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 37C
0.004
L-alanyl-L-alanyl-4-nitroanilide
-
at pH 8.0 and 37C
0.273
L-gamma-glutamyl-4-nitroanilide
-
at pH 8.0 and 37C
0.093
L-leucyl-4-nitroanilide
-
at pH 8.0 and 37C
1.8
Leu-Leu-Pro-Ala-Ala-Leu
-
pH 8.0, 37C
3.9
Leu-Leu-Pro-Asn-Ala-Leu
-
pH 8.0, 37C
5.6
Leu-Leu-Pro-Gln-Ala-Leu
-
pH 8.0, 37C
2.8
Leu-Leu-Pro-Glu-Ala-Leu
-
pH 8.0, 37C
3
Leu-Leu-Pro-Glu-Lys-Leu
-
pH 8.0, 37C
0.8
Leu-Leu-Pro-Glu-Ser-Leu
-
pH 8.0, 37C
2.9
Leu-Leu-Pro-His-Ala-Leu
-
pH 8.0, 37C
0.7
Leu-Leu-Pro-Leu-Ala-Leu
-
pH 8.0, 37C
4.1
Leu-Leu-Pro-Met-Ala-Leu
-
pH 8.0, 37C
0.6
Leu-Leu-Pro-Phe-Ala-Leu
-
pH 8.0, 37C
0.6
Leu-Leu-Pro-Ser-Ala-Leu
-
pH 8.0, 37C
1.1
Leu-Leu-Pro-Thr-Ala-Leu
-
pH 8.0, 37C
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 37C
25.48
L-alanyl-L-alanyl-4-nitroanilide
Ficus religiosa
-
at pH 8.0 and 37C
207.8
L-gamma-glutamyl-4-nitroanilide
Ficus religiosa
-
at pH 8.0 and 37C
749.7
L-leucyl-4-nitroanilide
Ficus religiosa
-
at pH 8.0 and 37C
14
Leu-Leu-Pro-Ala-Ala-Leu
Cucumis melo
-
pH 8.0, 37C
98
Leu-Leu-Pro-Asn-Ala-Leu
Cucumis melo
-
pH 8.0, 37C
162
Leu-Leu-Pro-Gln-Ala-Leu
Cucumis melo
-
pH 8.0, 37C
5
Leu-Leu-Pro-Glu-Ala-Leu
Cucumis melo
-
pH 8.0, 37C
4
Leu-Leu-Pro-Glu-Lys-Leu
Cucumis melo
-
pH 8.0, 37C
7
Leu-Leu-Pro-Glu-Ser-Leu
Cucumis melo
-
pH 8.0, 37C
59
Leu-Leu-Pro-His-Ala-Leu
Cucumis melo
-
pH 8.0, 37C
20
Leu-Leu-Pro-Leu-Ala-Leu
Cucumis melo
-
pH 8.0, 37C
177
Leu-Leu-Pro-Met-Ala-Leu
Cucumis melo
-
pH 8.0, 37C
5
Leu-Leu-Pro-Phe-Ala-Leu
Cucumis melo
-
pH 8.0, 37C
3
Leu-Leu-Pro-Ser-Ala-Leu
Cucumis melo
-
pH 8.0, 37C
27
Leu-Leu-Pro-Thr-Ala-Leu
Cucumis melo
-
pH 8.0, 37C
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 37C
81539
6888
L-alanyl-L-alanyl-4-nitroanilide
Ficus religiosa
-
at pH 8.0 and 37C
202345
749.7
L-gamma-glutamyl-4-nitroanilide
Ficus religiosa
-
at pH 8.0 and 37C
202346
422.2
L-leucyl-4-nitroanilide
Ficus religiosa
-
at pH 8.0 and 37C
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 30C
-
0.0000062
cucumisin propeptide
-
in 150 mM sodium phosphate buffer, pH 7.5 containing 0.2 M NaCl, at 30C
-
0.0001
RSP1 propeptide
-
in 150 mM sodium phosphate buffer, pH 7.5 containing 0.2 M NaCl, at 30C
-
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
-
30C: 15% of the maximal activity, 90C: 25% of the maximal activity
40 - 55
-
more than 80% of the activity is observed from 40 to 55C. The activity decreases steadily as the temperature rises over 60C and no activity is observed at 80C
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 35C between pH 4.0 and 10.0, rapid activity loss at pH 2 or pH 12 for 20 h at 35C, 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 60C
95351
8 - 11
-
most stable between pH 8 and pH 11, after 2 h incubation at 25C
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, 20C, 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 37C for 1 h, no effect
acetonitrile
-
20% w/v, at 37C for 1 h, no effect
dioxan
-
20% w/v, at 37C for 1 h, no effect
Ethanol
-
20% w/v, at 37C 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