IvaP I9 domain, can temporarily inhibit, and be cleaved by, the purified enzyme
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K+
at 37°C and pH of 7.5, with 1 mM results in an almost complete reduction of prosubtilisin JB1 activity, 5 mM reduces prosubtilisin JB1 relative activity to 53%
L-[(1R)-1-acetamido-2-(1-naphthyl)ethyl]boronic acid
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leupeptin
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inhibits the enzymatic activity by 20%
Mg2+
at 37°C and pH of 7.5, 1 mM reduces prosubtilisin JB1 relative activity to 79% and 5 mM reduces prosubtilisin JB1 relative activity to 48%
N-((tert-Butoxycarbonyl)alanylprolylphenylalanyl)-O-benzoylhydroxylamine
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N-(tert-butoxycarbonyl)-L-valyl-N-(1-[bis[4-(sulfanylmethyl)phenoxy]phosphoryl]-2-phenylethyl)-L-prolinamide
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N-(tert-butoxycarbonyl)-L-valyl-N-[1-(diphenoxyphosphoryl)-2-phenylethyl]-L-prolinamide
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N-(tert-butoxycarbonyl)-L-valyl-N-[1-[bis(3,4,5-trimethylphenoxy)phosphoryl]-3-methylbutyl]-L-prolinamide
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N-(tert-butoxycarbonyl)-L-valyl-N-[1-[bis(4-methoxyphenoxy)phosphoryl]-3-methylbutyl]-L-prolinamide
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N-(tert-butoxycarbonyl)-L-valyl-N-[1-[bis(4-tert-butylphenoxy)phosphoryl]-3-methylbutyl]-L-prolinamide
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N-acetyl-L-tryptophan amide
molecular dynamics simulations are performed with subtilisin in the presence and in the absence of an inhibitor both in hexane and in water. The inhibitor induces an open conformation of the S1 pocket that is maintained after the removal of the ligand in anhydrous, but not in aqueous, simulations. The analysis of fluctuations suggest that this behavior is caused by the decreased flexibility exhibited by subtilisin in hexane
N-benzoyl-L-Arg
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product inhibition
N-benzyloxycarbonyl-Ala-Pro-Phe-chloromethyl ketone
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synthetic inhibitor
N-ethylmaleimide
at 37°C and pH of 7.5, 0.1 mM inhibits prosubtilisin JB1 by 15%
N-tosyl-L-phenylalanyl chloromethyl ketone
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N1-18[ISP]
synthetic peptide corresponding to the N-terminal extension behaves as a mixed noncompetitive inhibitor of active ISP
neurolysin
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IC50 is 0.263 mg/ml
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p-chloromercuribenzoate
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partial inhibition
p-Nitrophenylarsonate
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pepstatin
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almost completely inhibits acid proteolytic activity, does not inhibit alkaline proteolytic activity of purified Arp
pepstatin A
at 37°C and pH of 7.5, 0.1 mM inhibits prosubtilisin JB1 by 48%
Peptidyl chloromethyl ketones
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phenylmethanesulfonyl fluoride
phenylmethylsulfonyl fluoride
Phenylmethylsulphonyl fluoride
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Potato extract
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subtilisin BPN'
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propeptide
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inhibition in a concentration-dependent manner. Wild-type propeptide is more potent than G56W-, G56S- and G56E-propeptide
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Suc-Val-Pro-PheP(OPh)2
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tert-butyl (2S)-2-([1-[bis(2-methylphenoxy)phosphoryl]-3-methylbutyl]carbamoyl)pyrrolidine-1-carboxylate
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tert-butyl (2S)-2-([1-[bis(3,4,5-trimethylphenoxy)phosphoryl]-3-methylbutyl]carbamoyl)pyrrolidine-1-carboxylate
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tert-butyl (2S)-2-([1-[bis(3,4-dimethylphenoxy)phosphoryl]-3-methylbutyl]carbamoyl)pyrrolidine-1-carboxylate
-
-
tert-butyl (2S)-2-([1-[bis(4-methoxyphenoxy)phosphoryl]-3-methylbutyl]carbamoyl)pyrrolidine-1-carboxylate
-
-
tert-butyl (2S)-2-([1-[bis(4-methylphenoxy)phosphoryl]-3-methylbutyl]carbamoyl)pyrrolidine-1-carboxylate
-
-
tert-butyl (2S)-2-[(1-[bis[4-(sulfanylmethyl)phenoxy]phosphoryl]-2-phenylethyl)carbamoyl]pyrrolidine-1-carboxylate
-
-
tert-butyl (2S)-2-[[1-(diphenoxyphosphoryl)-2-phenylethyl]carbamoyl]pyrrolidine-1-carboxylate
-
-
tomato inhibitor-II
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TI-II, enzyme binding structure, the interdomain interface in TI-II consists of a small cluster of highly conserved hydrophobic residues Ile14, Pro16, Tyr98, Phe100 and Phe106 from domain I and Tyr34, Pro54 and Lys55 from domain II. Although this interface is quite small (buried surface area of 487A), it forms a stable packing arrangement between the two domains. Each reactive site loop in TI-II interacts with a separate molecule of subtilisin in the canonical manner observed in other proteinaseinhibitor complexes. The domains of TI-II appear to bind the proteinase independently of each other
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tosyl-Phe chloromethyl ketone
Triton X-100
at 37°C and pH of 7.5, 0.01% reduces prosubtilisin JB1 relative activity to 92% and 0.05% reduces prosubtilisin JB1 relative activity to 69%
turkey egg white inhibitor
-
Tween 20
at 37°C and pH of 7.5, 0.01% reduces prosubtilisin JB1 relative activity to 53% and 0.05% reduces prosubtilisin JB1 relative activity to 70%
Urea
high concentrations (6 M) of urea significantly decrease the enzyme activity by over 60%, most likely due to disrupting the enzyme structural integrity
1,4-dioxane
-
104fold decrease in the enzymes catalytic activity for the hydrolysis reaction of vinyl butyrate with D2O and a 50% decrease in enzyme structural dynamics. Attaching increasing amounts of PEG to the enzyme reverses some of the activity loss. Poly(ethylene)-glycolylation increases protein structural dynamics in 1,4-dioxane
1,4-dioxane
-
reduces the enzyme activity. Structural changes, flexibility, hydration, and changes of the enzyme ionization state are not responsible for the low storage stability. Possible depletion or rearrangement of water molecules around the active site, or small structural perturbations around the active site or movements of counter ions
antipain
-
-
antipain
at 37°C and pH of 7.5, 0.1 mM inhibits prosubtilisin JB1 by 75%
antipain
-
totally inhibits recombinant Sub2
antipain
35% inhibition at 1 mM, 95% at 5 mM
Aprotinin
-
-
Aprotinin
-
inhibits the enzymatic activity by 15%
chymostatin
-
-
chymostatin
at 37°C and pH of 7.5, 0.1 mM inhibits prosubtilisin JB1 by 95%
chymostatin
-
totally inhibits recombinant Sub2
chymostatin
complete inhibition at 1 mM
Cu2+
-
strain DJ-4, strong inhibition
Cu2+
at 37°C and pH of 7.5, with 1 mM results in an almost complete reduction of prosubtilisin JB1 activity, 5 mM reduces prosubtilisin JB1 relative activity to 19%
E-64
at 37°C and pH of 7.5, 0.1 mM inhibits prosubtilisin JB1 by 31%
E-64
37% inhibition at 5 mM
EDTA
inactivates the enzyme at 0.01 mM, the enzyme protein becomes less structured and potentially monomeric. Removal of Ca2+ at sites close to the dimer interface and the S1 pocket are involved enzyme inhhibition by EDTA
EDTA
5 mM partially inhibits by 35%, in 100 mM Tris-HCl buffer, pH 7.0 at 15°C for 20 min
EDTA
at 37°C and pH of 7.5, 0.1 mM inhibits prosubtilisin JB1 by 52%
EDTA
-
subtilisin exhibits little activity at 80°C in the presence of 10 mM. Subtilisin-like serine protease is fully active even in the presence of 10 mM EDTA
Inhibitor from egg white
-
subtilisin Carlsberg, subtilisin BPN'
-
Inhibitor from egg white
-
-
-
Inhibitor from seeds of Canavalia lineata
-
low MW protein of about 6500 MW
-
Inhibitor from seeds of Canavalia lineata
-
MW 22000, Kunitz type inhibitors
-
Inhibitor from Vigna unguiculata subsp. cylindrica
-
inactive with other enzymes
-
Inhibitor from Vigna unguiculata subsp. cylindrica
-
properties and kinetics of the inhibitor
-
Inhibitor of Amaranthus caudatus seeds
-
subtilisin Novo (BPN') from Bacillus amyloliquefaciens, subtilisin Carlsberg from Bacillus licheniformis
-
Inhibitor of Amaranthus caudatus seeds
-
subtilisin Novo (BPN') from Bacillus amyloliquefaciens, subtilisin Carlsberg from Bacillus licheniformis
-
nitrogen
-
together with carbon significantly reduces protease activity of KV01 at 16 and 36 h, and KV54 at 16 h
nitrogen
-
absence of C or N metabolite repression in subtilisins from KV42 isolate. Together with carbon significantly reduces protease activity of KV71 at 16 and 36 h, and KV22 at 16 h
phenylmethanesulfonyl fluoride
-
-
phenylmethanesulfonyl fluoride
-
-
phenylmethanesulfonyl fluoride
-
totally inhibits recombinant Sub2
phenylmethylsulfonyl fluoride
-
1 mM, 82% inhibition
phenylmethylsulfonyl fluoride
1 mM completely inhibits, in 100 mM Tris-HCl buffer, pH 7.0 at 15°C for 20 min
phenylmethylsulfonyl fluoride
-
-
phenylmethylsulfonyl fluoride
-
strain DJ-4
phenylmethylsulfonyl fluoride
-
-
phenylmethylsulfonyl fluoride
-
1 mM, 5% residual activity
phenylmethylsulfonyl fluoride
at 37°C and pH of 7.5, 0.1 mM inhibits prosubtilisin JB1 by 79%
phenylmethylsulfonyl fluoride
-
inhibits alkaline proteolytic activity of purified Arp by 100%, does not inhibit acid proteolytic activity
PMSF
-
-
PMSF
-
circular-dichroism and fluorescence studies of PMSF derivative of subtilisin indicate a closely similar structure to that of native subtilisin
PMSF
complete inhibition at 10 mM, no effect at 0.01 mM
Sodium dodecyl sulfate
-
activity of the enzyme is retarded by 2.3 and 244times in 1 mM and 40 mM sodium dodecyl sulfate respectively compared to that in buffer solution. No evidence of sandwich-like subtilisinsodium dodecyl sulfate complex formation, thus the enzyme does not encroach into the hydrophobic surfactant core of sodium dodecyl sulfate micelle to form an elongated structure. Retains its structural integrity in sodium dodecyl sulfate solution. Micellar crowding in the vicinity of the enzyme
Sodium dodecyl sulfate
at 37°C and pH of 7.5, 0.01% reduces prosubtilisin JB1 relative activity to 52% and 0.05% reduces prosubtilisin JB1 relative activity to 29%
sucrose
-
together with carbon significantly reduces protease activity of KV01 at 16 and 36 h, and KV54 at 16 h
sucrose
-
absence of C or N metabolite repression in subtilisins from KV42 isolate. Together with carbon significantly reduces protease activity of KV71 at 16 and 36 h, and KV22 at 16 h
tosyl-Phe chloromethyl ketone
-
not
tosyl-Phe chloromethyl ketone
-
-
turkey egg white inhibitor
-
-
-
turkey egg white inhibitor
-
-
-
Zn2+
-
strain DJ-4, strong inhibition
Zn2+
-
1 mM, 59% residual activity
Zn2+
at 37°C and pH of 7.5, 1 mM reduces prosubtilisin JB1 relative activity to 30%, with 5 mM results in an almost complete reduction of prosubtilisin JB1 activity
additional information
-
not inhibited by 1,10 phenanthroline
-
additional information
-
not inhibitory: Tween-20, Tween-40, Tween-60, Tween-80 at 1%, sodium dodecylsulfate at 0.2%, for 1 h at 30°C. Not inhibitory: iodoacetate, ethylacetimide, phenylglyoxal, N-ethylmaleimide, N-bromosuccinimide
-
additional information
-
enzyme-specific, thermostable inhibitor from Physarum polycephalum with molecular mass of 32-33 kDa, 50% inhibition at 0.00014 mM
-
additional information
-
aldehyde and fluoromethyketone (FMK)-based inhibitors inhibit SAS-1 and -2 reversibly and only CMK-based inhibitors irreversibly inhibit the enzyme
-
additional information
-
molecular dynamics simulations, residue displacement correlations, and inhibitor design based on the enzyme inhibitor comlpex of TI-II and subtilisin, overview
-
additional information
-
not: tosyl-leucine chloromethyl ketone
-
additional information
-
metal chelating reagents; not: tosyl-leucine chloromethyl ketone; sulfhydryl reagents
-
additional information
-
strain DJ-4, no inhibition by EDTA or leupeptin
-
additional information
-
not inhibitory: EDTA at 5 mM
-
additional information
-
not inhibitory: sodium dodecylsulfate at 1 mM
-
additional information
at 37°C and pH of 7.5, 0.1 mM leupeptin does not inhibit prosubtilisin JB1
-
additional information
enzyme destabilization in the presence of EDTA is due to chelation of a tightly bound calcium ion by EDTA, rather than destabilizing effects caused by EDTA on the structure
-
additional information
-
is not inhibited by 1,10-phenanthroline, EDTA, E64, bestatin, phosphoramidon and pepstatin A
-
additional information
-
not inhibited by 1,10 phenanthroline
-
additional information
-
alkaline proteolytic activity of purified Arp not inhibited by 3,4-dichloroisocumarin, tosyl lysine chloromethyl ketone, tosyl phenylalanine chloromethyl ketone, leupeptin, chymostatin, elastatinal, iodoacetamide, E-64, EDTA, 1,10-phenanthroline, aprotinin, antithrombin III, alpha1-antitrypsin and soybean trypsin inhibitor
-
additional information
the enzyme activity is not affected by various metal ions or non-specific protease inhibitors, e.g. bestatin, leupeptin, or pefabloc SC
-
additional information
-
enzymatic activity of mature subtilisin is inhibited by G56S-propeptide and wild-type propeptide in a concentration-dependent manner
-
additional information
-
subtilisin-like serine protease is fully resistant to treatment with 2-5% SDS, 4-8 M urea, 10% Tween-20 or 10% Triton X-100. In gel assay, subtilisin-like serine protease is fully denatured prior to SDS-PAGE by trichloroacetic acid treatment, followed by boiling for 5 min in the presence of SDS
-
additional information
no inhibition by EDTA and benzamidine
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.85
acetyl-L-Phe
-
30°C, pH 8.0
0.22
acetyl-L-Phe ethyl ester
-
30°C, pH 8.0
4
acetyl-L-Tyr
-
30°C, pH 8.0
0.37
acetyl-L-Tyr ethyl ester
-
30°C, pH 8.0
7 - 10
benzoyl-Arg ethyl ester
2.1
benzoyl-L-Arg ethyl ester
-
30°C, pH 8.0
8.3
benzyloxycarbonyl-Gly-4-nitroanilide
-
pH 7.5, 20°C, in presence and absence of DTT
-
0.0054
benzyloxycarbonyl-L-Ala-L-Ala-L-Leu-4-nitroanilide
-
-
0.059
casein
-
pH 10, 45°C, Vmax: 0.336 mg/min
0.13 - 0.25
Glp-Ala-Ala-Leu-p-nitroanilide
0.98 - 1.99
L-Ala-L-Ala-L-Pro-L-Ala
1.15 - 1.93
L-Ala-L-Ala-L-Pro-L-Phe
0.039 - 0.053
L-Ala-L-Ala-L-Val-L-Ala
0.223 - 0.24
L-Phe-L-Ala-L-Ala-L-Phe
0.62 - 0.75
L-Tyr-L-Val-L-Ala-L-Asp
0.15 - 0.22
MeO-succinyl-Ala-Ala-Phe 4-nitroanilide
120
N-Acetyl-Ala methyl ester
-
subtilisin BPN'
66
N-Acetyl-Leu methyl ester
-
subtilisin BPN'
91
N-Acetyl-Lys methyl ester
-
subtilisin BPN'
17
N-acetyl-Phe ethyl ester
-
subtilisin BPN'
60
N-Acetyl-Phe methyl ester
-
subtilisin Novo
24
N-Acetyl-Trp ethyl ester
-
subtilisin BPN'
50
N-Acetyl-Trp methyl ester
-
subtilisin Carlsberg
22 - 70
N-Acetyl-Tyr ethyl ester
90
N-Acetyl-Tyr methyl ester
-
subtilisin Novo, N-acetyl-Tyr ethyl ester, subtilisin Carlsberg, N-acetyl-Trp methyl ester, subtilisin Novo
3.13 - 4.28
N-methoxysuccinyl-Ala-Ala-Pro-Val-4-nitroanilide
0.15 - 0.35
N-Succ-Ala-Ala-Pro-Phe-4-nitroanilide
0.115 - 0.59
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
0.11 - 7.9
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide
0.000655
N-succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-nitroanilide
-
37°C, pH 10.5
130 - 319
sec-phenethyl alcohol
0.28 - 2.25
Suc-Ala-Ala-Ala-p-nitroanilide
4 - 17
Suc-Ala-Ala-p-nitroanilide
0.33 - 0.92
Suc-Ala-Ala-Pro-Ala-p-nitroanilide
0.68 - 3.37
Suc-Ala-Ala-Pro-Leu-p-nitroanilide
0.0027 - 0.43
Suc-Ala-Ala-Pro-Phe-4-nitroanilide
0.8 - 2
succinyl-AAPA-p-nitroanilide
1.9 - 4.4
succinyl-AAPE-p-nitroanilide
0.39 - 2.46
succinyl-AAPF-p-nitroanilide
3.4 - 8.2
succinyl-AAPR-p-nitroanilide
1.2 - 1.5
Succinyl-Ala-Ala-Ala 4-nitroanilide
0.13
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
0.07 - 1
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
0.36
succinyl-L-Ala-L-Ala-L-Phe-7-amido-4-methylcoumarin
-
mutant Y217L, pH 8.3, 25°C
0.45
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-nitroanilide
-
mutant Y217L, pH 8.3, 25°C
0.33
succinyl-L-Asp-L-Val-L-Arg-L-Ala-L-Phe-7-amido-4-methylcoumarin
-
mutant Y217L, pH 8.3, 25°C
30 - 40
toluenesulfonyl-Arg methyl ester
0.09
Urea-denatured hemoglobin
-
30°C, pH 8.0
-
0.14 - 4
Z-Ala-Ala-Leu-p-nitroanilide
additional information
additional information
-
7
benzoyl-Arg ethyl ester
-
subtilisin Novo, subtilisin Carlsberg
10
benzoyl-Arg ethyl ester
-
subtilisn BPN'
0.13
Glp-Ala-Ala-Leu-p-nitroanilide
-
in 2% DMSO
0.18
Glp-Ala-Ala-Leu-p-nitroanilide
-
in 2% DMF
0.25
Glp-Ala-Ala-Leu-p-nitroanilide
-
in 2% DMF
0.98
L-Ala-L-Ala-L-Pro-L-Ala
-
V104S/L124M/P129S/S130G/P131E/A133S/T134L/L135I, pH 9.0, 24°C
1.99
L-Ala-L-Ala-L-Pro-L-Ala
-
wild-type, pH 9.0, 24°C
1.15
L-Ala-L-Ala-L-Pro-L-Phe
-
wild-type, pH 9.0, 24°C
1.93
L-Ala-L-Ala-L-Pro-L-Phe
-
V104S/L124M/P129S/S130G/P131E/A133S/T134L/L135I, pH 9.0, 24°C
0.039
L-Ala-L-Ala-L-Val-L-Ala
-
wild-type, pH 9.0, 24°C
0.053
L-Ala-L-Ala-L-Val-L-Ala
-
V104S/L124M/P129S/S130G/P131E/A133S/T134L/L135I, pH 9.0, 24°C
0.223
L-Phe-L-Ala-L-Ala-L-Phe
-
wild-type, pH 9.0, 24°C
0.24
L-Phe-L-Ala-L-Ala-L-Phe
-
V104S/L124M/P129S/S130G/P131E/A133S/T134L/L135I, pH 9.0, 24°C
0.62
L-Tyr-L-Val-L-Ala-L-Asp
-
wild-type, pH 9.0, 24°C
0.75
L-Tyr-L-Val-L-Ala-L-Asp
-
V104S/L124M/P129S/S130G/P131E/A133S/T134L/L135I, pH 9.0, 24°C
0.15
MeO-succinyl-Ala-Ala-Phe 4-nitroanilide
-
-
0.15
MeO-succinyl-Ala-Ala-Phe 4-nitroanilide
-
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide, subtilisin BPN'
0.15
MeO-succinyl-Ala-Ala-Phe 4-nitroanilide
-
subtilisin DY
0.22
MeO-succinyl-Ala-Ala-Phe 4-nitroanilide
-
subtilisin Carlsberg
22
N-Acetyl-Tyr ethyl ester
-
subtilisin BPN'
70
N-Acetyl-Tyr ethyl ester
-
subtilisin Novo, N-acetyl-Tyr methyl ester, subtilisin Carlsberg
3.13
N-methoxysuccinyl-Ala-Ala-Pro-Val-4-nitroanilide
-
pH 8.5, 37°C
3.74
N-methoxysuccinyl-Ala-Ala-Pro-Val-4-nitroanilide
-
pH 8.5, 37°C, mutant D182G
3.84
N-methoxysuccinyl-Ala-Ala-Pro-Val-4-nitroanilide
-
pH 8.5, 37°C, wild-type
4.02
N-methoxysuccinyl-Ala-Ala-Pro-Val-4-nitroanilide
-
pH 8.5, 37°C, mutant D180G/D182G
4.28
N-methoxysuccinyl-Ala-Ala-Pro-Val-4-nitroanilide
-
pH 8.5, 37°C, mutant D180G
0.15
N-Succ-Ala-Ala-Pro-Phe-4-nitroanilide
-
pH 7.4, 37°C, mutant S101W/G169A/V192A
0.35
N-Succ-Ala-Ala-Pro-Phe-4-nitroanilide
-
pH 7.4, 37°C, wild-type
0.115
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
recombinant enzyme, 5°C, pH 8.6
0.133
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
recombinant enzyme, 25°C, pH 9.4
0.15
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
recombinant mutant T58A/L216W, pH 7.5, 30°C
0.178
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
recombinant enzyme, 25°C, pH 8.6
0.198
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
recombinant enzyme, 25°C, pH 7.4
0.2
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
recombinant mutant T58A/G165Y/L216W, pH 7.5, 30°C
0.227
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 8.0, 25°C, recombinant mutant N212G
0.227
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
recombinant enzyme, 45°C, pH 8.6
0.233
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 8.0, 25°C, recombinant wild-type enzyme
0.278
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 8.0, 25°C, recombinant mutant P210G
0.279
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 8.0, 25°C, recombinant wmutant T211G
0.29
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 8.0, 25°C, recombinant mutant P210G/T211G
0.301
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 8.0, 25°C, recombinant mutant P210G/T211G/N212G
0.325
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 8.0, 25°C, recombinant mutant P210A
0.42
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
recombinant mutant T58A/G165L/L216W, pH 7.5, 30°C
0.54
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
recombinant mutant T58A/G165I/L216W, pH 7.5, 30°C
0.59
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
recombinant wild-type enzyme, pH 7.5, 30°C
0.11
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide
-
subtilisin-like serine protease, at 20°C, in 50 mM Tris-HCl buffer, pH 7.5
0.41
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide
-
subtilisin-like serine protease, at 80°C, in 50 mM Tris-HCl buffer, pH 7.5
2.4
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide
-
subtilisin, at 20°C, in 50 mM Tris-HCl buffer, pH 8.0
7.9
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide
-
subtilisin, at 80°C, in 50 mM Tris-HCl buffer, pH 8.0
130
sec-phenethyl alcohol
-
after incubation in 1,4-dioxane, co-lyophilization with methyl-beta-cyclodextrin
319
sec-phenethyl alcohol
-
after a 4-day incubation period in 1,4-dioxane, co-lyophilization with methyl-beta-cyclodextrin
0.28
Suc-Ala-Ala-Ala-p-nitroanilide
-
pH 7.5, 5°C
0.32
Suc-Ala-Ala-Ala-p-nitroanilide
-
pH 7.5, 20°C
0.58
Suc-Ala-Ala-Ala-p-nitroanilide
-
pH 7.5, 20°C, DTT
0.63
Suc-Ala-Ala-Ala-p-nitroanilide
-
pH 7.5, 40°C
2.25
Suc-Ala-Ala-Ala-p-nitroanilide
-
pH 7.5, 75°C
4
Suc-Ala-Ala-p-nitroanilide
-
pH 7.5, 20°C
6.67
Suc-Ala-Ala-p-nitroanilide
-
pH 7.5, 20°C, DTT
17
Suc-Ala-Ala-p-nitroanilide
-
pH 7.5, 40°C
0.33
Suc-Ala-Ala-Pro-Ala-p-nitroanilide
-
pH 7.5, 5°C or 40°C
0.92
Suc-Ala-Ala-Pro-Ala-p-nitroanilide
-
pH 7.5, 75°C
0.68
Suc-Ala-Ala-Pro-Leu-p-nitroanilide
-
pH 7.5, 5°C
1.01
Suc-Ala-Ala-Pro-Leu-p-nitroanilide
-
pH 7.5, 40°C
3.37
Suc-Ala-Ala-Pro-Leu-p-nitroanilide
-
pH 7.5, 75°C
0.0027
Suc-Ala-Ala-Pro-Phe-4-nitroanilide
-
1 mol lactose bound per 1 mol subtilisin, in 10 mM potassium phosphate buffer, pH 7.8, at 25°C
0.0036
Suc-Ala-Ala-Pro-Phe-4-nitroanilide
-
2.2 mol lactose bound per 1 mol subtilisin, in 10 mM potassium phosphate buffer, pH 7.8, at 25°C
0.0037
Suc-Ala-Ala-Pro-Phe-4-nitroanilide
-
3.5 mol lactose bound per 1 mol subtilisin, in 10 mM potassium phosphate buffer, pH 7.8, at 25°C
0.0037
Suc-Ala-Ala-Pro-Phe-4-nitroanilide
-
subtilisin without bound lactose, in 10 mM potassium phosphate buffer, pH 7.8, at 25°C
0.43
Suc-Ala-Ala-Pro-Phe-4-nitroanilide
-
recombinant enzyme, pH 8.5, 22°C
0.8
succinyl-AAPA-p-nitroanilide
-
pH 8.6, 25°C mutant S166C-S-c
1.74
succinyl-AAPA-p-nitroanilide
-
pH 8.6, 25°C mutant S166C-S-g
1.9
succinyl-AAPA-p-nitroanilide
-
pH 8.6, 25°C mutant S166C-S-e and S166S-f
2
succinyl-AAPA-p-nitroanilide
-
pH 8.6, 25°C wild-type
1.9
succinyl-AAPE-p-nitroanilide
-
pH 8.6, 25°C mutant S166C-S-a
4.4
succinyl-AAPE-p-nitroanilide
-
pH 8.6, 25°C wild-type
0.39
succinyl-AAPF-p-nitroanilide
-
pH 7.5, 25°C mutant S166C-S-a
0.51
succinyl-AAPF-p-nitroanilide
-
pH 7.5, 25°C mutant S166C
0.54
succinyl-AAPF-p-nitroanilide
-
pH 7.5, 25°C mutant S156C-S-d
0.55
succinyl-AAPF-p-nitroanilide
-
pH 7.5, 25°C, wild-type and mutant M222C-S-e
0.6
succinyl-AAPF-p-nitroanilide
-
pH 7.5, 25°C mutant S156C-S-c and S166C-S-f
0.61
succinyl-AAPF-p-nitroanilide
-
pH 7.5, 25°C mutant M222C-S-f
0.63
succinyl-AAPF-p-nitroanilide
-
pH 7.5, 25°C mutant M222C-S-b
0.65
succinyl-AAPF-p-nitroanilide
-
pH 7.5, 25°C mutant S156C
0.67
succinyl-AAPF-p-nitroanilide
-
pH 7.5, 25°C mutant M222C-S-d
0.68
succinyl-AAPF-p-nitroanilide
-
pH 7.5, 25°C mutant S156C-S-b and M222-S-a
0.68
succinyl-AAPF-p-nitroanilide
-
pH 8.6, 25°C, mutant S166C-a
0.69
succinyl-AAPF-p-nitroanilide
-
pH 7.5, 25°C mutant M222C-S-c
0.7
succinyl-AAPF-p-nitroanilide
-
pH 7.5, 25°C mutant S166C-S-e
0.7
succinyl-AAPF-p-nitroanilide
-
pH 8.6, 25°C, mutant S166C-f
0.72
succinyl-AAPF-p-nitroanilide
-
pH 7.5, 25°C mutant S166C-S-c
0.73
succinyl-AAPF-p-nitroanilide
-
pH 8.6, 25°C wild-type
0.74
succinyl-AAPF-p-nitroanilide
-
pH 7.5, 25°C mutant S166C-S-d
0.74
succinyl-AAPF-p-nitroanilide
-
pH 8.6, 25°C, mutant S166C-g
0.77
succinyl-AAPF-p-nitroanilide
-
pH 7.5, 25°C mutant M222C
0.78
succinyl-AAPF-p-nitroanilide
-
pH 7.5, 25°C mutant S156C-S-e
0.79
succinyl-AAPF-p-nitroanilide
-
pH 7.5, 25°C mutant S156C-S-a
0.86
succinyl-AAPF-p-nitroanilide
-
pH 7.5, 25°C mutant S156C-S-f
0.92
succinyl-AAPF-p-nitroanilide
-
pH 7.5, 25°C mutant S166C-S-b
1.09
succinyl-AAPF-p-nitroanilide
-
pH 8.6, 25°C mutant S166C-S-e
1.17
succinyl-AAPF-p-nitroanilide
-
pH 8.6, 25°C mutant S166C-S-c
1.34
succinyl-AAPF-p-nitroanilide
-
pH 8.6, 25°C mutant S166C-S-b
1.5 - 2
succinyl-AAPF-p-nitroanilide
-
pH 8.6, 25°C mutant S166C-S-h
1.6
succinyl-AAPF-p-nitroanilide
-
pH 8.6, 25°C mutant S166C-S-d
2.26
succinyl-AAPF-p-nitroanilide
-
pH 8.6, 25°C mutant S166C-S-i
2.46
succinyl-AAPF-p-nitroanilide
-
pH 8.6, 25°C mutant S166C-S-j
3.4
succinyl-AAPR-p-nitroanilide
-
pH 8.6, 25°C mutant S166C-S-b
5.2
succinyl-AAPR-p-nitroanilide
-
pH 8.6, 25°C mutant S166C-S-j
5.3
succinyl-AAPR-p-nitroanilide
-
pH 8.6, 25°C mutant S166C-S-i
5.5
succinyl-AAPR-p-nitroanilide
-
pH 8.6, 25°C mutant S166C-S-d
7.2
succinyl-AAPR-p-nitroanilide
-
pH 8.6, 25°C wild-type
8.2
succinyl-AAPR-p-nitroanilide
-
pH 8.6, 25°C mutant S166C-S-h
1.2
Succinyl-Ala-Ala-Ala 4-nitroanilide
-
subtilisin Carlsberg
1.5
Succinyl-Ala-Ala-Ala 4-nitroanilide
-
subtilisin DY
0.13
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
-
-
0.13
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
-
succinyl-Leu-Leu-Val-Tyr-4-methylcoumaryl 7-amide, subtilisin Sendai
0.13
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
-
mutant subtilisin BPN' Asp to Ser99
0.07
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
pH 7.5, 5°C
0.15
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
pH 7.5, 20°C
0.3
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
pH 7.5, 40°C
0.44
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
pH 7.5, 20°C, DTT
0.71
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
subtilisin DY
0.79
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
subtilisin Carlsberg
1
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
pH 7.5, 75°C
30
toluenesulfonyl-Arg methyl ester
-
subtilisin Novo, N-acetyl-Phe methyl ester, subtilisin Carlsberg
40
toluenesulfonyl-Arg methyl ester
-
subtilisin Carlsberg
0.14
Z-Ala-Ala-Leu-p-nitroanilide
-
in 20% DMSO
0.19
Z-Ala-Ala-Leu-p-nitroanilide
-
in 20% DMF
0.25
Z-Ala-Ala-Leu-p-nitroanilide
-
in 20% DMSO
4
Z-Ala-Ala-Leu-p-nitroanilide
-
in 20% DMF
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
Km of subtilisin Novo chemically attached to soluble DEAE-dextran and insoluble DEAE-Sephadex
-
additional information
additional information
-
the temperature dependence of the kinetics and thermodynamic parameters suggest that the enzyme exists in two, i.e. cold and hot forms, at 22°C the cold form turns into the hot one possibly owing to a conformational change
-
additional information
additional information
kinetic analysis of the perhydrolytic wild-type and mutant enzyme activities, overview
-
additional information
additional information
-
Michaelis-Menten kinetics using Lineweaver-Burk and Hanes plots at pH 8.5 and 22°C, purified recombinant enzyme
-
additional information
additional information
Michaelis-Menten kinetics and thermodynamics
-
additional information
additional information
-
Michaelis-Menten kinetics using Lineweaver-Burk and Hanes plots
-
additional information
additional information
Michaelis-Menten kinetics, Km is 0.175% w/v
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.022
acetyl-L-Phe
-
30°C, pH 8.0
0.38
acetyl-L-Phe ethyl ester
-
30°C, pH 8.0
0.1
acetyl-L-Tyr
-
30°C, pH 8.0
0.04
acetyl-L-Tyr ethyl ester
-
30°C, pH 8.0
1900 - 2500
benzyloxycarbonyl-Gly-4-nitroanilide
-
16550
benzyloxycarbonyl-L-Ala-L-Ala-L-Leu-4-nitroanilide
-
-
5.186
casein
recombinant enzyme, pH 8.0, 60°C
64.3 - 80
Glp-Ala-Ala-Leu-p-nitroanilide
35.5
Hammarsten casein
-
37°C, pH 10.5
-
31 - 47
L-Ala-L-Ala-L-Pro-L-Ala
185 - 403
L-Ala-L-Ala-L-Pro-L-Phe
10 - 12
L-Ala-L-Ala-L-Val-L-Ala
90 - 189
L-Phe-L-Ala-L-Ala-L-Phe
4 - 10
L-Tyr-L-Val-L-Ala-L-Asp
47 - 97
MeO-succinyl-Ala-Ala-Phe 4-nitroanilide
0.0064 - 0.0089
N-methoxysuccinyl-Ala-Ala-Pro-Val-4-nitroanilide
231.3 - 586.2
N-Succ-Ala-Ala-Pro-Phe-4-nitroanilide
1.7 - 759
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
1.6 - 440
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide
70.2
N-succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-nitroanilide
-
37°C, pH 10.5
222 - 97000
Suc-Ala-Ala-Ala-p-nitroanilide
93 - 3700
Suc-Ala-Ala-p-nitroanilide
222 - 130000
Suc-Ala-Ala-Pro-Ala-p-nitroanilide
389 - 97000
Suc-Ala-Ala-Pro-Leu-p-nitroanilide
90 - 200
Suc-Ala-Ala-Pro-Phe-4-nitroanilide
0.052 - 28.2
succinyl-AAPA-p-nitroanilide
1.75 - 14.5
succinyl-AAPE-p-nitroanilide
0.017 - 153
succinyl-AAPF-p-nitroanilide
0.16 - 6.08
succinyl-AAPR-p-nitroanilide
1.6 - 1.8
Succinyl-Ala-Ala-Ala 4-nitroanilide
52
succinyl-Ala-Ala-Phe-4-nitroanilide
-
subtilisin DY
45 - 57
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
148 - 130000
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
6.4
succinyl-L-Ala-L-Ala-L-Phe-7-amido-4-methylcoumarin
-
mutant Y217L, pH 8.3, 25°C
15 - 141
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-methyl-coumaryl-7-amide
210
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-nitroanilide
-
mutant Y217L, pH 8.3, 25°C
68
succinyl-L-Asp-L-Val-L-Arg-L-Ala-L-Phe-7-amido-4-methylcoumarin
-
mutant Y217L, pH 8.3, 25°C
29
succinyl-Leu-Leu-Val-Tyr-4-methylcoumaryl 7-amide
-
subtilisin Sendai
0.04
Urea-denatured hemoglobin
-
30°C, pH 8.0
-
70.9 - 104
Z-Ala-Ala-Leu-p-nitroanilide
additional information
additional information
-
1900
benzyloxycarbonyl-Gly-4-nitroanilide
-
pH 7.5, 20°C
-
2500
benzyloxycarbonyl-Gly-4-nitroanilide
-
pH 7.5, 20°C, DTT
-
64.3
Glp-Ala-Ala-Leu-p-nitroanilide
-
in 2% DMF
69
Glp-Ala-Ala-Leu-p-nitroanilide
-
in 2% DMF
80
Glp-Ala-Ala-Leu-p-nitroanilide
-
in 2% DMSO
31
L-Ala-L-Ala-L-Pro-L-Ala
-
V104S/L124M/P129S/S130G/P131E/A133S/T134L/L135I, pH 9.0, 24°C
47
L-Ala-L-Ala-L-Pro-L-Ala
-
wild-type, pH 9.0, 24°C
185
L-Ala-L-Ala-L-Pro-L-Phe
-
wild-type, pH 9.0, 24°C
403
L-Ala-L-Ala-L-Pro-L-Phe
-
V104S/L124M/P129S/S130G/P131E/A133S/T134L/L135I, pH 9.0, 24°C
10
L-Ala-L-Ala-L-Val-L-Ala
-
V104S/L124M/P129S/S130G/P131E/A133S/T134L/L135I, pH 9.0, 24°C
12
L-Ala-L-Ala-L-Val-L-Ala
-
wild-type, pH 9.0, 24°C
90
L-Phe-L-Ala-L-Ala-L-Phe
-
wild-type, pH 9.0, 24°C
189
L-Phe-L-Ala-L-Ala-L-Phe
-
V104S/L124M/P129S/S130G/P131E/A133S/T134L/L135I, pH 9.0, 24°C
4
L-Tyr-L-Val-L-Ala-L-Asp
-
V104S/L124M/P129S/S130G/P131E/A133S/T134L/L135I, pH 9.0, 24°C
10
L-Tyr-L-Val-L-Ala-L-Asp
-
wild-type, pH 9.0, 24°C
47
MeO-succinyl-Ala-Ala-Phe 4-nitroanilide
-
subtilisin DY
57
MeO-succinyl-Ala-Ala-Phe 4-nitroanilide
-
subtilisin Carlsberg
57
MeO-succinyl-Ala-Ala-Phe 4-nitroanilide
-
subtilisin Carlsberg
97
MeO-succinyl-Ala-Ala-Phe 4-nitroanilide
-
subtilisin
0.0064
N-methoxysuccinyl-Ala-Ala-Pro-Val-4-nitroanilide
-
pH 8.5, 37°C
0.0074
N-methoxysuccinyl-Ala-Ala-Pro-Val-4-nitroanilide
-
pH 8.5, 37°C, mutant D180G
0.0079
N-methoxysuccinyl-Ala-Ala-Pro-Val-4-nitroanilide
-
pH 8.5, 37°C, mutant D182G
0.0089
N-methoxysuccinyl-Ala-Ala-Pro-Val-4-nitroanilide
-
pH 8.5, 37°C
0.0089
N-methoxysuccinyl-Ala-Ala-Pro-Val-4-nitroanilide
-
pH 8.5, 37°C, mutant D180G/D182G
231.3
N-Succ-Ala-Ala-Pro-Phe-4-nitroanilide
-
pH 7.4, 37°C, wild-type
586.2
N-Succ-Ala-Ala-Pro-Phe-4-nitroanilide
-
pH 7.4, 37°C, mutant S101W/G169A/V192A
1.7
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
recombinant mutant T58A/G165I/L216W, pH 7.5, 30°C
15.1
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
recombinant mutant T58A/G165L/L216W, pH 7.5, 30°C
22.8
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
recombinant mutant T58A/G165Y/L216W, pH 7.5, 30°C
33.1
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
recombinant mutant T58A/L216W, pH 7.5, 30°C
40.8
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
recombinant enzyme, 5°C, pH 8.6
172.6
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
recombinant wild-type enzyme, pH 7.5, 30°C
193.1
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
recombinant enzyme, 25°C, pH 7.4
225.7
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
recombinant enzyme, 25°C, pH 8.6
248.7
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
recombinant enzyme, 25°C, pH 9.4
419
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 8.0, 25°C, recombinant wild-type enzyme
462
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 8.0, 25°C, recombinant wmutant T211G
475
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 8.0, 25°C, recombinant mutant N212G
552.3
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
recombinant enzyme, 45°C, pH 8.6
638
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 8.0, 25°C, recombinant mutant P210G
697
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 8.0, 25°C, recombinant mutant P210G/T211G
715
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 8.0, 25°C, recombinant mutant P210A
759
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 8.0, 25°C, recombinant mutant P210G/T211G/N212G
1.6
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide
-
subtilisin-like serine protease, at 20°C, in 50 mM Tris-HCl buffer, pH 7.5
14
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide
-
subtilisin, at 20°C, in 50 mM Tris-HCl buffer, pH 8.0
25
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide
-
subtilisin-like serine protease, at 80°C, in 50 mM Tris-HCl buffer, pH 7.5
440
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide
-
subtilisin, at 80°C, in 50 mM Tris-HCl buffer, pH 8.0
222
Suc-Ala-Ala-Ala-p-nitroanilide
-
pH 7.5, 5°C
750
Suc-Ala-Ala-Ala-p-nitroanilide
-
pH 7.5, 20°C, DTT
1200
Suc-Ala-Ala-Ala-p-nitroanilide
-
pH 7.5, 20°C
22000
Suc-Ala-Ala-Ala-p-nitroanilide
-
pH 7.5, 40°C
97000
Suc-Ala-Ala-Ala-p-nitroanilide
-
pH 7.5, 75°C
93
Suc-Ala-Ala-p-nitroanilide
-
pH 7.5, 20°C, in presence and absence of DTT
3700
Suc-Ala-Ala-p-nitroanilide
-
pH 7.5, 40°C
222
Suc-Ala-Ala-Pro-Ala-p-nitroanilide
-
pH 7.5, 5°C
8800
Suc-Ala-Ala-Pro-Ala-p-nitroanilide
-
pH 7.5, 40°C
130000
Suc-Ala-Ala-Pro-Ala-p-nitroanilide
-
pH 7.5, 75°C
389
Suc-Ala-Ala-Pro-Leu-p-nitroanilide
-
pH 7.5, 5°C
97000
Suc-Ala-Ala-Pro-Leu-p-nitroanilide
-
pH 7.5, 40°C
90
Suc-Ala-Ala-Pro-Phe-4-nitroanilide
-
3.5 mol lactose bound per 1 mol subtilisin, in 10 mM potassium phosphate buffer, pH 7.8, at 25°C
132
Suc-Ala-Ala-Pro-Phe-4-nitroanilide
-
2.2 mol lactose bound per 1 mol subtilisin, in 10 mM potassium phosphate buffer, pH 7.8, at 25°C
137
Suc-Ala-Ala-Pro-Phe-4-nitroanilide
-
recombinant enzyme, pH 8.5, 22°C
166
Suc-Ala-Ala-Pro-Phe-4-nitroanilide
-
1 mol lactose bound per 1 mol subtilisin, in 10 mM potassium phosphate buffer, pH 7.8, at 25°C
200
Suc-Ala-Ala-Pro-Phe-4-nitroanilide
-
subtilisin without bound lactose, in 10 mM potassium phosphate buffer, pH 7.8, at 25°C
0.052 - 2.1
succinyl-AAPA-p-nitroanilide
-
pH 8.6, 25°C mutant S166C-S-g
6.8
succinyl-AAPA-p-nitroanilide
-
pH 8.6, 25°C mutant S166C-S-c and S166C-S-e
9.65
succinyl-AAPA-p-nitroanilide
-
pH 8.6, 25°C mutant S166C-S-g
17.7
succinyl-AAPA-p-nitroanilide
-
pH 8.6, 25°C wild-type
28.2
succinyl-AAPA-p-nitroanilide
-
pH 8.6, 25°C mutant S166C-S-f
1.75
succinyl-AAPE-p-nitroanilide
-
pH 8.6, 25°C wild-type
14.5
succinyl-AAPE-p-nitroanilide
-
pH 8.6, 25°C mutant S166C-S-a
0.017
succinyl-AAPF-p-nitroanilide
-
pH 7.5, 25°C mutant M222C-S-a
0.49
succinyl-AAPF-p-nitroanilide
-
pH 7.5, 25°C mutant M222C-S-c
0.833
succinyl-AAPF-p-nitroanilide
-
pH 7.5, 25°C mutant S166C-S-f
1.04
succinyl-AAPF-p-nitroanilide
-
pH 7.5, 25°C mutant M222C-S-f
1.64
succinyl-AAPF-p-nitroanilide
-
pH 7.5, 25°C mutant M222C-S-e
2.94
succinyl-AAPF-p-nitroanilide
-
pH 7.5, 25°C mutant M222C-S-e
3.7
succinyl-AAPF-p-nitroanilide
-
pH 7.5, 25°C mutant S156C-S-e
3.8
succinyl-AAPF-p-nitroanilide
-
pH 7.5, 25°C mutant S166C-S-e
4.8
succinyl-AAPF-p-nitroanilide
-
pH 8.6, 25°C mutant S166C-S-f
6.08
succinyl-AAPF-p-nitroanilide
-
pH 7.5, 25°C mutant M222C-S-f
6.9
succinyl-AAPF-p-nitroanilide
-
pH 7.5, 25°C mutant S166C-S-d and M222C-S-d
7.2
succinyl-AAPF-p-nitroanilide
-
pH 7.5, 25°C mutant M222C-S-b
11.8
succinyl-AAPF-p-nitroanilide
-
pH 7.5, 25°C mutant S166C-S-b
14.2
succinyl-AAPF-p-nitroanilide
-
pH 7.5, 25°C mutant S166C
16.3
succinyl-AAPF-p-nitroanilide
-
pH 7.5, 25°C mutant S166C-S-f
16.9
succinyl-AAPF-p-nitroanilide
-
pH 8.6, 25°C mutant S166C-S-c
17.3
succinyl-AAPF-p-nitroanilide
-
pH 7.5, 25°C mutant M222C
17.4
succinyl-AAPF-p-nitroanilide
-
pH 7.5, 25°C mutant S166C-S-a
18
succinyl-AAPF-p-nitroanilide
-
pH 7.5, 25°C mutant S156C-S-c
21.8
succinyl-AAPF-p-nitroanilide
-
pH 7.5, 25°C mutant S156C-S-d
23.1
succinyl-AAPF-p-nitroanilide
-
pH 8.6, 25°C mutant S166C-S-c
23.4
succinyl-AAPF-p-nitroanilide
-
pH 7.5, 25°C mutant S156C-S-b
24.2
succinyl-AAPF-p-nitroanilide
-
pH 7.5, 25°C mutant S156C-S-c
25
succinyl-AAPF-p-nitroanilide
-
pH 8.6, 25°C mutant S166C-S-b
29
succinyl-AAPF-p-nitroanilide
-
pH 8.6, 25°C mutant S166C-S-g
30
succinyl-AAPF-p-nitroanilide
-
pH 7.5, 25°C mutant S156C-S-a
31
succinyl-AAPF-p-nitroanilide
-
pH 7.5, 25°C mutant S166C-S-c
31.6
succinyl-AAPF-p-nitroanilide
-
pH 7.5, 25°C mutant S156C-S-e
33.3
succinyl-AAPF-p-nitroanilide
-
pH 7.5, 25°C mutant M222C-S-a
39
succinyl-AAPF-p-nitroanilide
-
pH 7.5, 25°C mutant S156C-S-f
43
succinyl-AAPF-p-nitroanilide
-
pH 7.5, 25°C mutant S156C
47
succinyl-AAPF-p-nitroanilide
-
pH 8.6, 25°C mutant S166C-S-d
48
succinyl-AAPF-p-nitroanilide
-
pH 7.5, 25°C, wild-type
48
succinyl-AAPF-p-nitroanilide
-
pH 8.6, 25°C, mutant S166C-h
50
succinyl-AAPF-p-nitroanilide
-
pH 8.6, 25°C mutant S166C-S-a
67
succinyl-AAPF-p-nitroanilide
-
pH 8.6, 25°C mutant S166C-S-i
76
succinyl-AAPF-p-nitroanilide
-
pH 8.6, 25°C mutant S166C-S-j
82
succinyl-AAPF-p-nitroanilide
-
pH 8.6, 25°C mutant S166C-S-e
153
succinyl-AAPF-p-nitroanilide
-
pH 8.6, 25°C wild-type
0.16
succinyl-AAPR-p-nitroanilide
-
pH 8.6, 25°C wild-type
0.17
succinyl-AAPR-p-nitroanilide
-
pH 8.6, 25°C mutant S166C-S-b
0.35
succinyl-AAPR-p-nitroanilide
-
pH 8.6, 25°C mutant S166C-S-h
0.43
succinyl-AAPR-p-nitroanilide
-
pH 8.6, 25°C mutant S166C-S-i
0.68
succinyl-AAPR-p-nitroanilide
-
pH 8.6, 25°C mutant S166C-S-d
1.06
succinyl-AAPR-p-nitroanilide
-
pH 8.6, 25°C mutant S166C-S-j
6.08
succinyl-AAPR-p-nitroanilide
-
pH 8.6, 25°C mutant S166C-S-d
6.08
succinyl-AAPR-p-nitroanilide
-
pH 8.6, 25°C mutant S166C-S-j
1.6
Succinyl-Ala-Ala-Ala 4-nitroanilide
-
subtilisin Carlsberg
1.8
Succinyl-Ala-Ala-Ala 4-nitroanilide
-
subtilisin DY
45
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
-
mutant subtilisin BPN' Asp99Ser
57
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
-
subtilisin BPN'
57
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
-
subtilisin BPN'
148
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
pH 7.5, 5°C
2900
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
pH 7.5, 20°C, DTT
10000
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
pH 7.5, 20°C
130000
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
pH 7.5, 40°C
15
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-methyl-coumaryl-7-amide
pH 8.5, 37°C, recombinant wild-type enzyme, in presence of 2 M GdmCl
34
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-methyl-coumaryl-7-amide
pH 8.5, 37°C, recombinant mutant S62I/A153V/G166S/I205V, in presence of 2 M GdmCl
35
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-methyl-coumaryl-7-amide
pH 8.5, 37°C, recombinant wild-type enzyme, in presence of SDS
42
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-methyl-coumaryl-7-amide
pH 8.5, 37°C, recombinant mutant S62I/A153V/G166S/I205V, in absence of GdmCl or SDS
45
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-methyl-coumaryl-7-amide
pH 8.5, 37°C, recombinant mutant S62I/A153V/G166S/I205V, in presence of SDS
50
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-methyl-coumaryl-7-amide
pH 8.5, 37°C, recombinant wild-type enzyme, in absence of GdmCl or SDS
62
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-methyl-coumaryl-7-amide
pH 8.5, 37°C, recombinant mutant G166M, in presence of 2 M GdmCl
65
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-methyl-coumaryl-7-amide
pH 8.5, 37°C, recombinant mutant S62I, in presence of SDS
70
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-methyl-coumaryl-7-amide
pH 8.5, 37°C, recombinant mutant S62I/G166M, in presence of 2 M GdmCl
81
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-methyl-coumaryl-7-amide
pH 8.5, 37°C, recombinant mutant S62I/G166M, in presence of SDS
102
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-methyl-coumaryl-7-amide
pH 8.5, 37°C, recombinant mutant S62I, in absence of GdmCl or SDS
104
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-methyl-coumaryl-7-amide
pH 8.5, 37°C, recombinant mutant G166M, in presence of SDS
123
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-methyl-coumaryl-7-amide
pH 8.5, 37°C, recombinant mutant S62I/G166M, in absence of GdmCl or SDS
141
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-methyl-coumaryl-7-amide
pH 8.5, 37°C, recombinant mutant G166M, in absence of GdmCl or SDS
70.9
Z-Ala-Ala-Leu-p-nitroanilide
-
in 20% DMF
77
Z-Ala-Ala-Leu-p-nitroanilide
-
in 20% DMSO
100
Z-Ala-Ala-Leu-p-nitroanilide
-
in 20% DMSO
104
Z-Ala-Ala-Leu-p-nitroanilide
-
in 20% DMF
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
turnover number of subtilisin Novo chemically attached to soluble DEAE-dextran and insoluble DEAE-Sephadex
-
additional information
additional information
-
increasing the level of glycosylation causes a linearly dependent reduction in structural dynamics, which leads to a decrease in the catalytic turnover rate for both, the enzyme acylation and deacylation steps
-
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0.00274
2,2'-[[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphoryl]bis(oxybenzene-4,1-diyl)]diacetic acid
-
in 50 mM Tris, 1M NaCl, pH 7.5 containing 0.01% Triton X-100
0.02
2,2'-[[(1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphoryl]bis(oxybenzene-4,1-diyl)]diacetic acid
-
in 50 mM Tris, 1M NaCl, pH 7.5 containing 0.01% Triton X-100
0.00135
2,2'-[[(1-[[1-(tert-butoxycarbonyl)-L-prolyl]amino]-3-methylbutyl)phosphoryl]bis(oxybenzene-3,1-diyl)]diacetic acid
-
in 50 mM Tris, 1M NaCl, pH 7.5 containing 0.01% Triton X-100
0.02
bis(2,3,5-trimethylphenyl) (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
-
in 50 mM Tris, 1M NaCl, pH 7.5 containing 0.01% Triton X-100
0.02
bis(2,3-dimethylphenyl) (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
-
in 50 mM Tris, 1M NaCl, pH 7.5 containing 0.01% Triton X-100
0.02
bis(2,3-dimethylphenyl) (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
-
in 50 mM Tris, 1M NaCl, pH 7.5 containing 0.01% Triton X-100
0.02
bis(2,5-dimethylphenyl) (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
-
in 50 mM Tris, 1M NaCl, pH 7.5 containing 0.01% Triton X-100
0.02
bis(2-methylphenyl) (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
-
in 50 mM Tris, 1M NaCl, pH 7.5 containing 0.01% Triton X-100
0.02
bis(2-methylphenyl) (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
-
in 50 mM Tris, 1M NaCl, pH 7.5 containing 0.01% Triton X-100
0.02
bis(3,4,5-trimethylphenyl) (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
-
in 50 mM Tris, 1M NaCl, pH 7.5 containing 0.01% Triton X-100
0.02
bis(3,4,5-trimethylphenyl) (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
-
in 50 mM Tris, 1M NaCl, pH 7.5 containing 0.01% Triton X-100
0.02
bis(3,4-dimethylphenyl) (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
-
in 50 mM Tris, 1M NaCl, pH 7.5 containing 0.01% Triton X-100
0.02
bis(3,4-dimethylphenyl) (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
-
in 50 mM Tris, 1M NaCl, pH 7.5 containing 0.01% Triton X-100
0.02
bis(3-chlorophenyl) (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
-
in 50 mM Tris, 1M NaCl, pH 7.5 containing 0.01% Triton X-100
0.02
bis(3-chlorophenyl) (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
-
in 50 mM Tris, 1M NaCl, pH 7.5 containing 0.01% Triton X-100
0.02
bis(3-methoxyphenyl) (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
-
in 50 mM Tris, 1M NaCl, pH 7.5 containing 0.01% Triton X-100
0.02
bis(4-chlorophenyl) (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
-
in 50 mM Tris, 1M NaCl, pH 7.5 containing 0.01% Triton X-100
0.02
bis(4-chlorophenyl) (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
-
in 50 mM Tris, 1M NaCl, pH 7.5 containing 0.01% Triton X-100
0.02
bis(4-ethylphenyl) (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
-
in 50 mM Tris, 1M NaCl, pH 7.5 containing 0.01% Triton X-100
0.02
bis(4-ethylphenyl) (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
-
in 50 mM Tris, 1M NaCl, pH 7.5 containing 0.01% Triton X-100
0.02
bis(4-methoxyphenyl) (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
-
in 50 mM Tris, 1M NaCl, pH 7.5 containing 0.01% Triton X-100
0.02
bis(4-methylphenyl) (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
-
in 50 mM Tris, 1M NaCl, pH 7.5 containing 0.01% Triton X-100
0.02
bis(4-tert-butylphenyl) (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
-
in 50 mM Tris, 1M NaCl, pH 7.5 containing 0.01% Triton X-100
0.00792
bis(4-tert-butylphenyl) (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
-
in 50 mM Tris, 1M NaCl, pH 7.5 containing 0.01% Triton X-100
0.000076
bis[4-(methylsulfonyl)phenyl] (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
-
in 50 mM Tris, 1M NaCl, pH 7.5 containing 0.01% Triton X-100
0.02
bis[4-(propan-2-yl)phenyl] (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
-
in 50 mM Tris, 1M NaCl, pH 7.5 containing 0.01% Triton X-100
0.02
bis[4-(propan-2-yl)phenyl] (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
-
in 50 mM Tris, 1M NaCl, pH 7.5 containing 0.01% Triton X-100
0.00213
bis[4-(sulfanylmethyl)phenyl] (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
-
in 50 mM Tris, 1M NaCl, pH 7.5 containing 0.01% Triton X-100
0.02
bis[4-(sulfanylmethyl)phenyl] (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
-
in 50 mM Tris, 1M NaCl, pH 7.5 containing 0.01% Triton X-100
0.000000003
chymotrypsin inhibitor
-
-
-
0.000000017
chymotrypsin inhibitor 2 mutant M59A, chymotrypsin inhibitor 2 mutant M59F
-
-
-
0.00000013
chymotrypsin inhibitor 2 mutant M59G
-
-
-
0.000000019
chymotrypsin inhibitor 2 mutant M59K
-
-
-
0.0000000033
chymotrypsin inhibitor 2 mutant M59Y
-
-
-
0.00000046
chymotrypsin inhibitor 2 mutant Y61A
-
-
-
0.00637
diphenyl (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
-
in 50 mM Tris, 1M NaCl, pH 7.5 containing 0.01% Triton X-100
0.02
diphenyl (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
-
in 50 mM Tris, 1M NaCl, pH 7.5 containing 0.01% Triton X-100
0.0000043
EPI1a
-
predicted by use of Laskowski algorithm
-
50
EPI1b
-
predicted by use of Laskowski algorithm
-
0.0000000339 - 0.00000468
fungal protease inhibitor F
-
0.000049
human LEKTI
-
pH 7.4, 25°C
-
0.0000000036
human proteinase inhibitor 9
-
pH 7.5, 25°C
-
0.000093
N-(tert-butoxycarbonyl)-L-valyl-N-(1-[bis[4-(sulfanylmethyl)phenoxy]phosphoryl]-2-phenylethyl)-L-prolinamide
-
in 50 mM Tris, 1M NaCl, pH 7.5 containing 0.01% Triton X-100
0.00023
N-(tert-butoxycarbonyl)-L-valyl-N-[1-(diphenoxyphosphoryl)-2-phenylethyl]-L-prolinamide
-
in 50 mM Tris, 1M NaCl, pH 7.5 containing 0.01% Triton X-100
0.02
N-(tert-butoxycarbonyl)-L-valyl-N-[1-[bis(3,4,5-trimethylphenoxy)phosphoryl]-3-methylbutyl]-L-prolinamide
-
in 50 mM Tris, 1M NaCl, pH 7.5 containing 0.01% Triton X-100
0.00006
N-(tert-butoxycarbonyl)-L-valyl-N-[1-[bis(4-methoxyphenoxy)phosphoryl]-3-methylbutyl]-L-prolinamide
-
in 50 mM Tris, 1M NaCl, pH 7.5 containing 0.01% Triton X-100
0.02
N-(tert-butoxycarbonyl)-L-valyl-N-[1-[bis(4-tert-butylphenoxy)phosphoryl]-3-methylbutyl]-L-prolinamide
-
in 50 mM Tris, 1M NaCl, pH 7.5 containing 0.01% Triton X-100
0.001
N1-18[ISP]
synthetic peptide corresponding to the N-terminal extension behaves as a mixed noncompetitive inhibitor of active ISP, pH and temperature not specified in the publication
0.0025
RNA aptamer
-
pH 7.8, 37°C
-
0.00206
Suc-Val-Pro-PheP(OPh)2
-
in 50 mM Tris, 1M NaCl, pH 7.5 containing 0.01% Triton X-100
0.02
tert-butyl (2S)-2-([1-[bis(2-methylphenoxy)phosphoryl]-3-methylbutyl]carbamoyl)pyrrolidine-1-carboxylate
-
in 50 mM Tris, 1M NaCl, pH 7.5 containing 0.01% Triton X-100
0.02
tert-butyl (2S)-2-([1-[bis(3,4,5-trimethylphenoxy)phosphoryl]-3-methylbutyl]carbamoyl)pyrrolidine-1-carboxylate
-
in 50 mM Tris, 1M NaCl, pH 7.5 containing 0.01% Triton X-100
0.036
tert-butyl (2S)-2-([1-[bis(3,4-dimethylphenoxy)phosphoryl]-3-methylbutyl]carbamoyl)pyrrolidine-1-carboxylate
-
in 50 mM Tris, 1M NaCl, pH 7.5 containing 0.01% Triton X-100
0.00705
tert-butyl (2S)-2-([1-[bis(4-methoxyphenoxy)phosphoryl]-3-methylbutyl]carbamoyl)pyrrolidine-1-carboxylate
-
in 50 mM Tris, 1M NaCl, pH 7.5 containing 0.01% Triton X-100
0.00228
tert-butyl (2S)-2-([1-[bis(4-methylphenoxy)phosphoryl]-3-methylbutyl]carbamoyl)pyrrolidine-1-carboxylate
-
in 50 mM Tris, 1M NaCl, pH 7.5 containing 0.01% Triton X-100
0.0053
tert-butyl (2S)-2-[(1-[bis[4-(sulfanylmethyl)phenoxy]phosphoryl]-2-phenylethyl)carbamoyl]pyrrolidine-1-carboxylate
-
in 50 mM Tris, 1M NaCl, pH 7.5 containing 0.01% Triton X-100
0.0121
tert-butyl (2S)-2-[[1-(diphenoxyphosphoryl)-2-phenylethyl]carbamoyl]pyrrolidine-1-carboxylate
-
in 50 mM Tris, 1M NaCl, pH 7.5 containing 0.01% Triton X-100
0.0000000339
fungal protease inhibitor F
-
mutant T29M
-
0.000000148
fungal protease inhibitor F
-
wild-type
-
0.000000285
fungal protease inhibitor F
-
mutant T29L
-
0.000000327
fungal protease inhibitor F
-
mutant T29F
-
0.000000678
fungal protease inhibitor F
-
mutant T29E
-
0.00000245
fungal protease inhibitor F
-
mutant T29R
-
0.00000468
fungal protease inhibitor F
-
mutant T29G
-
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evolution
Q0WWH7
phylogenetic analysis, AtSASP and its putative orthologues clustering in one discrete group of subtilisin proteases in which no other Arabidospsis subtilisin protease is present. The enzyme function is at least partially conserved between Arabidopsis thaliana and Oryza sativa
evolution
the enzyme belongs to a structurally distinct class of the subtilase family
evolution
the enzyme is a member of the peptidases_S8/PCSK9/proteinase K-like family (Pf00082)
evolution
-
the subtilisin-like proteases share the same catalytic mechanism as the trypsin-like proteases, depending upon the hydroxyl group of a serine residue. The catalytic triad of subtilisin-like proteases is composed of Asp, His, and Ser. Due to its different specificity compared to the members of the S8 family of clan SB of proteases, the Fe protease might be a protease distinct from previously defined IUBMB groups of proteases, it is no member of the the S8 peptidase family
evolution
enzyme SOPT has a PEXEL-like sequence, is predicted to contain a subtilisin-like fold with a non-canonical catalytic triad, and is orthologous to Plasmodium falciparum SOPT. The function of SOPT is conserved in different Plasmodium species, overview
evolution
enzyme SOPT has a PEXEL-like sequence, it is predicted to contain a subtilisin-like fold with a non-canonical catalytic triad, and it is orthologous to Plasmodium berghei PIMMS2. The function of SOPT is conserved in different Plasmodium species, overview
evolution
-
enzyme subtilisin E-S7 (SES7) has 3 amino acids different from subtilisin E (1SCJ): S85A, T130S, and T162S
evolution
IvaP bears homology to subtilisin-like enzymes, a large family of serine proteases primarily comprised of secreted endopeptidases. IvaP contains a C-terminal bacterial prepeptidase PPC domain that is not typically found in subtilases but facilitates the secretion of other prokaryotic enzymes and is often cleaved extracellularly
evolution
subtilisin QK is highly homologous to nattokinase (NK, Q548F3)
evolution
the Arabidopsis thaliana genome encodes 56 subtilisin-like serine proteases (subtilases), enzyme AtSBT1.9 is a member of the subtilase subfamily 1
evolution
-
the enzyme belongs to the S8 peptidase family
evolution
-
enzyme SOPT has a PEXEL-like sequence, is predicted to contain a subtilisin-like fold with a non-canonical catalytic triad, and is orthologous to Plasmodium falciparum SOPT. The function of SOPT is conserved in different Plasmodium species, overview
-
evolution
Vibrio cholerae serotype O1 C6706
-
IvaP bears homology to subtilisin-like enzymes, a large family of serine proteases primarily comprised of secreted endopeptidases. IvaP contains a C-terminal bacterial prepeptidase PPC domain that is not typically found in subtilases but facilitates the secretion of other prokaryotic enzymes and is often cleaved extracellularly
-
evolution
-
the subtilisin-like proteases share the same catalytic mechanism as the trypsin-like proteases, depending upon the hydroxyl group of a serine residue. The catalytic triad of subtilisin-like proteases is composed of Asp, His, and Ser. Due to its different specificity compared to the members of the S8 family of clan SB of proteases, the Fe protease might be a protease distinct from previously defined IUBMB groups of proteases, it is no member of the the S8 peptidase family
-
evolution
-
the enzyme is a member of the peptidases_S8/PCSK9/proteinase K-like family (Pf00082)
-
evolution
-
the Arabidopsis thaliana genome encodes 56 subtilisin-like serine proteases (subtilases), enzyme AtSBT1.9 is a member of the subtilase subfamily 1
-
evolution
-
subtilisin QK is highly homologous to nattokinase (NK, Q548F3)
-
evolution
-
IvaP bears homology to subtilisin-like enzymes, a large family of serine proteases primarily comprised of secreted endopeptidases. IvaP contains a C-terminal bacterial prepeptidase PPC domain that is not typically found in subtilases but facilitates the secretion of other prokaryotic enzymes and is often cleaved extracellularly
-
evolution
-
the enzyme belongs to the S8 peptidase family
-
evolution
-
enzyme subtilisin E-S7 (SES7) has 3 amino acids different from subtilisin E (1SCJ): S85A, T130S, and T162S
-
evolution
-
IvaP bears homology to subtilisin-like enzymes, a large family of serine proteases primarily comprised of secreted endopeptidases. IvaP contains a C-terminal bacterial prepeptidase PPC domain that is not typically found in subtilases but facilitates the secretion of other prokaryotic enzymes and is often cleaved extracellularly
-
malfunction
-
gene knock-out results in reduced ability by the parasite to undergo promastigote to amastigote differentiation in vitro. SUB-deficient Leishmania display reduced virulence in infection models. SUB knock-out parasites show altered regulation of the terminal peroxidases of the trypanothione reductase system and the predominant tryparedoxin peroxidases are decreased in SUB-/- parasites. knock-out parasites show increased sensitivity to hydroperoxide. Data suggest that subtilisin is the maturase for tryparedoxin peroxidases and is necessary for full virulence
malfunction
-
using a protease mutant of Dichelobacter nodosus it is shown in a sheep virulence model that AprV2 is required for virulence
malfunction
Q0WWH7
at maturity, enzyme knockout sasp-1 plants produce 25% more inflorescence branches and siliques, mostly due to an increased number of second and third order branches, than either the wild-type or the rescued lines
malfunction
SOPT-deficient parasites develop normally through the asexual and sexual stages and produce equivalent numbers of ookinetes to NF54 controls, but they form fewer oocysts and sporozoites in mosquitoes
malfunction
the mutant PbDELTASOPT/PIMMS2 produces low numbers of salivary gland sporozoites
malfunction
-
the mutant PbDELTASOPT/PIMMS2 produces low numbers of salivary gland sporozoites
-
physiological function
AcpII comprises a prepropeptide, a catalytic domain that includes a protease-associated domain, and tandem repeat prepeptidase C-terminal domains
physiological function
-
alcalase-hydrolyzed potato protein has both antioxidant and emulsifying properties
physiological function
-
during growth of Pichia pastoris, Sub2 is produced as a secreted enzyme at a concentration of 10 microg/ml of culture supernatant after overexpression of the full-length SUB2 gene. During fermentative production of recombinant enzymes in methanol medium, 1 ml of Pichia pastoris culture supernatant is found to contain approximately 3 ng of Sub2, while the enzyme is not detected during growth in a medium containing glycerol as a carbon source
physiological function
-
is involved in Streptococcus suis virulence
physiological function
-
isolation of angiotensin I-converting enzyme inhibitory peptide from hydrolysates and enzymatic digests of Spirulina platensis by alcalase. The digests by alcalase with a molecular weight range of 0-3000 show the most potent inhibitory activity of 0.23 mg/ml with a yield of 15.0% among tested hydrolysates
physiological function
-
peanut hydrolysate obtained after 6 h of digestion by alcalase used to isolate angiotensin I converting enzyme inhibitory peptides
physiological function
-
Pro-subtilisin-like serine protease consists of an N-terminal propeptide (Ala1-Ala113), a mature domain (subtilisin-like serine protease, Val114-Val539) and a C-terminal propeptide (Asp540-Gly640)
physiological function
-
significantly inhibits carrageenan-induced mouse tail thrombus formation in vivo. Inhibition activity increases along with the injection amount of subtilisin QK, which presents linearity relationship. When the amount of subtilisin QK reaches 12000 IU, thrombus nearly disappears in mouse tail
physiological function
-
silk fibroin hydrolysate obtained through alcalase digestion demonstrates in vitro angiotensin I converting enzyme inhibitory activity and in vivo antihypertensive activity in spontaneously hypertensive rats. Degrees of hydrolysis and angiotensin I converting enzyme inhibitory activities is related with hydrolysis period of silk fibroin hydrolysates obtained with alcalase treatments: highest angiotensin I converting enzyme inhibitory activities (72.5%) are obtained with a hydrolysis time of 105 min, whereby degree of hydrolysis is 17.1%
physiological function
strains causing benign footrot secrete AprB2
physiological function
strains causing benign footrot secrete subtilisin-like protease BprB
physiological function
strains causing virulent footrot secrete the subtilisin-like protease AprV2
physiological function
strains causing virulent footrot secrete the subtilisin-like protease BprV
physiological function
-
subtilisin enhances transpeptidase activity of 67 kDa gamma-glutamyl transpeptidase and 30 kDa gamma-glutamyl transpeptidase, by nearly 1.5- and 2fold, respectively. In presence of subtilisin, 30 kDa gamma-glutamyl transpeptidase has improved catalytic efficiency, altered pH and temperature optima and has salt-tolerant glutaminase activity
physiological function
subtilisin-like serine proteases from nematode-trapping fungi are involved in the penetration and digestion of nematode cuticles
physiological function
subtilisin-like serine proteases from nematode-trapping fungi are involved in the penetration and digestion of nematode cuticles
physiological function
subtilisin-like serine proteases from nematode-trapping fungi are involved in the penetration and digestion of nematode cuticles
physiological function
subtilisin-like serine proteases from nematode-trapping fungi are involved in the penetration and digestion of nematode cuticles
physiological function
subtilisin-like serine proteases from nematode-trapping fungi are involved in the penetration and digestion of nematode cuticles
physiological function
subtilisin-like serine proteases from nematode-trapping fungi are involved in the penetration and digestion of nematode cuticles
physiological function
-
when subtilisin C. is chemically modified with polyethylene glycol and inhibited with a dansyl fluorophore, and initially dissolved in two organic solvents (acetonitrile and 1,4-dioxane), the active site environment of the enzyme is similar to that in water. Prolonged exposure to the organic medium causes this environment to resemble that of the solvent in which the enzyme is dissolved
physiological function
-
acts extracellularly in the apoplast of stomatal precursor cells where it may be involved in the generation of signals responsible for stomata density regulation
physiological function
-
enzyme shows caspase specificity
physiological function
-
enzyme shows caspase specificity
physiological function
-
implicated in fragmentation of the membrane-bound transcription factor AtbZIP1723 and precursors of pectin methylesterase and rapid alkalinization growth factor
physiological function
-
involved in proteolysis of the seed storage protein, beta-conglycinin
physiological function
-
pathogenesis related protein which is shown to be one of several subtilases that are specifically induced following pathogen infection. P69 is suggested to process a leucin-rich repeat cell wall protein in virus-infected tomato plants
physiological function
-
principal allergen produced by Aspergillus strains
physiological function
-
some caspase-like activities are attributable to the plant subtilisin-like proteases, saspases and phytaspases. Enzyme hydrolyzes a range of tetrapeptide caspase substrates following the aspartate residue. Enzyme is implicated the proteolytic degradation of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) during biotic and abiotic programmed cell death
physiological function
-
some caspase-like activities are attributable to the plant subtilisin-like proteases, saspases and phytaspases. Enzyme hydrolyzes a range of tetrapeptide caspase substrates following the aspartate residue. In response to death-inducing stimuli, phytaspase is shown to re-localize to the cell interior
physiological function
-
some caspase-like activities are attributable to the plant subtilisin-like proteases, saspases and phytaspases. Enzyme hydrolyzes a range of tetrapeptide caspase substrates following the aspartate residue. In response to death-inducing stimuli, phytaspase is shown to re-localize to the cell interior
physiological function
-
Subtilisin A applied at nanomolar concentrations suppresses epileptiform spikes in rat hippocampal slices and neocortex in vivo
physiological function
-
the subtilase ALE1 is involved in the generation of peptide signals that are required for cuticle formation and epidermal differentiation during Arabidopsis embryo development
physiological function
-
a cold-adapted protease, residue Ala284 is an important cold-adaptation determinant of the enzyme
physiological function
-
fungal subtilisin is a defense elicitor, culture filtrates from avirulent Acremonium spp. induce resistance against pathogens in strawberry plants or accumulation of reactive oxygen species (e.g. H2O2 and O2 -) and callose in Arabidopsis thaliana plants, expression analysis of defense-related genes in strawberry and defense responses induced by the enzyme in Arabidopsis leaves, overview
physiological function
modeling of intracellular subtilisin protease regulation within the cell
physiological function
Q0WWH7
the enzyme downregulates branching and silique production during monocarpic senescence
physiological function
the serine protease may be involved in both mycoparasitism and antibiotic secretion
physiological function
Plasmodium berghei PbSOPT/PIMMS2 is dispensable for ookinete development, and PbSOPT/PIMMS2 is dispensable for sporozoite infectivity and establishing patency. PIMMS2 is involved in midgut traversal in Anopheles gambiae. SOPT facilitates transmission of Plasmodium berghei ookinetes to mosquitoes
physiological function
Plasmodium falciparum subtilisin-like ookinete protein SOPT plays an important and conserved role during ookinete infection of the Anopheles stephensi midgut. It may be involved in infecting the human or mosquito host. SOPT facilitates transmission of Plasmodium falciparum ookinetes to mosquitoes
physiological function
subtilisin Carlsberg is a serine protease naturally secreted from Bacillus licheniformis
physiological function
Vibrio cholerae-secreted serine protease, IvaP, is active in Vibrio cholerae-infected rabbits and human choleric stool. Enzyme IvaP alters the activity of several host and pathogen enzymes in the gut and, along with other secreted Vibrio cholerae proteases, decreases binding of intelectin, an intestinal carbohydrate-binding protein, to Vibrio cholerae in vivo. IvaP plays a role in modulating intelectin-Vibrio cholerae interactions, it subverts this host-pathogen interaction in vivo
physiological function
-
Plasmodium berghei PbSOPT/PIMMS2 is dispensable for ookinete development, and PbSOPT/PIMMS2 is dispensable for sporozoite infectivity and establishing patency. PIMMS2 is involved in midgut traversal in Anopheles gambiae. SOPT facilitates transmission of Plasmodium berghei ookinetes to mosquitoes
-
physiological function
Vibrio cholerae serotype O1 C6706
-
Vibrio cholerae-secreted serine protease, IvaP, is active in Vibrio cholerae-infected rabbits and human choleric stool. Enzyme IvaP alters the activity of several host and pathogen enzymes in the gut and, along with other secreted Vibrio cholerae proteases, decreases binding of intelectin, an intestinal carbohydrate-binding protein, to Vibrio cholerae in vivo. IvaP plays a role in modulating intelectin-Vibrio cholerae interactions, it subverts this host-pathogen interaction in vivo
-
physiological function
-
the serine protease may be involved in both mycoparasitism and antibiotic secretion
-
physiological function
-
significantly inhibits carrageenan-induced mouse tail thrombus formation in vivo. Inhibition activity increases along with the injection amount of subtilisin QK, which presents linearity relationship. When the amount of subtilisin QK reaches 12000 IU, thrombus nearly disappears in mouse tail
-
physiological function
-
Vibrio cholerae-secreted serine protease, IvaP, is active in Vibrio cholerae-infected rabbits and human choleric stool. Enzyme IvaP alters the activity of several host and pathogen enzymes in the gut and, along with other secreted Vibrio cholerae proteases, decreases binding of intelectin, an intestinal carbohydrate-binding protein, to Vibrio cholerae in vivo. IvaP plays a role in modulating intelectin-Vibrio cholerae interactions, it subverts this host-pathogen interaction in vivo
-
physiological function
-
AcpII comprises a prepropeptide, a catalytic domain that includes a protease-associated domain, and tandem repeat prepeptidase C-terminal domains
-
physiological function
-
strains causing benign footrot secrete subtilisin-like protease BprB
-
physiological function
-
is involved in Streptococcus suis virulence
-
physiological function
-
Vibrio cholerae-secreted serine protease, IvaP, is active in Vibrio cholerae-infected rabbits and human choleric stool. Enzyme IvaP alters the activity of several host and pathogen enzymes in the gut and, along with other secreted Vibrio cholerae proteases, decreases binding of intelectin, an intestinal carbohydrate-binding protein, to Vibrio cholerae in vivo. IvaP plays a role in modulating intelectin-Vibrio cholerae interactions, it subverts this host-pathogen interaction in vivo
-
physiological function
-
strains causing virulent footrot secrete the subtilisin-like protease BprV
-
physiological function
-
strains causing virulent footrot secrete the subtilisin-like protease AprV2
-
additional information
molecular modeling and docking analysis using crystal structure PDB ID 1yu6
additional information
Q0WWH7
occurrence of the two variant forms of AtSASP can be due to posttranslational modifications
additional information
-
occurrence of the two variant forms of AtSASP can be due to posttranslational modifications
additional information
-
structure homology modeling, structure comparisons, overview
additional information
structure molecular modeling using the crystal structure of the pro-subtilisin E complex, PDB ID 1SCJ, the active site Cys221 is replaced with the catalytic serine, molecular dynamics simulation, overview
additional information
substrate specificity and the role of stress signals such as divalent metal ions play roles in defining the proteolytic activity of Bacillus clausii intracellular subtilisin protease, molecular basis, overview. Heat-denatured whole proteins are found to be better substrates for the enzyme than the native forms. The S1, S2 and S4 sites form defined substrate binding pockets
additional information
-
substrate specificity and the role of stress signals such as divalent metal ions play roles in defining the proteolytic activity of Bacillus clausii intracellular subtilisin protease, molecular basis, overview. Heat-denatured whole proteins are found to be better substrates for the enzyme than the native forms. The S1, S2 and S4 sites form defined substrate binding pockets
additional information
the catalytic triad residues consists of Ser221, Pro210 to His64
additional information
homology modeling of Plasmodium berghei SOPT, overview
additional information
-
homology modeling of Plasmodium berghei SOPT, overview
additional information
homology modeling of Plasmodium falciparum SOPT, overview
additional information
-
homology modeling of Plasmodium falciparum SOPT, overview
additional information
initial in-silico sequence analysis and protein modelling reveal the dominant alpha-helical structural features embedding the catalytic residues Asp180, His213, and Ser364, which form the canonical catalytic triad of subtilisin-like serine protease. In the N-terminal region, a subtilisin-N domain is detected between residues Asp55 and Thr135
additional information
-
the Fe protease contains an insertion (amino acids 168-173 of the mature sequence) which is not present in the proteinase K sequence
additional information
the salt-bridge triad Gln125-Gln377-Gln381 in subtilisin E contributes to thermostability and activity. The Q125 residue is important for catalytic activity
additional information
-
the salt-bridge triad Gln125-Gln377-Gln381 in subtilisin E contributes to thermostability and activity. The Q125 residue is important for catalytic activity
additional information
-
homology modeling of Plasmodium berghei SOPT, overview
-
additional information
-
the salt-bridge triad Gln125-Gln377-Gln381 in subtilisin E contributes to thermostability and activity. The Q125 residue is important for catalytic activity
-
additional information
-
initial in-silico sequence analysis and protein modelling reveal the dominant alpha-helical structural features embedding the catalytic residues Asp180, His213, and Ser364, which form the canonical catalytic triad of subtilisin-like serine protease. In the N-terminal region, a subtilisin-N domain is detected between residues Asp55 and Thr135
-
additional information
-
the Fe protease contains an insertion (amino acids 168-173 of the mature sequence) which is not present in the proteinase K sequence
-
additional information
-
initial in-silico sequence analysis and protein modelling reveal the dominant alpha-helical structural features embedding the catalytic residues Asp180, His213, and Ser364, which form the canonical catalytic triad of subtilisin-like serine protease. In the N-terminal region, a subtilisin-N domain is detected between residues Asp55 and Thr135
-
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N115D
GN111900.1
site-directed mutagenesis, inactive mutant
N154D
GN111900.1
site-directed mutagenesis, the mutant has 107% proteolytc activity compared to the wild-type enzyme
N167D
GN111900.1
site-directed mutagenesis, the mutant has 77% proteolytc activity compared to the wild-type enzyme
N205D
GN111900.1
site-directed mutagenesis, the mutant has 113% proteolytc activity compared to the wild-type enzyme
N236D
GN111900.1
site-directed mutagenesis, the mutant has 115% proteolytc activity compared to the wild-type enzyme
N242D
GN111900.1
site-directed mutagenesis, the mutant has 118% proteolytc activity compared to the wild-type enzyme
N250D
GN111900.1
site-directed mutagenesis, the mutant has 113% proteolytc activity compared to the wild-type enzyme
N253D
GN111900.1
site-directed mutagenesis, the mutant has 135% proteolytc activity compared to the wild-type enzyme and shows a dramatic pH activity profiles shifted towards higher activity at lower pH range of pH 8.5-10
N253D/Q256E
GN111900.1
site-directed mutagenesis, the mutant shows a dramatic pH activity profiles shifted towards higher activity at lower pH range of pH 8.5-10, the mutant has a 2fold increased activity compared to the wild-type enzyme with a thermal resistance increased by 2.4°C at pH 8.5
N60D
GN111900.1
site-directed mutagenesis, the mutant has 32% proteolytc activity compared to the wild-type enzyme
N97D
GN111900.1
site-directed mutagenesis, the mutant has 146% proteolytc activity compared to the wild-type enzyme
Q107E
GN111900.1
site-directed mutagenesis, the mutant has 53% proteolytc activity compared to the wild-type enzyme
Q12E
GN111900.1
site-directed mutagenesis, the mutant has 114% proteolytc activity compared to the wild-type enzyme
Q176E
GN111900.1
site-directed mutagenesis, the mutant has 97% proteolytc activity compared to the wild-type enzyme
Q185E
GN111900.1
site-directed mutagenesis, inactive mutant
Q200E
GN111900.1
site-directed mutagenesis, the mutant has 125% proteolytc activity compared to the wild-type enzyme
Q230E
GN111900.1
site-directed mutagenesis, the mutant has 107% proteolytc activity compared to the wild-type enzyme
Q256E
GN111900.1
site-directed mutagenesis, the mutant has 129% proteolytc activity compared to the wild-type enzyme and shows a dramatic pH activity profiles shifted towards higher activity at lower pH range of pH 8.5-10
Q37E
GN111900.1
site-directed mutagenesis, the mutant has 136% proteolytc activity compared to the wild-type enzyme
N250D
-
site-directed mutagenesis, the mutant has 113% proteolytc activity compared to the wild-type enzyme
-
N97D
-
site-directed mutagenesis, the mutant has 146% proteolytc activity compared to the wild-type enzyme
-
Q107E
-
site-directed mutagenesis, the mutant has 53% proteolytc activity compared to the wild-type enzyme
-
Q12E
-
site-directed mutagenesis, the mutant has 114% proteolytc activity compared to the wild-type enzyme
-
A116E
-
site-directed mutagenesis, BPN'
A194P
-
site-directed mutagenesis, savinase
A1C
does not change the catalytic properties of subtilisin S189 but allows the introduction of a fluorescent group at its N-terminus
D32A
engineered variant of the protease subtilisin, denoted S189, mutation renders the enzyme's activity dependent on the presence of certain small anions such as fluoride or azide. Is activated more than 3000fold by azide
D32N
-
does not fold at all in the presence of proR9
D97G
-
site-directed mutagenesis, subtilisin E
E89S
-
site-directed mutagenesis, BPN'
G131D
-
site-directed mutagenesis, BPN'
G166R
-
site-directed mutagenesis, subtilisin E
G166S
-
site-directed mutagenesis, BPN'
G195E
-
site-directed mutagenesis, BPN'
H120D
-
site-directed mutagenesis, savinase
I107V
-
site-directed mutagenesis, BPN'
K213R
-
site-directed mutagenesis, BPN'
K235L
-
site-directed mutagenesis, savinase
K256Y
-
site-directed mutagenesis, BPN'
K27R
-
site-directed mutagenesis, BPN'
N109S
-
site-directed mutagenesis, BPN'
N118S
-
site-directed mutagenesis, subtilisin E
N155L
-
folding kinetics very similar to that of S221A
N181D
-
site-directed mutagenesis, subtilisin E
N218D
-
site-directed mutagenesis, BPN'
N77K
-
site-directed mutagenesis, BPN'
P14L
-
site-directed mutagenesis, subtilisin E
P168G
-
weaker binding of proR9
P172D
-
site-directed mutagenesis, BPN'
Q19E/Q271E
-
site-directed mutagenesis, BPN'
Q206Cox
-
site-directed mutagenesis, BPN'
R170Y
-
site-directed mutagenesis, BPN'
S101K/G169A
-
mutant shows 3.3fold activity compared to wild-type
S101L/G169A
-
mutant shows 2.9fold activity compared to wild-type
S101R/G169A
-
mutant shows 2.2fold activity compared to wild-type
S101W/G169A
-
mutant shows 3.9fold activity compared to wild-type
S101W/G169A/V192A
-
mutant shows 1.4fold activity compared to wild-type, kcat doubled compared to wild-type, Km decreased compared to wild-type
S128G
-
site-directed mutagenesis, savinase
S161C
-
site-directed mutagenesis, subtilisin E
S53TI
-
site-directed mutagenesis, BPN'
S63D
-
site-directed mutagenesis, BPN'
S78D
-
site-directed mutagenesis, BPN'
T22C/S87C/S221C
-
if denatured, it is refolded with an excess of proR9. About 75% is rapidly bound to proR9. 25% undergoes a slow step prior to binding
V205I
-
site-directed mutagenesis, savinase
V8I
-
site-directed mutagenesis, BPN'
Y217L
-
commercial version of enzyme, i.e. SBT*
G165L
site-directed mutagenesis, the mutant shows slightly increased transacylation activity compared to wild-type
G165L/M221C
site-directed mutagenesis, the mutant shows about 5fold increased transacylation activity compared to wild-type
G165L/M221F
site-directed mutagenesis, the mutant shows about 6.5fold increased transacylation activity compared to wild-type
G165L/M221S
site-directed mutagenesis, the mutant shows slightly increased transacylation activity compared to wild-type
G165X
site-directed mutagenesis, catalytic constants of subtilisin Carlsberg for perhydrolysis of methylpropionate, methylbutyrate and methylpentanoate are increased up to 3.5fold, 5.4fold and 5.5fold, respectively, while proteolysis is decreased up to 100fold for N-succinyl-Ala-Ala-Pro-Phe-pnitroanilide substrate
G166R
-
the mutant is both more stable and displays more activity compared to the wild-type enzyme
M221A
site-directed mutagenesis, the mutant shows reduced transacylation activity compared to wild-type
M221C
site-directed mutagenesis, the mutant shows similar transacylation activity compared to wild-type
M221F
site-directed mutagenesis, the mutant shows similar transacylation activity compared to wild-type
M221S
site-directed mutagenesis, the mutant shows unaltered transacylation activity compared to wild-type
M221W
site-directed mutagenesis, the mutant shows reduced transacylation activity compared to wild-type
N212G
site-directed mutagenesis, the mutant shows increased kcat compared to the wild-type enzyme
P210A
site-directed mutagenesis, the mutant shows increased kcat compared to the wild-type enzyme
P210G
site-directed mutagenesis, the mutant shows 1.5fold increased kcat compared to the wild-type enzyme
P210G/T211G
site-directed mutagenesis, the mutant shows 1.7fold increased kcat compared to the wild-type enzyme
P210G/T211G/N212G
site-directed mutagenesis, the mutant shows 1.8fold increased kcat compared to the wild-type enzyme
S161C
-
the mutant brings increased stability to subtilisin compared to the wild-type
T211G
site-directed mutagenesis, the mutant shows 1.8fold increased kcat compared to the wild-type enzyme
T58A/L216W
site-directed mutagenesis, the mutant catalyzes in addition to its proteolytic activity the generation of peroxycarboxylic acids from corresponding esters in the presence of hydrogen peroxide
A153V
site-directed mutagenesis, the mutant shows increased activity without detergents compared to the wild-type, but does not show improved properties in chaotropic conditions
G166M
site-directed mutagenesis, the mutant shows increased activity without detergents compared to the wild-type, and improved properties in chaotropic conditions
G166S
site-directed mutagenesis, the mutant shows increased activity without detergents compared to the wild-type, and improved properties in chaotropic conditions
I205V
site-directed mutagenesis, the mutant shows increased activity without detergents compared to the wild-type, but does not show improved properties in chaotropic conditions
K211P/R212A
mutant is more thermostable compared to wild-type, half-life at 60°C 10times longer compared to wild-type. Molecular dynamics simulation at 10°C and 90°C reveal that the average global flexibility of both variants is slightly higher than wild-type
K211P/R212A/S145I/S175T/K221E/N291I/S295T
mutant is more thermostable compared to wild-type, half-life at 60°C 500times longer compared to wild-type. Molecular dynamics simulation at 10°C and 90°C reveal that the average global flexibility of both variants is slightly higher than wild-type
N218S
site-directed mutagenesis, the mutant shows increased activity and stability in the presence of GdmCl or SDS compared to the wild-type enzyme
Q125/Q377E/Q381R
site-directed mutagenesis, the mutant shows increased thermotolerance compared to the wild-type enzyme, but is 60% less active than the wild-type
Q125R
site-directed mutagenesis, the mutant does not show increased thermotolerance compared to the wild-type enzyme, it is 60% less active than the wild-type
Q377E
site-directed mutagenesis, the mutant shows increased thermotolerance and an increase in protease activity of 46.5% compared to the wild-type enzyme
Q381R
site-directed mutagenesis, the mutant shows increased thermotolerance and an increase in protease activity of 46.5% compared to the wild-type enzyme
S221C
-
site-directed mutagenesis, mutation of the critical catalytic residue Ser221 of SES7 to a cysteine to avoid protease self-digestion
S62I
site-directed mutagenesis, the mutant shows increased activity without detergents compared to the wild-type, and slightly improved properties in chaotropic conditions
S62I/A153V/G166S/I205V/N218S/T224A
site-directed mutagenesis, the mutant shows high activity and stability in the presence of GdmCl or SDS compared to the wild-type enzyme
S62I/A153V/G166S/T224A/T240S
S62I/G166M
site-directed mutagenesis, the mutant shows increased activity without detergents compared to the wild-type, and highly improved properties in chaotropic conditions
T224A
site-directed mutagenesis, the mutant shows increased activity and stability in the presence of GdmCl or SDS compared to the wild-type enzyme
Q125/Q377E/Q381R
-
site-directed mutagenesis, the mutant shows increased thermotolerance compared to the wild-type enzyme, but is 60% less active than the wild-type
-
Q125R
-
site-directed mutagenesis, the mutant does not show increased thermotolerance compared to the wild-type enzyme, it is 60% less active than the wild-type
-
Q377E
-
site-directed mutagenesis, the mutant shows increased thermotolerance and an increase in protease activity of 46.5% compared to the wild-type enzyme
-
Q381R
-
site-directed mutagenesis, the mutant shows increased thermotolerance and an increase in protease activity of 46.5% compared to the wild-type enzyme
-
S221C
-
site-directed mutagenesis, mutation of the critical catalytic residue Ser221 of SES7 to a cysteine to avoid protease self-digestion
-
D180G
-
mutant using substrate N-methoxysuccinyl-Ala-Ala-Pro-Val-4-nitroanilide Km similar to wild-type, kcat value enhanced, kcat/Km value enhanced by 4%
D180G/D182G
-
using substrate N-methoxysuccinyl-Ala-Ala-Pro-Val-4-nitroanilide Km similar to wild-type, kcat value highly enhanced, kcat/Km value enhanced by 33%
D182G
-
using substrate N-methoxysuccinyl-Ala-Ala-Pro-Val-4-nitroanilide Km similar to wild-type, kcat value enhanced, kcat/Km value enhanced by 27%
DELTA83-99
-
truncation mutant is not functional
Y92A
-
mutant shows decreased elastin degradation
Y92D
-
mutant shows decreased elastin degradation
Y92F
-
mutant shows increased elastin degradation
Y92L
-
mutant shows decreased elastin degradation
M222C
-
site-directed mutagenesis combined with chemical modification
S156C
-
site-directed mutagenesis combined with chemical modification
S166C
-
site-directed mutagenesis combined with chemical modification
V104S/L124M/P129S/S130G/P131E/A133S/T134L/L135I
-
mutant containing the highly flexible region of psychrophilic enzyme TA39 subtilisin. Mutant shows the same temperature optimum and pH-profile as wild-type, but higher specificity for substrate succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-nitroanilide and broader substrate specificity. Mutant has a decreased thermostability, but increased activity at low temperature
G6G
-
possesses a single Tn917 insertion, is devoid of subtilisin-like proteinase activity, has longer generation times and is more susceptible to killing by whole blood than the wild-type
M3G
-
possesses a single Tn917 insertion, is devoid of subtilisin-like proteinase activity, has longer generation times and is more susceptible to killing by whole blood than the wild-type
G6G
-
possesses a single Tn917 insertion, is devoid of subtilisin-like proteinase activity, has longer generation times and is more susceptible to killing by whole blood than the wild-type
-
M3G
-
possesses a single Tn917 insertion, is devoid of subtilisin-like proteinase activity, has longer generation times and is more susceptible to killing by whole blood than the wild-type
-
DELTACa2-Pro-S324A
-
does not completely lose the ability to fold into a native structure, probably because binding of the water molecule to the position corresponding to the Ca2 site and movement of the epsilon-amino group of Lys213 to the position corresponding to the Ca3 site compensate at least partly for the destabilization of the structure of the Ca2+-binding loop caused by the removal of the Ca2 or Ca3 site
DELTACa3-Pro-S324A
-
does not completely lose the ability to fold into a native structure, probably because binding of the water molecule to the position corresponding to the Ca2 site and movement of the epsilon-amino group of Lys213 to the position corresponding to the Ca3 site compensate at least partly for the destabilization of the structure of the Ca2+-binding loop caused by the removal of the Ca2 or Ca3 site
DELTAloop-subtilisin
-
the unique insertion sequence of subtilisin (Pro207-Asp226) is removed and Gly206,Ala228, and Glu229 are replaced with Asn, Met, and Asp, respectively. Lacks the Ca2+-binding loop, completely loses the ability to fold into a native structure
E61G
-
pro-subtilisin mutant, exhibits a halo-forming activity at 80, 70 and 60°C
E61K
-
pro-subtilisin mutant, exhibits a halo-forming activity at 80, 70 and 60°C
G56E
-
Pro-G56E gives a halo at temperatures equal or higher than 60 °C
G56F
-
Pro-G56F gives a halo only at temperatures equal or higher than 70 °C
G56S/T135S
-
low-temperature adaptation of prepro-G56S/T135S-subtilisin
G56W
-
Pro-G56W gives a halo only at 80 °C like the wild-type
S255A
-
active-site mutant of pro-subtilisin. Accumulates in cells in inclusion bodies like pro-subtilisin
S324C
-
propeptide:subtilisin complex is stable
S359A
-
active site mutant. Upon overproduction, Pro-S359A accumulates in the cells in a soluble form
G169A
-
site-directed mutagenesis, BPN'
G169A
-
stable only in presence of excess Ca2+
G169A
-
mutant shows 1.4fold activity compared to wild-type
L126I
-
site-directed mutagenesis, BPN'
L126I
-
site-directed mutagenesis, BPN', stable only in presence of excess Ca2+
M50F
-
site-directed mutagenesis, BPN'
M50F
-
site-directed mutagenesis, BPN',stabilized in EDTA, but destabilized slightly in CaCl2
N218S
-
site-directed mutagenesis, BPN'
N218S
-
site-directed mutagenesis, BPN', stabilized significantly, either with or without Ca2+
N218S
-
site-directed mutagenesis, subtilisin E
N76D
-
site-directed mutagenesis, BPN'
N76D
-
site-directed mutagenesis, subtilisin E
Q271E
-
site-directed mutagenesis, BPN'
Q271E
-
site-directed mutagenesis, BPN', stabilized significantly, either with or without Ca2+
S188P
-
site-directed mutagenesis, BPN'
S188P
-
site-directed mutagenesis, BPN', stable only in presence of excess Ca2+
S194P
-
site-directed mutagenesis, BPN'
S194P
-
site-directed mutagenesis, subtilisin E
S221A
-
a delta75-83 mutant. Shows slow folding reaction. Is unstable at low metal concentration, unfolding at a rate of 0.6 h-1. If denatured, it is refolded with an excess of proR9
S221A
inactive form of subtilisin S189
S221C
-
site-directed mutagenesis, BPN'
S221C
-
folding kinetics very similar to that of S221A
T254A
-
site-directed mutagenesis, BPN'
T254A
-
site-directed mutagenesis, BPN', stable only in presence of excess Ca2+
Y217K
-
site-directed mutagenesis, BPN'
Y217K
-
site-directed mutagenesis, BPN', stabilized significantly, either with or without Ca2+
S62I/A153V/G166S/I205V
site-directed mutagenesis, the mutant shows increased activity and stability in the presence of GdmCl or SDS compared to the wild-type enzyme
S62I/A153V/G166S/I205V
site-directed mutagenesis, the mutant shows increased activity without detergents compared to the wild-type, and highly improved properties in chaotropic conditions
S62I/A153V/G166S/T224A/T240S
site-directed mutagenesis, the mutant shows high activity and stability in the presence of GdmCl or SDS compared to the wild-type enzyme
S62I/A153V/G166S/T224A/T240S
site-directed mutagenesis, the mutant shows increased activity and stability in the presence of GdmCl or SDS compared to the wild-type enzyme
G56S
-
Pro-G56S gives a halo from 40-80°C
G56S
-
pro-subtilisin mutant, does not seriously affect the structure of pro-subtilisin. Is more effectively matured than pro-subtilisin at lower temperatures
S324A
-
active-site mutant of Pro-subtilisin
S324A
-
pro-subtilisin, which is not autoprocessed at all when the active site serine residue is replaced with Ala. Is refolded in the presence of Ca2+
S324A
-
Pro-S324A represents the active site mutant of pro-subtilisin, Pro-S324A is used to construct mutant proteins to prevent their autoprocessing and self-degradation
S324A
site-directed mutagenesis, active site mutant
S361A
site-directed mutagenesis, mutation of the catalytic residue partially inhibits autoproteolysis, but the IvaPS361A mutant can be cleaved to the 47-kDa mature form through a mechanism other than autoproteolysis
S361A
-
site-directed mutagenesis, mutation of the catalytic residue partially inhibits autoproteolysis, but the IvaPS361A mutant can be cleaved to the 47-kDa mature form through a mechanism other than autoproteolysis
-
S361A
Vibrio cholerae serotype O1 C6706
-
site-directed mutagenesis, mutation of the catalytic residue partially inhibits autoproteolysis, but the IvaPS361A mutant can be cleaved to the 47-kDa mature form through a mechanism other than autoproteolysis
-
S361A
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site-directed mutagenesis, mutation of the catalytic residue partially inhibits autoproteolysis, but the IvaPS361A mutant can be cleaved to the 47-kDa mature form through a mechanism other than autoproteolysis
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additional information
GN111900.1
mimicking surface deamidation by substituting Gln by Glu and/or Asn by Asp might be a simple and fast protein reengineering approach for modulating enzyme properties such as activity, pH optimum, and thermal resistance, deamidation in five (N97, N253, Q37, Q200, and Q256) out of eight (N97, N154, N250, N253, Q37, Q107, Q200, and Q256) amino acids, comparison of wild-type and mutant enzymes, overview
additional information
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mimicking surface deamidation by substituting Gln by Glu and/or Asn by Asp might be a simple and fast protein reengineering approach for modulating enzyme properties such as activity, pH optimum, and thermal resistance, deamidation in five (N97, N253, Q37, Q200, and Q256) out of eight (N97, N154, N250, N253, Q37, Q107, Q200, and Q256) amino acids, comparison of wild-type and mutant enzymes, overview
additional information
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mimicking surface deamidation by substituting Gln by Glu and/or Asn by Asp might be a simple and fast protein reengineering approach for modulating enzyme properties such as activity, pH optimum, and thermal resistance, deamidation in five (N97, N253, Q37, Q200, and Q256) out of eight (N97, N154, N250, N253, Q37, Q107, Q200, and Q256) amino acids, comparison of wild-type and mutant enzymes, overview
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additional information
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introduction of about 20 site-directed mutations to obtain a variant with increased sequence selectivity, a predomain that can direct cleavage to the junction of any protein fused to it, and a modified active site to kinetically isolate binding and cleavage reactions. Identification of specific anions that trigger the processing reaction so that column-immobilized mutant enzyme can be used as both the affinity ligand and the processing protease for one-step purification methods
additional information
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sequential randomization of 12 amino acid positions in calcium-free enzyme. Mutations increase the half-life of enzyme at elevated temperature by 15000fold and partially increase ratio of kcat/KM-value
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site saturation mutagenesis of the subtilisin Carlsberg variant T58A/L216W at positionsThr33, Val67, Ser124, Gly126, Ser155, Gly165, Ala168, Trp216, Asn217, Gly218, Met221
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immobilization of recombinant subtilisin Carlsberg. Enantioselectivities of immobilized wild-type and mutants of subtilisin Carlsberg in the transacylation of racemic 1-phenylethanol and vinyl butyrate in tetrahydrofuran
additional information
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ionic-surfactant-coated Bacillus licheniformis subtilisin (ISCBLS) is prepared by freeze-drying Bacillus licheniformis subtilisin with both ionic surfactant and dextrin. ISCBCL displays 9300fold enhanced activity relative to its native counterpart in the transesterificaion of N-acetyl phenylalanine ethyl ester with 1-propanol in hexane and 12800fold enhanced activity in the transesterification of trifluoroethyl butyrate with 1-phenylethanol in tetrahydrofuran
additional information
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the enzyme subtilisin A is immobilized by simple hydrophobic adsorption onto various surface-grafted macroporous silica gels resulting in easy-to-prepare and stable biocatalysts enabling the efficient kinetic resolution (KR) and dynamic kinetic resolution (DKR) of racemic N-tert-butyloxycarbonylphenylalanine ethyl thioester with benzylamine
additional information
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mutant lacking three secreted serine proteases regulated by sigma-H, subtilisin, Epr and Vpr, produce less CSF and has less proCSF-processing activity
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directed evolution of subtilisin E into a highly active and guanidinium chloride- and sodium dodecylsulfate-tolerant protease, subtilisin E is engineered into a chaotolerent protease, the enzyme gains a protease stability improved in a chaotropic salt (GdmCl) or a detergent (SDS), nultiple screening, overview
additional information
CRISPR-Cas9 in situ engineering of subtilisin E in Bacillus subtilis by usage of a flexible, co-transformation approach where the single guide RNA is inserted in a plasmid for Cas9 co-expression, and the donor DNA is supplied as a linear PCR product observing an editing efficiency of 76%. The method allows multiple, rapid rounds of in situ editing of the subtilisin E gene to incorporate a salt bridge triad present in the Bacillus clausii thermotolerant homologue, M-protease. Method, overview. The enzyme mutant obtained shows increased thermotolerance and activity
additional information
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CRISPR-Cas9 in situ engineering of subtilisin E in Bacillus subtilis by usage of a flexible, co-transformation approach where the single guide RNA is inserted in a plasmid for Cas9 co-expression, and the donor DNA is supplied as a linear PCR product observing an editing efficiency of 76%. The method allows multiple, rapid rounds of in situ editing of the subtilisin E gene to incorporate a salt bridge triad present in the Bacillus clausii thermotolerant homologue, M-protease. Method, overview. The enzyme mutant obtained shows increased thermotolerance and activity
additional information
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CRISPR-Cas9 in situ engineering of subtilisin E in Bacillus subtilis by usage of a flexible, co-transformation approach where the single guide RNA is inserted in a plasmid for Cas9 co-expression, and the donor DNA is supplied as a linear PCR product observing an editing efficiency of 76%. The method allows multiple, rapid rounds of in situ editing of the subtilisin E gene to incorporate a salt bridge triad present in the Bacillus clausii thermotolerant homologue, M-protease. Method, overview. The enzyme mutant obtained shows increased thermotolerance and activity
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additional information
generation of enzyme-deficient mutant PbDELTASOPT/PIMMS2, production of oocysts and sporozoites in mosquitoes containing PbDELTASOPT/PIMMS2 parasites
additional information
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generation of enzyme-deficient mutant PbDELTASOPT/PIMMS2, production of oocysts and sporozoites in mosquitoes containing PbDELTASOPT/PIMMS2 parasites
additional information
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generation of enzyme-deficient mutant PbDELTASOPT/PIMMS2, production of oocysts and sporozoites in mosquitoes containing PbDELTASOPT/PIMMS2 parasites
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additional information
construction of pro-enzyme derivatives lacking the Ca1 ion (Pro-TKS/DELTACa1), Ca6 ion (Pro-TKS/DELTACa6), and Ca7 ion (Pro-TKS/DELTACa7), and their active site mutants, Pro-S324A/DELTACa1, Pro-S324A/DELTACa6, and Pro-S324A/DELTACa7, respectively. Mutants Pro-TKS/DELTACa6 and Pro-TKS/DELTACa7 fully mature into their active forms upon incubation at 80°C for 30 min like the wild-type enzyme. In contrast, mutant Pro-TKS/DELTACa1 matures poorly at 80°C because of the instability of its mature domain. Refolding rates of all Pro-S324A derivatives are comparable to that of Pro-S324A (active site mutant of wild-type pro-enzyme), indicating that these Ca(2+) ions are not needed for folding of Tk-subtilisin
additional information
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construction of pro-enzyme derivatives lacking the Ca1 ion (Pro-TKS/DELTACa1), Ca6 ion (Pro-TKS/DELTACa6), and Ca7 ion (Pro-TKS/DELTACa7), and their active site mutants, Pro-S324A/DELTACa1, Pro-S324A/DELTACa6, and Pro-S324A/DELTACa7, respectively. Mutants Pro-TKS/DELTACa6 and Pro-TKS/DELTACa7 fully mature into their active forms upon incubation at 80°C for 30 min like the wild-type enzyme. In contrast, mutant Pro-TKS/DELTACa1 matures poorly at 80°C because of the instability of its mature domain. Refolding rates of all Pro-S324A derivatives are comparable to that of Pro-S324A (active site mutant of wild-type pro-enzyme), indicating that these Ca(2+) ions are not needed for folding of Tk-subtilisin
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