Information on EC 3.4.21.62 - Subtilisin

New: Word Map on EC 3.4.21.62
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Search Reference ID:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


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

EC NUMBER
COMMENTARY hide
3.4.21.62
-
RECOMMENDED NAME
GeneOntology No.
Subtilisin
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyses peptide amides
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ester bond hydrolysis
hydrolysis of peptide bond
-
-
-
-
transesterification
-
-
-
-
transpeptidation
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
9014-01-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain AC40T
UniProt
Manually annotated by BRENDA team
strain AC40T
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Opticlean
-
-
Manually annotated by BRENDA team
Opticlean
-
-
Manually annotated by BRENDA team
strain GMBAE 42, highest activity in late stationary growth phase in protein-rich medium at pH 10.5
-
-
Manually annotated by BRENDA team
-
GN111900.1
GenBank
Manually annotated by BRENDA team
-
GN111900.1
GenBank
Manually annotated by BRENDA team
strain 3-19
-
-
Manually annotated by BRENDA team
Bacillus intermedius Mrz 19
strain 3-19
-
-
Manually annotated by BRENDA team
strain 1168
-
-
Manually annotated by BRENDA team
strain DJ-1
-
-
Manually annotated by BRENDA team
strain G-825-6 (subtilisin Sendai)
-
-
Manually annotated by BRENDA team
Bacillus sp. GX6644
strain GX6644 (subtilisin GX)
-
-
Manually annotated by BRENDA team
strain TA41 (antarctic psychrophilic Bacillus)
-
-
Manually annotated by BRENDA team
strain 1168
-
-
Manually annotated by BRENDA team
strain 72
-
-
Manually annotated by BRENDA team
strain CN2, growth on soy peptone medium
-
-
Manually annotated by BRENDA team
strain DB104 harboring the subtilisin gene ligated into plasmid pUB110
-
-
Manually annotated by BRENDA team
strain DB428 a clone producing Q103R subtilisin E
-
-
Manually annotated by BRENDA team
strain DY
-
-
Manually annotated by BRENDA team
strain IBTC-3
-
-
Manually annotated by BRENDA team
JB1
UniProt
Manually annotated by BRENDA team
QK02
-
-
Manually annotated by BRENDA team
strain RT-5, a thermostable soil isolate from the Tharparkar desert of Pakistan
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
BprB; strain C305
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
collected at Base Frei Montalva, King George Island, Chilean Antarctic
-
-
Manually annotated by BRENDA team
gene prtS8A
-
-
Manually annotated by BRENDA team
gene prtS8A
-
-
Manually annotated by BRENDA team
subtilisin J, Bacillus stearothermophilus NCIMB10278 gene expressed in Bacillus subtilis DB104/pZS101
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strains GS115 and KM71
-
-
Manually annotated by BRENDA team
KV71, KV22 and KV42
-
-
Manually annotated by BRENDA team
KV01 and KV54
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
an avirulent isolate
-
-
Manually annotated by BRENDA team
strain P1/7
C5VW36
UniProt
Manually annotated by BRENDA team
synthetic construct
-
-
-
Manually annotated by BRENDA team
gene ThSS45
UniProt
Manually annotated by BRENDA team
gene ThSS45
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(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
show the reaction diagram
-
-
-
-
-
(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
show the reaction diagram
-
-
-
-
-
(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
show the reaction diagram
-
-
-
-
-
67 kDa gamma-glutamyl transpeptidase + H2O
30 kDa gamma-glutamyl transpeptidase + ?
show the reaction diagram
synthetic construct
-
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
?
show the reaction diagram
-
-
-
-
?
acetyl-L-Ala-L-Ala-L-Ala-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
acetyl-L-Phe + ethanol
acetyl-L-Phe ethyl ester + H2O
show the reaction diagram
acetyl-L-Phe ethyl ester + H2O
acetyl-L-Phe + ethanol
show the reaction diagram
acetyl-L-Tyr + ethanol
acetyl-L-Tyr ethyl ester + H2O
show the reaction diagram
-
-
-
-
r
acetyl-L-Tyr ethyl ester + H2O
acetyl-L-Tyr + ethanol
show the reaction diagram
acid casein + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
Ala-Ala-Pro-Leu-4-nitroanilide + H2O
Ala-Ala-Pro-Leu + 4-nitroaniline
show the reaction diagram
-
low activity
-
-
?
Ala-Ala-Pro-Lys-4-nitroanilide + H2O
Ala-Ala-Pro-Lys + 4-nitroaniline
show the reaction diagram
-
low activity
-
-
?
Ala-Ala-Pro-Met-4-nitroanilide + H2O
Ala-Ala-Pro-Met + 4-nitroaniline
show the reaction diagram
-
low activity
-
-
?
Ala-Ala-Pro-Nle-4-nitroanilide + H2O
Ala-Ala-Pro-Nle + 4-nitroaniline
show the reaction diagram
-
low activity
-
-
?
Ala-Ala-Pro-Phe 4-nitroanilide + H2O
?
show the reaction diagram
Ala-Ala-Pro-Phe-4-nitroanilide + H2O
Ala-Ala-Pro-Phe + 4-nitroaniline
show the reaction diagram
-
low activity
-
-
?
Ala-Ala-Val-Ala-4-nitroanilide + H2O
Ala-Ala-Val-Ala + 4-nitroaniline
show the reaction diagram
-
low activity
-
-
?
azocasein + H2O
?
show the reaction diagram
Benzoyl-Arg ethyl ester + H2O
?
show the reaction diagram
benzoyl-L-Arg + ethanol
benzoyl-L-Arg ethyl ester + H2O
show the reaction diagram
-
-
-
-
r
Benzoyl-L-Arg ethyl ester + H2O
Benzoyl-L-Arg + ethanol
show the reaction diagram
Benzyloxycarbonyl-Ala-Ala-Leu 4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
-
Benzyloxycarbonyl-Gly-Gly-L-Leu-NH2 + H2O
?
show the reaction diagram
-
-
-
-
-
Benzyloxycarbonyl-Gly-L-Leu-NH2 + H2O
?
show the reaction diagram
-
-
-
-
-
Benzyloxycarbonyl-Gly-L-Tyr-NH2 + H2O
?
show the reaction diagram
-
-
-
-
-
Benzyloxycarbonyl-glycyl-L-tyrosinamide + H2O
?
show the reaction diagram
-
-
-
-
-
benzyloxycarbonyl-L-Ala ethyl ester + butanol
benzyloxycarbonyl-L-Ala butyl ester + ethanol
show the reaction diagram
-
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
show the reaction diagram
benzyloxycarbonyl-L-Asp methyl ester + serine amide
benzyloxycarbonyl-L-Asp-L-Ser-NH2 + methanol
show the reaction diagram
-
-
-
-
?
beta subunit of haemoglobin + H2O
?
show the reaction diagram
-
-
-
-
?
beta-casein + H2O
?
show the reaction diagram
Bovine serum albumin + H2O
?
show the reaction diagram
bovine serum albumin+ H2O
?
show the reaction diagram
-
poor substrate in native form, but can be digested in heat-denatured form
-
-
?
Carboxybenzoyl-Gly-Ala-NH2 + H2O
Carboxybenzoyl-Gly-Ala + NH3
show the reaction diagram
-
subtilisin BPN'
subtilisin BPN'
-
Carboxybenzoyl-Gly-Leu-NH2 + H2O
Carboxybenzoyl-Gly-Leu + NH3
show the reaction diagram
-
subtilisin BPN'
subtilisin BPN'
-
Carboxybenzoyl-Gly-Pro-Leu-Gly-Pro-OH + H2O
Carboxybenzoyl-Gly-Pro-Leu + Gly-Pro-OH
show the reaction diagram
-
subtilisin BPN'
subtilisin BPN'
-
casein + H2O
?
show the reaction diagram
chicken-feather keratin + H2O
?
show the reaction diagram
-
-
-
-
?
chitin + H2O
?
show the reaction diagram
Clupein + H2O
?
show the reaction diagram
-
-
-
-
-
Collagen + H2O
?
show the reaction diagram
cuticle + H2O
?
show the reaction diagram
Cytochrome c + H2O
?
show the reaction diagram
D-Val-Leu-Lys p-nitroanilide + H2O
D-Val-Leu-Lys + p-nitroaniline
show the reaction diagram
-
-
-
?
eglin-c + H2O
?
show the reaction diagram
-
proteinase inhibitor, subtilisin DY hydrolyses the peptide bond between residues 45 and 46 in the reactive centre of eglin-c
-
?
Elastin + H2O
?
show the reaction diagram
ethyl 2-(4-ethylphenoxy)propionate + butanol
butyl 2-(4-ethylphenoxy)propanoate + propanol
show the reaction diagram
-
in isooctane, preferential use of S-enantiomer. Comparison with enantioselectivity in water and DMSO
-
-
?
Fibrin + H2O
?
show the reaction diagram
Fibrinogen + H2O
?
show the reaction diagram
Gelatin + H2O
?
show the reaction diagram
Glp-Ala-Ala-Leu-p-nitroanilide + H2O
?
show the reaction diagram
glutaryl-Ala-Ala-Pro-Leu-p-nitroanilide + H2O
glutaryl-Ala-Ala-Pro-Leu + p-nitroaniline
show the reaction diagram
relative hydrolysis rate is 22%
-
-
?
Hammarsten casein + H2O
?
show the reaction diagram
Hemoglobin + H2O
?
show the reaction diagram
Human fibrinogen + H2O
?
show the reaction diagram
-
fibrinolytic activity is determined using the fibrin plate method
-
-
?
human fibronectin + H2O
?
show the reaction diagram
-
-
-
-
?
insoluble elastin + H2O
?
show the reaction diagram
-
-
-
-
?
kappa casein + H2O
?
show the reaction diagram
-
purified caseins from animal's milk from cow, sheep, goat and water buffalo used as substrate for subtilisin
-
?
Keratin + H2O
?
show the reaction diagram
KOH chitin + H2O
?
show the reaction diagram
L-Ala-L-Ala-L-Ala-L-Ala-L-Pro-L-Phe + H2O
?
show the reaction diagram
-
-
-
-
?
L-Ala-L-Ala-L-Phe-L-Ala-L-Ala-L-Phe + H2O
?
show the reaction diagram
-
-
-
-
?
L-Ala-L-Ala-L-Pro-L-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
L-Ala-L-Ala-L-Pro-L-Phe + H2O
?
show the reaction diagram
-
-
-
-
?
L-Ala-L-Ala-L-Val-L-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
L-Lys-L-His-L-Asp-L-Arg-L-Lys-L-Asp + H2O
?
show the reaction diagram
-
-
-
-
?
L-Phe-L-Ala-L-Ala-L-Phe + H2O
?
show the reaction diagram
-
-
-
-
?
L-phenylalanine-isopropylester + H2O
L-phenylalanine + isopropanol
show the reaction diagram
-
-
-
-
-
L-Tyr-L-Val-L-Ala-L-Asp + H2O
?
show the reaction diagram
-
-
-
-
?
lactate dehydrogenase + H2O
?
show the reaction diagram
-
poor substrate in native form, but can be digested in heat-denatured form
-
-
?
malate dehydrogenase + H2O
?
show the reaction diagram
-
poor substrate in native form, but can be digested in heat-denatured form
-
-
?
MeO-succinyl-Ala-Ala-Phe 4-nitroanilide + H2O
?
show the reaction diagram
methoxysuccinyl-Ala-Ile-Pro-Met-p-nitroanilide + H2O
methoxysuccinyl-Ala-Ile-Pro-Met + p-nitroaniline
show the reaction diagram
is the most favorable substrate, relative hydrolysis rate is 100%
-
-
?
methyl mandelate + butanol
butyl mandelate + methanol
show the reaction diagram
-
in isooctane, preferential use of S-enantiomer. Comparison with enantioselectivity in water and DMSO
-
-
?
N-Acetyl-Ala methyl ester + H2O
?
show the reaction diagram
-
subtilisin BPN'
-
-
-
N-Acetyl-Gly ethyl ester + H2O
?
show the reaction diagram
-
subtilisin BPN'
-
-
-
N-Acetyl-L-norvaline ethyl ester + H2O
?
show the reaction diagram
-
subtilisin BPN'
-
-
-
N-acetyl-L-phenylalanine ethyl ester
?
show the reaction diagram
-
-
-
-
?
N-acetyl-L-phenylalanine ethyl ester + 1-butanol
?
show the reaction diagram
-
transesterification catalyzed by poly(ethylene glycol)-modified subtilisin
-
-
?
N-acetyl-L-phenylalanine ethyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
N-Acetyl-Leu methyl ester + H2O
?
show the reaction diagram
-
subtilisin BPN'
-
-
-
N-Acetyl-Lys methyl ester + H2O
?
show the reaction diagram
-
subtilisin BPN'
-
-
-
N-Acetyl-Phe ethyl ester + H2O
?
show the reaction diagram
-
subtilisin BPN'
-
-
-
N-Acetyl-Phe methyl ester + H2O
?
show the reaction diagram
N-Acetyl-Trp ethyl ester + H2O
?
show the reaction diagram
-
subtilisin BPN'
-
-
-
N-Acetyl-Trp methyl ester + H2O
?
show the reaction diagram
N-Acetyl-Tyr ethyl ester + H2O
?
show the reaction diagram
N-acetyl-Tyr ethyl ester + H2O
N-acetyl-Tyr + ethanol
show the reaction diagram
-
-
-
?
N-Acetyl-Tyr methyl ester + H2O
?
show the reaction diagram
N-Acetyl-Val methyl ester + H2O
?
show the reaction diagram
N-acetylglucosamine + H2O
?
show the reaction diagram
N-CBZ-Gly-Gly-Leu p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
N-methoxysuccinyl-Ala-Ala-Pro-Val-4-nitroanilide + H2O
N-methoxysuccinyl-Ala-Ala-Pro-Val + 4-nitroanilide
show the reaction diagram
-
-
-
-
?
N-methoxysuccinyl-Ala-Ala-Pro-Val-p-nitroanilide + H2O
N-methoxysuccinyl-Ala-Ala-Pro-Val + p-nitroaniline
show the reaction diagram
N-Succ-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-Succ-Ala-Ala-Pro-Phe + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
N-succinyl-Ala-Ala-Pro-Leu-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Leu + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
N-succinyl-Ala-Ala-Pro-Met-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Met + p-nitroaniline
show the reaction diagram
relative hydrolysis rate is 39%
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
show the reaction diagram
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
show the reaction diagram
N-succinyl-Ala-Ala-Val-Ala-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Val-Ala + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
N-succinyl-L-Ala-L-Ala-L-L-Ala-4-nitroanilide + H2O
?
show the reaction diagram
N-succinyl-L-Ala-L-Ala-L-Pro-L-Leu-4-nitroanilide + H2O
?
show the reaction diagram
N-succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-nitroanilide + H2O
?
show the reaction diagram
N-succinyl-L-Ala-L-Ala-L-Val-4-nitroanilide + H2O
?
show the reaction diagram
N-tosyl-L-Arg methyl ester + H2O
N-tosyl-L-Arg + methanol
show the reaction diagram
N-trans-cinnamoyl imidazole + H2O
(E)-cinnamate + imidazole
show the reaction diagram
-
-
-
-
?
Nalpha-benzoyl-DL-Arg-4-nitroanilide + H2O
Nalpha-benzoyl-DL-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
Nalpha-Benzoyl-L-Arg ethyl ester + H2O
?
show the reaction diagram
-
-
-
-
-
Oxidized insulin B-chain + H2O
?
show the reaction diagram
oxidized insulin chain B + H2O
?
show the reaction diagram
-
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
show the reaction diagram
-
catalyzed by native subtilisin
-
-
?
peanut flour + H2O
?
show the reaction diagram
synthetic construct
-
6 h alcalase hydrolysate
-
-
?
peptidyl-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
?
Phe-Ala-Ala-Phe-4-nitroanilide + H2O
Phe-Ala-Ala-Phe + 4-nitroaniline
show the reaction diagram
-
highly preferred substrate
-
-
?
porcine brain tubulin + H2O
peptides
show the reaction diagram
-
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
-
-
?
proCSF + H2O
CSF
show the reaction diagram
proPhrA + H2O
PhrA
show the reaction diagram
-
-
-
-
?
sec-phenethyl alcohol + vinyl butyrate
?
show the reaction diagram
-
-
-
-
?
serum albumin + H2O
?
show the reaction diagram
-
-
-
-
?
silk fibroin + H2O
?
show the reaction diagram
-
-
-
-
?
Spirulina platensis powder + H2O
?
show the reaction diagram
-
-
-
-
?
strobilurin fungicide + H2O
?
show the reaction diagram
-
-
-
-
?
Suc-Ala-Ala-Pro-Phe-4-methyl-coumaryl-7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
Suc-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
Suc-Ala-Ala-Pro-Phe + 4-nitroaniline
show the reaction diagram
succinyl-AAPA-p-nitroanilide + H2O
?
show the reaction diagram
succinyl-AAPE-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
?
succinyl-AAPF-p-nitroanilide + H2O
succinyl-AAPF + p-nitroaniline
show the reaction diagram
succinyl-AAPF-p-nitroanilide + H2O
succinyl-alanyl-alanyl propyl-phenylalanine
show the reaction diagram
-
-
-
?
succinyl-AAPR-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
?
Succinyl-Ala-Ala 4-nitroanilide + H2O
?
show the reaction diagram
Succinyl-Ala-Ala-Ala 4-nitroanilide + H2O
?
show the reaction diagram
succinyl-Ala-Ala-Ala-Ala-Ala-p-nitroanilide + H2O
succinyl-AAAAA + p-nitroaniline
show the reaction diagram
-
-
-
?
succinyl-Ala-Ala-Ala-p-nitroanilide + H2O
succinyl-AAA + p-nitroaniline
show the reaction diagram
-
-
-
?
succinyl-Ala-Ala-p-nitroanilide + H2O
succinyl-Ala-Ala + p-nitroaniline
show the reaction diagram
-
-
-
?
succinyl-Ala-Ala-Pro-Ala-p-nitroanilide + H2O
succinyl-AAPA + p-nitroaniline
show the reaction diagram
-
-
-
?
succinyl-Ala-Ala-Pro-Leu-p-nitroanilide + H2O
succinyl-AAPL + p-nitroaniline
show the reaction diagram
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
show the reaction diagram
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe-7-amido-4-methylcoumarin + H2O
succinyl-Ala-Ala-Pro-Phe + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
show the reaction diagram
-
-
-
-
?
succinyl-Ala2-Phe-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
?
succinyl-L-Ala-L-Ala-L-Ala-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-L-Ala-L-Ala-L-Phe-7-amido-4-methylcoumarin + H2O
succinyl-L-Ala-L-Ala-L-Phe + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
succinyl-L-Ala-L-Ala-L-Pro-Gly-4-nitroanilide + H2O
succinyl-L-Ala-L-Ala-L-Pro-Gly + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
succinyl-L-Ala-L-Ala-L-Pro-L-Ala-4-nitroanilide + H2O
succinyl-L-Ala-L-Ala-L-Pro-L-Ala + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
succinyl-L-Ala-L-Ala-L-Pro-L-Lys-4-nitroanilide + H2O
succinyl-L-Ala-L-Ala-L-Pro-L-Lys + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
succinyl-L-Ala-L-Ala-L-Pro-L-Met-4-nitroanilide + H2O
succinyl-L-Ala-L-Ala-L-Pro-L-Met + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-nitroanilide + H2O
succinyl-L-Ala-L-Ala-L-Pro-L-Phe + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
succinyl-L-Ala-L-Ala-L-Pro-L-Tyr-4-nitroanilide + H2O
succinyl-L-Ala-L-Ala-L-Pro-L-Tyr + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
Succinyl-Leu-Leu-Val-Tyr 4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
succinyl-Phe-Ala-Ala-Phe-p-nitroanilide + H2O
succinyl-Phe-Ala-Ala-Phe + p-nitroaniline
show the reaction diagram
-
-
-
?
Toluenesulfonyl-Arg methyl ester + H2O
?
show the reaction diagram
-
subtilisin Carlsberg, subtilisin Novo
-
-
-
type I keratin + H2O
?
show the reaction diagram
-
-
-
-
?
ubiquitin + H2O
?
show the reaction diagram
Urea-denatured hemoglobin + H2O
?
show the reaction diagram
vinyl butyrate + H2O
?
show the reaction diagram
-
-
-
-
?
Z-Ala-Ala-Leu-OCH3 + H2O
?
show the reaction diagram
-
-
-
-
?
Z-Ala-Ala-Leu-OMe + Phe-p-nitroanilide
Z-Ala-Ala-Leu-Phe-p-nitroanilide + methanol
show the reaction diagram
-
-
-
-
?
Z-Ala-Ala-Leu-p-nitroanilide + H2O
?
show the reaction diagram
Z-Ala-Phe-OMe + H2O
Z-Ala-Phe-NH2 + methanol
show the reaction diagram
-
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 30C 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
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
biosynthesis of subtilisin requires participation of an N-terminal prodomain
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cd2+
-
stabilizes
Cl-
-
treatment with CsCl increases the activity several fold. Two Cl- ions are close to the mouth of the active site cleft, where they may affect catalysis
Cs+
-
treatment with CsCl increases the activity several fold. Two Cs+ ions are close to the mouth of the active site cleft, where they may affect catalysis
KCl
-
increases enzymatic activity somewhat, while choline-Cl has a larger effect
Sr2+
-
increases thermostability, but to a significantly lower degree than Ca2+
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(dimethylamino)-1-naphthalenesulfonyl fluoride
-
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 37C and pH of 7.5, 0.1 mM inhibits prosubtilisin JB1 by 40%
1,4-dioxane
2,2'-[[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphoryl]bis(oxybenzene-4,1-diyl)]diacetic acid
-
-
2,2'-[[(1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphoryl]bis(oxybenzene-4,1-diyl)]diacetic acid
-
-
2,2'-[[(1-[[1-(tert-butoxycarbonyl)-L-prolyl]amino]-3-methylbutyl)phosphoryl]bis(oxybenzene-3,1-diyl)]diacetic acid
-
-
2-phenylethaneboronic acid
-
-
2-phenylethanesulfonic acid
-
-
3,4-dichloroisocoumarin
-
-
4-(2-aminoethyl)-benzenesulfonyl fluoride
-
-
4-(2-aminoethyl)benzenesulfonyl fluoride
-
-
4-(4'-Aminophenylazo)phenylarsonic acid
-
-
4-bromophenacyl bromide
-
-
5-Dimethylaminonaphthalene-1-sulfonate
-
circular-dichroism and fluorescence studies of 5-dimethylaminonaphthalene-1-sulfonyl derivative of subtilisin indicate a closely similar structure to that of native subtilisin
acetone
-
-
acetonitrile
-
-
alpha2-Macroglobulin
-
inhibits alkaline proteolytic activity of purified Arp by 80%
-
antipain
Aprotinin
Benzamide
-
-
benzeneboronic acid
-
-
Benzenesulfonic acid
-
-
Benzyloxycarbonyl-(Ala)n-PheCH2Cl
-
benzyloxycarbonyl-(Ala)2-PheCH2Cl is the best inhibitor
Benzyloxycarbonyl-Ala-XaaCH2Cl
-
Xaa : Gly, Val, Ala, Leu, Phe
Benzyloxycarbonyl-L-phenylalanylbromomethane
-
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
-
-
bis(2,3-dimethylphenyl) (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
-
-
bis(2,3-dimethylphenyl) (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
-
-
bis(2,5-dimethylphenyl) (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
-
-
bis(2-methylphenyl) (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
-
-
bis(2-methylphenyl) (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
-
-
bis(3,4,5-trimethylphenyl) (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
-
-
bis(3,4,5-trimethylphenyl) (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
-
-
bis(3,4-dimethylphenyl) (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
-
-
bis(3,4-dimethylphenyl) (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
-
-
bis(3-chlorophenyl) (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
-
-
bis(3-chlorophenyl) (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
-
-
bis(3-methoxyphenyl) (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
-
-
bis(4-chlorophenyl) (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
-
-
bis(4-chlorophenyl) (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
-
-
bis(4-ethylphenyl) (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
-
-
bis(4-ethylphenyl) (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
-
-
bis(4-methoxyphenyl) (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
-
-
bis(4-methylphenyl) (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
-
-
bis(4-tert-butylphenyl) (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
-
-
bis(4-tert-butylphenyl) (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
-
-
bis[4-(methylsulfonyl)phenyl] (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
-
-
bis[4-(propan-2-yl)phenyl] (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
-
-
bis[4-(propan-2-yl)phenyl] (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
-
-
bis[4-(sulfanylmethyl)phenyl] (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
-
-
bis[4-(sulfanylmethyl)phenyl] (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
-
-
Brij 35
at 37C 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
-
subtilisin BPN'
Ca2+
at 37C and pH of 7.5, 1 mM reduces prosubtilisin JB1 relative activity to 57% and 5 mM reduces prosubtilisin JB1 relative activity to 45%
carbon
Chiral amine- and aminoalcohol-derivatives
-
-
-
chymostatin
Chymotrypsin I inhibitor from potato
-
subtilisin Carlsberg, subtilisin BPN'
-
chymotrypsin inhibitor 2
-
-
-
chymotrypsin inhibitor 2 mutant M59A
-
-
-
chymotrypsin inhibitor 2 mutant M59F
-
-
-
chymotrypsin inhibitor 2 mutant M59G
-
-
-
chymotrypsin inhibitor 2 mutant M59K
-
-
-
chymotrypsin inhibitor 2 mutant M59Y
-
-
-
chymotrypsin inhibitor 2 mutant Y61A
-
-
-
Co2+
at 37C 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
synthetic construct
-
Kazal-type inhibitor from the hepatopancreas of the Carcinoscorpius rotundicauda, potently inhibits subtilisin
-
Cyclohexanol
-
-
cyclohexanone
-
-
diisopropyl fluorophosphate
-
-
diisopropylphosphofluoridate
-
-
Dipeptidyl chloromethyl ketones
-
-
diphenyl (1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)phosphonate
-
-
diphenyl (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
-
-
duck ovomucoid
-
-
-
E-64
at 37C and pH of 7.5, 0.1 mM inhibits prosubtilisin JB1 by 31%
E-64c
at 37C and pH of 7.5, 0.1 mM inhibits prosubtilisin JB1 by 25%
Eglin c
-
-
EGTA
at 37C and pH of 7.5, 0.1 mM inhibits prosubtilisin JB1 by 34%
Elastatinol
-
weak
EPI1a
-
four-cysteine atypical Kazal-domain of protease inhibitor EPI1 from Phytophthora infestans. 80% inhibition at 0.00015 mM
-
EPI1b
-
typical Kazal-domain of protease inhibitor EPI1 from Phytophthora infestans, little inhibitory effect
-
fungal protease inhibitor F
-
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
-
guanidine hydrochloride
-
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
-
-
Hg+
at 37C 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
-
noncompetitive inhibition
-
human proteinase inhibitor 9
-
PI9, serine proteinase inhibitor
-
Hydrocinnamamide
-
-
Hydrocinnamate
-
-
indole
-
-
Inhibitor from Dolichos biflorus
-
purification and properties
-
Inhibitor from egg white
Inhibitor from seeds of Canavalia lineata
Inhibitor from seeds of Setaria italica
-
purification and characterization
-
Inhibitor from Streptomyces sp.
-
-
-
Inhibitor from Streptomyces virginiae
-
primary structure
-
Inhibitor from Vigna unguiculata subsp. cylindrica
Inhibitor of Amaranthus caudatus seeds
Inhibitor of trypsin from soybean
-
-
-
iodoacetamide
-
-
K+
at 37C 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
-
-
Leupeptin
-
inhibits the enzymatic activity by 20%
Methaneboronic acid
-
-
Mg2+
at 37C 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
-
-
N-(tert-butoxycarbonyl)-L-valyl-N-(1-[bis[4-(sulfanylmethyl)phenoxy]phosphoryl]-2-phenylethyl)-L-prolinamide
-
-
N-(tert-butoxycarbonyl)-L-valyl-N-[1-(diphenoxyphosphoryl)-2-phenylethyl]-L-prolinamide
-
-
N-(tert-butoxycarbonyl)-L-valyl-N-[1-[bis(3,4,5-trimethylphenoxy)phosphoryl]-3-methylbutyl]-L-prolinamide
-
-
N-(tert-butoxycarbonyl)-L-valyl-N-[1-[bis(4-methoxyphenoxy)phosphoryl]-3-methylbutyl]-L-prolinamide
-
-
N-(tert-butoxycarbonyl)-L-valyl-N-[1-[bis(4-tert-butylphenoxy)phosphoryl]-3-methylbutyl]-L-prolinamide
-
-
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
-
product inhibition
N-benzyloxycarbonyl-Ala-Pro-Phe-chloromethyl ketone
-
synthetic inhibitor
N-ethylmaleimide
at 37C and pH of 7.5, 0.1 mM inhibits prosubtilisin JB1 by 15%
N-tosyl-L-phenylalanyl chloromethyl ketone
-
-
N1-18[ISP]
-
synthetic peptide corresponding to the N-terminal extension behaves as a mixed noncompetitive inhibitor of active ISP
nitrogen
p-Arsanilate
-
-
p-chloromercuribenzoate
-
partial inhibition
p-Nitrophenylarsonate
-
-
p-Tolylarsonate
-
-
Pepstatin
-
almost completely inhibits acid proteolytic activity, does not inhibit alkaline proteolytic activity of purified Arp
pepstatin A
at 37C and pH of 7.5, 0.1 mM inhibits prosubtilisin JB1 by 48%
Peptidyl chloromethyl ketones
-
-
Phenol
-
-
Phenylarsonate
-
-
phenylmethanesulfonyl fluoride
phenylmethylsulfonyl fluoride
Phenylmethylsulphonyl fluoride
-
-
Potato extract
-
subtilisin BPN'
-
propeptide
-
inhibition in a concentration-dependent manner. Wild-type propeptide is more potent than G56W-, G56S- and G56E-propeptide
-
RNA aptamer
-
-
-
Sodium dodecyl sulfate
Suc-Val-Pro-PheP(OPh)2
-
-
tert-butyl (2S)-2-([1-[bis(2-methylphenoxy)phosphoryl]-3-methylbutyl]carbamoyl)pyrrolidine-1-carboxylate
-
-
tert-butyl (2S)-2-([1-[bis(3,4,5-trimethylphenoxy)phosphoryl]-3-methylbutyl]carbamoyl)pyrrolidine-1-carboxylate
-
-
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
-
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
-
tosyl-Phe chloromethyl ketone
Triton X-100
at 37C 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 37C and pH of 7.5, 0.01% reduces prosubtilisin JB1 relative activity to 53% and 0.05% reduces prosubtilisin JB1 relative activity to 70%
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
choline
-
increases the enzyme activity
dichloroisocoumarin
-
-
methyl-beta-cyclodextrin
-
activates and enhances the enantioselectivity of subtilisin C. mainly by prevention of structural perturbation during the initial lyophilization process. Minor contributions to increased activity likely stem from other factors, such as, reduction of possible mass transport limitations and changes in enzyme dynamics. Enhanced activity and enantioselectivity is not caused by formation of cyclodextrinsubstrate or -product complexes
n-Propanol
-
subtilisin precipitated and rinsed with propanol yields higher transesterfication activity. About 10000times increase in initial rates in 1-butyl-3-methylimidazolium hexafluorophosphate over what is obtained with pH tuned lyophilized powders
OSP400
-
in the presence of 10 mM calcium the half-life of the enzyme at 60C increases by 6.06fold. Among modifiers used OSP400 is most effective in stabilizing the enzyme. Thermally induced unfolding is delayed
-
OSP70
-
in the presence of 10 mM calcium the half-life of the enzyme at 60C increases by 5.20fold. Thermally induced unfolding is delayed
-
poly(ethylene glycol)
-
poly(ethylene glycol)-modified subtilisin suspended in ionic liquids exhibits excellent catalytic performance while the native enzyme shows no activity
poly(ethyleneglycol)
-
presence of poly(ethyleneglycol) combined with trehalose during lyphilization does help in obtaining a more active enzyme preparation for catalysis in ionic liquids
polyglutaraldehyde
-
in the presence of 10 mM calcium the half-life of the enzyme at 60C increases by 2.92fold. Thermally induced unfolding is delayed
Toluene
-
poly(ethylene glycol)-modified subtilisin
[C2OC1mim][Tf2N]
-
poly(ethylene glycol)-modified subtilisin
-
[C2OHmim][Tf2N]
-
poly(ethylene glycol)-modified subtilisin
-
[Emim][Tf2N]
-
poly(ethylene glycol)-modified subtilisin shows good stability in [Emim][Tf2N], and maintains 80% of its initial activity after 60 h. Preferred medium for enzymatic reaction. Enzyme activity is much higher than in conventional organic solvents. Excellent activity is associated with unique properties such as hydrophobicity and high polarity
-
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.85
acetyl-L-Phe
-
30C, pH 8.0
0.22
acetyl-L-Phe ethyl ester
-
30C, pH 8.0
4
acetyl-L-Tyr
-
30C, pH 8.0
-
0.37
acetyl-L-Tyr ethyl ester
-
30C, pH 8.0
7 - 10
benzoyl-Arg ethyl ester
2.1
benzoyl-L-Arg ethyl ester
-
30C, pH 8.0
8.3
benzyloxycarbonyl-Gly-p-nitroanilide
-
pH 7.5, 20C, in presence and absence of DTT
0.0054
benzyloxycarbonyl-L-Ala-L-Ala-L-Leu-4-nitroanilide
-
-
0.059
casein
-
pH 10, 45C, 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
0.2 - 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
-
37C, 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 - 0.0037
Suc-Ala-Ala-Pro-Phe-4-nitroanilide
0.07 - 1
Suc-Ala-Ala-Pro-Phe-p-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
0.71 - 0.79
succinyl-Ala-Ala-Phe 4-nitroanilide
0.13
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, 25C
0.45
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-nitroanilide
-
mutant Y217L, pH 8.3, 25C
0.33
succinyl-L-Asp-L-Val-L-Arg-L-Ala-L-Phe-7-amido-4-methylcoumarin
-
mutant Y217L, pH 8.3, 25C
30 - 40
toluenesulfonyl-Arg methyl ester
0.09
Urea-denatured hemoglobin
-
30C, pH 8.0
-
0.14 - 4
Z-Ala-Ala-Leu-p-nitroanilide
additional information
additional information