Information on EC 3.4.21.25 - cucumisin

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.21.25
-
RECOMMENDED NAME
GeneOntology No.
cucumisin
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
hydrolysis of proteins with broad specificity
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
endopeptidase
-
CAS REGISTRY NUMBER
COMMENTARY hide
82062-89-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Kachri fruit, Cucumis trigonus Roxburghi
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-Ala-Ala-Ala-p-nitroanilide + H2O
?
show the reaction diagram
-
1% of the activity with benzyloxycarbonyl-Tyr-nitrophenyl ester
-
-
?
Ala-Ala-Pro-Ala-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
Ala-Ala-Pro-Glu-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
Ala-Ala-Pro-Gly-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
Ala-Ala-Pro-L-diaminopropionic acid-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
Ala-Ala-Pro-Leu-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
Ala-Ala-Pro-Lys-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
Ala-Ala-Pro-Phe-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
Ala-Ala-Pro-Val-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-mating factor + H2O
?
show the reaction diagram
-
cleaves at one site, Glu-Leu
-
-
?
Angiotensin I + H2O
?
show the reaction diagram
-
cleaves at two sites, Tyr-Ile and Phe-His
-
-
?
benzoyl-Tyr-ethyl ester + H2O
benzoyl-Tyr + ethanol
show the reaction diagram
-
24% of the activity with benzyloxycarbonyl-Tyr-nitrophenyl ester
-
-
?
benzyloxycarbonyl-Ala-Ala-Ala-SCH2C6H5 + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Arg-SCH2C6H5 + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Asp-SCH2C6H5 + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Glu-SCH2C6H5 + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Leu-SCH2C6H5 + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Ala-Ala-norleucine-SCH2C6H5 + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Ala-Ala-norvaline-SCH2C6H5 + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Phe-SCH2C6H5 + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Ser-SCH2C6H5 + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Val-SCH2C6H5 + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Ala-Asn-SCH2C6H5 + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Glu-Phe + H2O
benzyloxycarbonyl-Glu + Phe
show the reaction diagram
-
weakly hydrolyzed
-
-
?
Benzyloxycarbonyl-Glu-Tyr + H2O
Benzyloxycarbonyl-Glu + Tyr
show the reaction diagram
benzyloxycarbonyl-Tyr-4-nitrophenyl ester + H2O
benzyloxycarbonyl-Tyr + 4-nitrophenyl ester
show the reaction diagram
-
best synthetic substrate
-
-
?
beta-conglycinin storage protein + H2O
?
show the reaction diagram
-
-
-
?
casein + H2O
?
show the reaction diagram
Cytochrome c + H2O
?
show the reaction diagram
-
initial cleavage site, Glu-Lys and Ala-Ala
-
-
?
delta sleep-inducing peptide + H2O
?
show the reaction diagram
-
cleaves at one site, Ala-Ser
-
-
?
glutaryl-Ala-Ala-Pro-Leu-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
glutaryl-L-alanyl-L-alanyl-L-prolyl-L-leucyl-4-nitroanilide + H2O
glutaryl-L-alanyl-L-alanyl-L-prolyl-L-leucine + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
insulin + H2O
?
show the reaction diagram
-
initial cleavage site, Gln-His
-
-
?
Insulin B-chain + H2O
?
show the reaction diagram
KVEKEESEE + H2O
KVEKE + ESEE
show the reaction diagram
-
-
-
?
L-alanyl-4-nitroanilide + H2O
L-alanine + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
L-alanyl-L-alanyl-4-nitroanilide + H2O
L-alanyl-L-alanine + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
L-gamma-glutamyl-4-nitroanilide + H2O
L-glutamate + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
L-leucyl-4-nitroanilide + H2O
L-leucine + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
Leu-Leu-Leu-Leu-Pro-Glu-Ala-Leu + H2O
Leu-Leu-Leu-Leu-Pro-Glu + Ala-Leu
show the reaction diagram
-
-
-
?
Leu-Leu-Leu-Pro-Glu-Ala-Leu + H2O
Leu-Leu-Leu-Pro-Glu + Ala-Leu
show the reaction diagram
-
-
-
?
Leu-Leu-Pro-Ala-Ala-Leu + H2O
Leu-Leu-Pro-Ala + Ala-Leu
show the reaction diagram
-
-
-
?
Leu-Leu-Pro-Arg-Ala-Leu + H2O
Leu-Leu-Pro-Arg + Ala-Leu
show the reaction diagram
-
low activity
-
?
Leu-Leu-Pro-Asn-Ala-Leu + H2O
Leu-Leu-Pro-Asn + Ala-Leu
show the reaction diagram
-
-
-
?
Leu-Leu-Pro-Asp-Ala-Leu + H2O
Leu-Leu-Pro-Asp + Ala-Leu
show the reaction diagram
-
-
-
?
Leu-Leu-Pro-Gln-Ala-Leu + H2O
Leu-Leu-Pro-Gln + Ala-Leu
show the reaction diagram
-
-
-
?
Leu-Leu-Pro-Glu-Ala + H2O
Leu-Leu-Pro-Glu + Ala
show the reaction diagram
-
low activity
-
?
Leu-Leu-Pro-Glu-Ala-Leu + H2O
Leu-Leu-Pro-Glu + Ala-Leu
show the reaction diagram
-
low activity
-
?
Leu-Leu-Pro-Glu-Ala-Leu-Leu + H2O
Leu-Leu-Pro-Glu + Ala-Leu-Leu
show the reaction diagram
-
-
-
?
Leu-Leu-Pro-Glu-Ala-Leu-Leu-Leu + H2O
Leu-Leu-Pro-Glu + Ala-Leu-Leu-Leu
show the reaction diagram
-
-
-
?
Leu-Leu-Pro-Glu-Glu-Leu + H2O
Leu-Leu-Pro-Glu + Glu-Leu
show the reaction diagram
-
low activity
-
?
Leu-Leu-Pro-Glu-Gly-Leu + H2O
Leu-Leu-Pro-Glu + Gly-Leu
show the reaction diagram
-
-
-
?
Leu-Leu-Pro-Glu-Lys-Leu + H2O
Leu-Leu-Pro-Glu + Lys-Leu
show the reaction diagram
-
-
-
?
Leu-Leu-Pro-Glu-Phe-Leu + H2O
Leu-Leu-Pro-Glu + Phe-Leu
show the reaction diagram
-
low activity
-
?
Leu-Leu-Pro-Glu-Ser-Leu + H2O
Leu-Leu-Pro-Glu + Ser-Leu
show the reaction diagram
-
-
-
?
Leu-Leu-Pro-His-Ala-Leu + H2O
Leu-Leu-Pro-His + Ala-Leu
show the reaction diagram
-
-
-
?
Leu-Leu-Pro-Leu-Ala-Leu + H2O
Leu-Leu-Pro-Leu + Ala-Leu
show the reaction diagram
-
-
-
?
Leu-Leu-Pro-Lys-Ala-Leu + H2O
Leu-Leu-Pro-Lys + Ala-Leu
show the reaction diagram
-
low activity
-
?
Leu-Leu-Pro-Met-Ala-Leu + H2O
Leu-Leu-Pro-Met + Ala-Leu
show the reaction diagram
Leu-Leu-Pro-Phe-Ala-Leu + H2O
Leu-Leu-Pro-Phe + Ala-Leu
show the reaction diagram
-
-
-
?
Leu-Leu-Pro-Ser-Ala-Leu + H2O
Leu-Leu-Pro-Ser + Ala-Leu
show the reaction diagram
-
-
-
?
Leu-Leu-Pro-Thr-Ala-Leu + H2O
Leu-Leu-Pro-Thr + Ala-Leu
show the reaction diagram
-
-
-
?
Leu-Leu-Pro-Trp-Ala-Leu + H2O
Leu-Leu-Pro-Trp + Ala-Leu
show the reaction diagram
-
-
-
?
Leu-Pro-Glu-Ala-Leu + H2O
Leu-Pro-Glu + Ala-Leu
show the reaction diagram
-
low activity
-
?
Myoglobin + H2O
?
show the reaction diagram
-
initial cleavage site, Asp-Ile and Glu-Ala
-
-
?
N-acetyl-L-alanyl-L-alanyl-alpha-azaalanine p-nitrophenyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
ovalbumin + H2O
?
show the reaction diagram
-
initial cleavage site, Asn-Ala
-
-
?
peptidyl-p-nitroanilide + H2O
p-nitroaniline + peptide
show the reaction diagram
-
-
-
-
?
Protein + H2O
?
show the reaction diagram
-
-
-
-
-
protein + H2O
hydrolyzed protein
show the reaction diagram
-
-
-
-
?
skim milk + H2O
?
show the reaction diagram
-
-
-
-
?
skim-milk powder + H2O
?
show the reaction diagram
-
milk-clotting activity, same activity as papain, EC 3.4.22.2 and half value of that of ficain, EC 3.4.22.3
-
-
?
Suc-Ala-Ala-Ala-p-nitroanilide + H2O
Suc-Ala-Ala-Ala + p-nitroaniline
show the reaction diagram
-
-
-
-
?
Suc-Ala-Ala-Pro-Leu-p-nitroanilide + H2O
Suc-Ala-Ala-Pro-Leu + p-nitroaniline
show the reaction diagram
-
-
-
-
?
Suc-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
Suc-Ala-Ala-Pro-Phe + p-nitroaniline
show the reaction diagram
-
-
-
-
?
succinyl-Ala-Ala-Ala-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-Ala-Ala-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-Ala-p-nitroanilide + H2O
succinyl-Ala + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
succinyl-Ala-Pro-Ala-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
superoxide dismutase + H2O
?
show the reaction diagram
-
initial cleavage site, His-Gly and Leu-Ala
-
-
?
TMA-lysozyme BrCN fragment + H2O
?
show the reaction diagram
-
cleaves at two sites, Cys-Lys and Arg-Gly
-
-
?
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
beta-conglycinin storage protein + H2O
?
show the reaction diagram
Q9ZTT3
-
-
-
?
Protein + H2O
?
show the reaction diagram
-
-
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-(2-aminoethyl)-benzenesulfonyl fluoride
-
17% inhibition by 1 mM; i.e. Pefabloc SC
5,5'-dithiobis(2-nitrobenzoic acid)
-
11% inhibition by 1 mM
acetonitrile
-
60.03% residual activity at 50% (v/v)
alpha2-Macroglobulin
-
38% inhibition by a concentration of 0.001 mM with casein as substrate, and 18% inhibition with succinyl-Ala-Pro-Ala-p-nitroanilide as substrate
-
ARA12 propeptide
-
-
-
butanol
-
68.24% residual activity at 50% (v/v)
chymostatin
-
2.45% residual activity at 5 mM
cucumisin propeptide
-
potent inhibitor of its mature enzyme, competitive inhibition
-
diisopropyl fluorophosphate
diisopropylfluorophosphate
-
2.34% residual activity at 1 mM
dioxane
-
65.35% residual activity at 50% (v/v)
ethanol
-
75.09% residual activity at 50% (v/v)
HgCl2
phenylmethylsulfonyl fluoride
-
5.12% residual activity at 5 mM
Phenylmethylsulfonylfluoride
-
strong inhibition
RSP1 propeptide
-
-
-
ZnCl2
-
11% inhibition by 2 mM
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.585
Ala-Ala-Pro-Ala-p-nitroanilide
-
-
0.355
Ala-Ala-Pro-Glu-p-nitroanilide
-
-
0.485
Ala-Ala-Pro-Gly-p-nitroanilide
-
-
1.11
Ala-Ala-Pro-L-diaminopropionic acid-p-nitroanilide
-
-
2.96
Ala-Ala-Pro-Leu-p-nitroanilide
-
-
0.826
Ala-Ala-Pro-Lys-p-nitroanilide
-
-
0.826
Ala-Ala-Pro-Phe-p-nitroanilide
-
-
0.595
Ala-Ala-Pro-Val-p-nitroanilide
-
-
3.33
benzoyl-Tyr-ethyl ester
-
-
2.02
Benzyloxycarbonyl-Glu-Tyr
-
-
1.25
glutaryl-Ala-Ala-Pro-Leu-p-nitroanilide
-
-
2.3
KVEKEESEE
pH and temperature not specified in the publication
0.002
L-alanyl-4-nitroanilide
-
at pH 8.0 and 37°C
0.004
L-alanyl-L-alanyl-4-nitroanilide
-
at pH 8.0 and 37°C
0.273
L-gamma-glutamyl-4-nitroanilide
-
at pH 8.0 and 37°C
0.093
L-leucyl-4-nitroanilide
-
at pH 8.0 and 37°C
1.8
Leu-Leu-Pro-Ala-Ala-Leu
-
pH 8.0, 37°C
3.9
Leu-Leu-Pro-Asn-Ala-Leu
-
pH 8.0, 37°C
5.6
Leu-Leu-Pro-Gln-Ala-Leu
-
pH 8.0, 37°C
2.8
Leu-Leu-Pro-Glu-Ala-Leu
-
pH 8.0, 37°C
3
Leu-Leu-Pro-Glu-Lys-Leu
-
pH 8.0, 37°C
0.8
Leu-Leu-Pro-Glu-Ser-Leu
-
pH 8.0, 37°C
2.9
Leu-Leu-Pro-His-Ala-Leu
-
pH 8.0, 37°C
0.7
Leu-Leu-Pro-Leu-Ala-Leu
-
pH 8.0, 37°C
4.1
Leu-Leu-Pro-Met-Ala-Leu
-
pH 8.0, 37°C
0.6
Leu-Leu-Pro-Phe-Ala-Leu
-
pH 8.0, 37°C
0.6
Leu-Leu-Pro-Ser-Ala-Leu
-
pH 8.0, 37°C
1.1
Leu-Leu-Pro-Thr-Ala-Leu
-
pH 8.0, 37°C
2.72
succinyl-Ala-Ala-Ala-p-nitroanilide
-
-
2.91
succinyl-Ala-Ala-p-nitroanilide
-
-
1
succinyl-Ala-Ala-Pro-Phe-p-nitroanilide
-
-
3.57
succinyl-Ala-p-nitroanilide
-
-
1.96
succinyl-Ala-Pro-Ala-p-nitroanilide
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.51
Ala-Ala-Pro-Ala-p-nitroanilide
Cucumis melo
-
-
1.21
Ala-Ala-Pro-Glu-p-nitroanilide
Cucumis melo
-
-
0.043
Ala-Ala-Pro-Gly-p-nitroanilide
Cucumis melo
-
-
0.603
Ala-Ala-Pro-L-diaminopropionic acid-p-nitroanilide
Cucumis melo
-
-
23.9
Ala-Ala-Pro-Leu-p-nitroanilide
Cucumis melo
-
-
0.295
Ala-Ala-Pro-Lys-p-nitroanilide
Cucumis melo
-
-
5.26
Ala-Ala-Pro-Phe-p-nitroanilide
Cucumis melo
-
-
0.022
Ala-Ala-Pro-Val-p-nitroanilide
Cucumis melo
-
-
0.22
benzoyl-Tyr-ethyl ester
Cucumis melo
-
-
0.767
benzyloxycarbonyl-Ala-Ala-Ala-SCH2C6H5
Cucumis melo
-
-
0.0833
benzyloxycarbonyl-Ala-Ala-Arg-SCH2C6H5
Cucumis melo
-
-
0.417
benzyloxycarbonyl-Ala-Ala-Asp-SCH2C6H5
Cucumis melo
-
-
0.0333
benzyloxycarbonyl-Ala-Ala-Glu-SCH2C6H5
Cucumis melo
-
-
0.8
benzyloxycarbonyl-Ala-Ala-Leu-SCH2C6H5
Cucumis melo
-
-
0.817
benzyloxycarbonyl-Ala-Ala-norleucine-SCH2C6H5
Cucumis melo
-
-
1.13
benzyloxycarbonyl-Ala-Ala-norvaline-SCH2C6H5
Cucumis melo
-
-
0.317
benzyloxycarbonyl-Ala-Ala-Phe-SCH2C6H5
Cucumis melo
-
-
0.9
benzyloxycarbonyl-Ala-Ala-Ser-SCH2C6H5
Cucumis melo
-
-
0.167
benzyloxycarbonyl-Ala-Ala-Val-SCH2C6H5
Cucumis melo
-
-
0.517
benzyloxycarbonyl-Ala-Asn-SCH2C6H5
Cucumis melo
-
-
2.2
benzyloxycarbonyl-Tyr-nitrophenyl ester
Cucumis melo
-
-
-
5.9
glutaryl-Ala-Ala-Pro-Leu-p-nitroanilide
Cucumis melo
-
-
32.13
L-alanyl-4-nitroanilide
Ficus religiosa
-
at pH 8.0 and 37°C
25.48
L-alanyl-L-alanyl-4-nitroanilide
Ficus religiosa
-
at pH 8.0 and 37°C
207.8
L-gamma-glutamyl-4-nitroanilide
Ficus religiosa
-
at pH 8.0 and 37°C
749.7
L-leucyl-4-nitroanilide
Ficus religiosa
-
at pH 8.0 and 37°C
14
Leu-Leu-Pro-Ala-Ala-Leu
Cucumis melo
-
pH 8.0, 37°C
98
Leu-Leu-Pro-Asn-Ala-Leu
Cucumis melo
-
pH 8.0, 37°C
162
Leu-Leu-Pro-Gln-Ala-Leu
Cucumis melo
-
pH 8.0, 37°C
5
Leu-Leu-Pro-Glu-Ala-Leu
Cucumis melo
-
pH 8.0, 37°C
4
Leu-Leu-Pro-Glu-Lys-Leu
Cucumis melo
-
pH 8.0, 37°C
7
Leu-Leu-Pro-Glu-Ser-Leu
Cucumis melo
-
pH 8.0, 37°C
59
Leu-Leu-Pro-His-Ala-Leu
Cucumis melo
-
pH 8.0, 37°C
20
Leu-Leu-Pro-Leu-Ala-Leu
Cucumis melo
-
pH 8.0, 37°C
177
Leu-Leu-Pro-Met-Ala-Leu
Cucumis melo
-
pH 8.0, 37°C
5
Leu-Leu-Pro-Phe-Ala-Leu
Cucumis melo
-
pH 8.0, 37°C
3
Leu-Leu-Pro-Ser-Ala-Leu
Cucumis melo
-
pH 8.0, 37°C
27
Leu-Leu-Pro-Thr-Ala-Leu
Cucumis melo
-
pH 8.0, 37°C
0.013
succinyl-Ala-Ala-Ala-p-nitroanilide
Cucumis melo
-
-
0.007
succinyl-Ala-Ala-p-nitroanilide
Cucumis melo
-
-
4.17
succinyl-Ala-Ala-Pro-Phe-p-nitroanilide
Cucumis melo
-
-
0.002
succinyl-Ala-p-nitroanilide
Cucumis melo
-
-
0.31
succinyl-Ala-Pro-Ala-p-nitroanilide
Cucumis melo
-
-
additional information
additional information
Cucumis melo
-
turnover number is pH-dependent and increases by a factor 6 upon going from pH 5 to pH 6
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.14
KVEKEESEE
Glycine max
Q9ZTT3
pH and temperature not specified in the publication
202344
13910
L-alanyl-4-nitroanilide
Ficus religiosa
-
at pH 8.0 and 37°C
81539
6888
L-alanyl-L-alanyl-4-nitroanilide
Ficus religiosa
-
at pH 8.0 and 37°C
202345
749.7
L-gamma-glutamyl-4-nitroanilide
Ficus religiosa
-
at pH 8.0 and 37°C
202346
422.2
L-leucyl-4-nitroanilide
Ficus religiosa
-
at pH 8.0 and 37°C
81538
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000062
ARA12 propeptide
-
in 150 mM sodium phosphate buffer, pH 7.5 containing 0.2 M NaCl, at 30°C
-
0.0000062
cucumisin propeptide
-
in 150 mM sodium phosphate buffer, pH 7.5 containing 0.2 M NaCl, at 30°C
-
0.0001
RSP1 propeptide
-
in 150 mM sodium phosphate buffer, pH 7.5 containing 0.2 M NaCl, at 30°C
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00002
cucumisin propeptide
Cucumis melo
-
pH and temperature not specified in the publication
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1500
-
cell extract, casein substrate
3155
-
after 2.0fold purification, casein substrate
9742
-
after 6.5fold purification, casein substrate
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
optimum ranges between 3.5 and 4.5
8
-
assay at
9
-
immobilized enzyme
10.5
-
both, the 67000 Da and the 54000 Da enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 11
-
pH 3: below 5% of the maximal activity, pH 11: 15% of the maximal activity
3.5 - 11.5
-
the enzyme retains more than 80% of activity from pH 3.5 to 11.5. No activity is observed at or below pH 2.0
3.5 - 7
-
activity known to decrease precipitously at pH values above the optimum pH range between 3.5 and 4.5, 10-20% activity retained at pH 6 and up to 10% activity retained at pH 7.0
4 - 12
-
pH 4: 50% of the maximal activity, pH 12: 10% of the maximal activity
5.8 - 11
-
pH 5.8: less than 15% of the maximal activity, pH 11: 80% of the maximal activity
8 - 11.5
-
50% of the maximal activity at pH 8 and pH 11.5
additional information
-
the 67000 Da native enzyme is more stable at acidic pH than the 54000 Da proteinase
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
45 - 50
-
-
75
-
soluble enzyme
85
-
immobilized enzyme
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 90
-
30°C: 15% of the maximal activity, 90°C: 25% of the maximal activity
40 - 55
-
more than 80% of the activity is observed from 40 to 55°C. The activity decreases steadily as the temperature rises over 60°C and no activity is observed at 80°C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.6
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
parenchyma cells of, detected by immunoelectron microscopy
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
protein storage vacuoles in parenchyma cells of seedling cotyledons and maturing seeds
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
51000
-
49000 Da by SDS-PAGE, consists of 475 amino acid residues and at least 7 mol of hexose, gel filtration
54000
-
native enzyme, a large precursor has a MW of 67000 Da, consists of a 14000 Da C-terminal polypeptide and the active 54000 Da protease domain, which arises by limited autolysis, SDS-PAGE
70000
-
SDS-PAGE
80000
-
1 * 80000, SDS-PAGE
86000
-
x * 86000, recombinant protein, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 86000, recombinant protein, SDS-PAGE
monomer
-
1 * 80000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
side-chain modification
-
glycoprotein, contains 2.4% neutral hexose, 7 mol hexose per mol of enzyme
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 0.1 M imidazole buffer (pH 6.5) containing 0.8 M sodium acetate
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 10
-
more than 80% of the initial activity after 20 h of incubation at 35°C between pH 4.0 and 10.0, rapid activity loss at pH 2 or pH 12 for 20 h at 35°C, casein substrate
670521
4 - 11.5
-
the enzyme shows more than 90% activity when incubated at pH 4.5 to 11.5 for 30 min
732844
6 - 11
-
80% of the activity remains after after incubation
95355
7 - 10
-
most stable between pH 7 and pH 10, after 1 h incubation at 60°C
95351
8 - 11
-
most stable between pH 8 and pH 11, after 2 h incubation at 25°C
95351
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 60
20 - 70
25
-
20 h at a pH of 11, 80% of the activity
37
-
24 h, 80% of the activity remains
47
-
20 min at a pH of 11, no loss of activity
50
-
the 54000 Da enzyme stable up to
60
-
1 h at a pH of 11, 65% of the activity
70
-
the 67000 Da enzyme was stable up to
72
-
inactivated after 20 min, ethylene glycol does not stablize, glycerol is effective to some extent
81
melting temperature
90
-
both, the 67000 Da and the 54000 Da enzyme were completely inactivated after 10 min above
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
20% dimethyl sulfoxide solution, 20°C, stable
-
8 M urea, pH 9.1, 20 min, no loss of activity
-
alpha-chymotrypsin has no effect on the activity
-
incubation with trypsin for 4 h decreases the activity to 30% of the initial activity and after 24 h the enzyme is completely inactivated
-
the stability of the 67000 Da and the 54000 Da enzyme is almost the same
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-propanol
-
20% w/v, at 37°C for 1 h, no effect
acetonitrile
-
20% w/v, at 37°C for 1 h, no effect
dioxan
-
20% w/v, at 37°C for 1 h, no effect
Ethanol
-
20% w/v, at 37°C for 1 h, no effect
additional information
-
the enzyme is not influenced by urea, methanol, and guanidine hydrochloride
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
rapidly inactivated by methylene blue-catalyzed photooxidation, the rate of inactivation becomes slower at lower pH, after 120 min at pH 6.5 the enzyme retains 50% of its activity
-
95348
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
lyophilization causes a loss of activity of more than 10%
-
very stable in a frozen solution, no loss of activity after one year
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
40fold
-
a quick purification method leads to an enzyme fraction with almost only the 67000 Da enzyme
-
ammonium sulfate precipitation, DEAE-Sepharose column chromatography, and Superdex 200 gel filtration
-
DEAE-Sepharose chromatography, CM-Sepharose chromatography and ammonium sulfate precipitation
-
gel filtration, SDS-PAGE
-
HiTrap SP column chromatography and Superdex 200 gel filtration
Ni-NTA affinity column chromatography
-
Ni-Sepharose column chromatography, HiTrap chelating column chromatography, DEAE-Sepharose column chromatography, and Sephacryl S-200 gel filtration
-
purified to homogeneity
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloned in Escherichia coli Y1090r-
-
expressed in Escherichia coli BL21 cells
-
expressed in Escherichia coli Rosetta (DE3) cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
subcellular localization of protease C1 and pH conditions in protein storage vacuoles in parenchyma cells of seedling cotyledons and maturing seeds examined
food industry
-
the high milk-clotting ability of religiosin C supports its use in the food industry
nutrition