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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
-
-
?
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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random mutagenesis to enhance the activity of subtilisin in organic solvents
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under relatively non-aqueous conditions, immobilized subtilisin is able to synthesize phenylacetic acid ethyl ester
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high elastolytic acitivity
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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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reactions catalyzed: 1. peptide bond hydrolysis, 2. ester bond hydrolysis, 3. transesterification, 4. transpeptidation
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reactions catalyzed: 1. peptide bond hydrolysis, 2. ester bond hydrolysis, 3. transesterification, 4. transpeptidation
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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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biosynthesis of subtilisin requires participation of an N-terminal prodomain
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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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high elastolytic acitivity
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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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random mutagenesis to enhance the activity of subtilisin in organic solvents
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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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reactions catalyzed: 1. peptide bond hydrolysis, 2. ester bond hydrolysis, 3. transesterification, 4. transpeptidation
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does not cleave proPhrE
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the enzyme shows activity towards complex substrates, e.g. skimmed milk
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the enzyme shows activity towards complex substrates, e.g. skimmed milk
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performance of a thrombolytic activity assay
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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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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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random mutagenesis to enhance the activity of subtilisin in organic solvents
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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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performance of a thrombolytic activity assay
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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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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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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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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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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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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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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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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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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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