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Information on EC 3.4.21.25 - cucumisin
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EC Tree
3.4.21.25 cucumisinSpecify your search results
Word Map
- 3.4.21.25
- melon
- subtilisin
-
subtilisin-like
- sarcocarp
-
prince
-
merrill
-
serping1
-
subtilase
- beta-conglycinin
- nutrition
- food industry
- analysis
The enzyme appears in viruses and cellular organisms
Synonyms
cucumisin, protease c1, soybean protease c1, cuc m 1, cucumisin homologue, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
cucumisin
additional information
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hydrolysis of proteins with broad specificity
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
endopeptidase
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CAS REGISTRY NUMBER
COMMENTARY
82062-89-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-Ala-Ala-Ala-p-nitroanilide + H2O
?
-
1% of the activity with benzyloxycarbonyl-Tyr-nitrophenyl ester
-
-
?
benzoyl-Tyr-ethyl ester + H2O
benzoyl-Tyr + ethanol
-
24% of the activity with benzyloxycarbonyl-Tyr-nitrophenyl ester
-
-
?
benzyloxycarbonyl-Glu-Phe + H2O
benzyloxycarbonyl-Glu + Phe
-
weakly hydrolyzed
-
-
?
benzyloxycarbonyl-Tyr-4-nitrophenyl ester + H2O
benzyloxycarbonyl-Tyr + 4-nitrophenyl ester
-
best synthetic substrate
-
-
?
glutaryl-alanyl-alanyl-prolyl-leucine-4-nitroanilide + H2O
glutaryl-alanyl-alanyl-prolyl-leucine + 4-nitroaniline
-
-
-
?
glutaryl-L-alanyl-L-alanyl-L-prolyl-L-leucyl-4-nitroanilide + H2O
glutaryl-L-alanyl-L-alanyl-L-prolyl-L-leucine + 4-nitroaniline
-
-
-
-
?
L-alanyl-L-alanyl-4-nitroanilide + H2O
L-alanyl-L-alanine + 4-nitroaniline
-
-
-
-
?
Leu-Leu-Leu-Leu-Pro-Glu-Ala-Leu + H2O
Leu-Leu-Leu-Leu-Pro-Glu + Ala-Leu
-
-
-
?
Leu-Leu-Pro-Arg-Ala-Leu + H2O
Leu-Leu-Pro-Arg + Ala-Leu
-
low activity
-
?
Leu-Leu-Pro-Glu-Ala-Leu + H2O
Leu-Leu-Pro-Glu + Ala-Leu
-
low activity
-
?
Leu-Leu-Pro-Glu-Ala-Leu-Leu-Leu + H2O
Leu-Leu-Pro-Glu + Ala-Leu-Leu-Leu
-
-
-
?
Leu-Leu-Pro-Glu-Glu-Leu + H2O
Leu-Leu-Pro-Glu + Glu-Leu
-
low activity
-
?
Leu-Leu-Pro-Glu-Phe-Leu + H2O
Leu-Leu-Pro-Glu + Phe-Leu
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low activity
-
?
Leu-Leu-Pro-Lys-Ala-Leu + H2O
Leu-Leu-Pro-Lys + Ala-Leu
-
low activity
-
?
N-acetyl-L-alanyl-L-alanyl-alpha-azaalanine p-nitrophenyl ester + H2O
?
-
-
-
-
?
Protein + H2O
?
-
-
-
-
?
protein + H2O
hydrolyzed protein
-
-
-
-
?
skim-milk powder + H2O
?
-
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
-
-
-
-
?
Suc-Ala-Ala-Pro-Leu-p-nitroanilide + H2O
Suc-Ala-Ala-Pro-Leu + p-nitroaniline
-
-
-
-
?
Suc-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
Suc-Ala-Ala-Pro-Phe + p-nitroaniline
-
-
-
-
?
TMA-lysozyme BrCN fragment + H2O
?
-
cleaves at two sites, Cys-Lys and Arg-Gly
-
-
?
Benzyloxycarbonyl-Glu-Tyr + H2O
Benzyloxycarbonyl-Glu + Tyr
-
weakly hydrolyzed
-
-
?
Insulin B-chain + H2O
?
-
broad substrate specificity, but the bonds of the valine residue are not split
-
-
?
Insulin B-chain + H2O
?
-
three cleavage sites are detected after a reaction period of 30 s, Leu-Cys, Cys-Gly, and Glu-Ala
-
-
?
Insulin B-chain + H2O
?
-
wide specificity in hydrolysis of reduced and carboxymethylated insulin B-chain, the carboxyl side of bonds containing acidic amino acid residues such as CM-cysteine and glutamic acid is appreciably cleaved by the enzyme
-
-
?
Leu-Leu-Pro-Met-Ala-Leu + H2O
Leu-Leu-Pro-Met + Ala-Leu
-
best substrate
-
?
additional information
?
-
-
no hydrolysis of benzyloxycarbonyl-Ala-Ala-Ile-SCH2C6H5, benzyloxycarbonyl-Ala-Ala-Pro-SCH2C6H5
-
-
?
additional information
?
-
-
no hydrolysis of Lys-p-nitroanilide, Tyr-p-nitroanilide, Leu-p-nitroanilide, tosyl-Arg-methyl ester, acetyl-Phe-ethyl ester, benzyloxycarbonyl-Lys-nitrophenyl ester and benzyloxycarbonyl-Gly-Gly-Leu-p-nitroanilide
-
-
?
additional information
?
-
-
the substrate specificity of the 67000 Da and the 54000 Da enzyme is almost the same
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-
?
additional information
?
-
-
no hydrolysis of acetyl-L-tyrosine ethyl ester, benzoyl-L-arginine ethyl ester, benzoyl-L-arginine-p-nitroanilide, benzoyl-L-tyrosine-p-nitroanilide, glutathione, glycyl-L-leucine, Gly-Gly-Gly and Leu-Gly-Gly
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-
?
additional information
?
-
-
substrate specificity at positions P6-P'4, no activity with Leu-Leu-Pro-Glu-Val-Leu, Pro-Glu-Ala-Leu, Leu-Pro-Glu-Ala, Leu-Leu-Pro-Gly-Ala-Leu, Leu-Leu-Pro-Ile-Ala-Leu and Leu-Leu-Pro-Pro-Ala-Leu, poor substrates are Leu-Leu-Pro-Tyr-Ala-Leu, Leu-Leu-Pro-Glu-Leu-Leu and Leu-Leu-Pro-Val-Ala-Leu
-
?
additional information
?
-
-
no activity toward Nalpha-benzoyl-DL-arginyl-4-nitroanilide and N-succinyl-L-phenylalanyl-4-nitroanilide
-
-
?
additional information
?
-
-
subtilisin-like serine protease initiating proteolysis of seed storage proteins during germination and early seedling growth
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
the enzyme activity is 2.35fold increased at 5 mM Ca2+. 2.5-10 mM Ca2+ increase the half-life of the enzyme at 35-55°C
additional information
additional information
-
the enzyme is not influenced by Hg2+, Na+, K+, Mg2+, Ca2+, Rb+, and Li+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-(2-aminoethyl)-benzenesulfonyl fluoride
-
17% inhibition by 1 mM; i.e. Pefabloc SC
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
-
cucumisin propeptide
-
potent inhibitor of its mature enzyme, competitive inhibition
-
diisopropyl fluorophosphate
-
synthesis of denatured diisopropyl phosphorylcucumisin derivatives, which are hydrolyzed by chymotrypsin, to get peptides for amino acid sequence analysis around the reactive serine of the active site
diisopropyl fluorophosphate
-
completely inactivated by incubation with 0.5 mM for 20 min
PMSF
-
slightly inactivated by 0.1 mM, 11% inhibition by 0.5 mM, 23% inhibition by 1 mM
additional information
-
cucumisin is not inhibited by the subtilisin E propeptide
-
additional information
not inhibited by the C-terminal hepta-peptide of the propeptide (Asn-Glu-Met-Asn-Glu-Leu-His)
-
additional information
-
not inhibited by the C-terminal hepta-peptide of the propeptide (Asn-Glu-Met-Asn-Glu-Leu-His)
-
additional information
-
no effect: iodoacetamide, EDTA, PCMB, beta-mercaptoethanol, cysteine, soybean trypsin inhibitor, N-tosyl-L-lysine chloromethyl ketone and N-tosyl-L-phenylalanine chloromethyl ketone
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additional information
-
no effect: iodoacetate, EDTA, PCMB, beta-mercaptoethanol, cysteine, N-tosyl-L-phenylalanine chloromethyl ketone and PCMB; no effect of plant proteinous inhibitors of serine proteinases
-
additional information
-
no inhibition with N-tosyl-L-lysine chloromethyl ketone, N-tosyl-L-phenylalanine chloromethyl ketone, iodoacetate, PCMB, p-chloromercuribenzenesulfonate, E-64, antipain, ovomucoid, EDTA, soybean trypsin inhibitors
-
additional information
-
no effect of leupeptin, alpha1-antitrypsin, soybean trypsin inhibitor, ovomucoid and aprotinin
-
additional information
-
no inhibition by EDTA, pepstatin or cysteine protease inhibitors
-
additional information
-
not inhibited by EDTA, EGTA, iodoacetic acid, 2-phenanthroline, SBTI, and dithiothreitol
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Breast Neoplasms
Unmasking Heavily O-Glycosylated Serum Proteins Using Perchloric Acid: Identification of Serum Proteoglycan 4 and Protease C1 Inhibitor as Molecular Indicators for Screening of Breast Cancer.
Colorectal Neoplasms
Revelation of Proteomic Indicators for Colorectal Cancer in Initial Stages of Development.
Colorectal Neoplasms
Super Secondary Structures of Proteins with Post-Translational Modifications in Colon Cancer.
Liver Cirrhosis
Quantitative analysis of core fucosylation of serum proteins in liver diseases by LC-MS-MRM.
Neoplasms
Comparative serum glycoproteomics using lectin selected sialic acid glycoproteins with mass spectrometric analysis: application to pancreatic cancer serum.
Neoplasms
Glycoprotein microarrays with multi-lectin detection: unique lectin binding patterns as a tool for classifying normal, chronic pancreatitis and pancreatic cancer sera.
Protein Deficiency
New therapeutics in C1INH deficiency: a review of recent studies and advances.
Tuberculosis
Mutation analysis of the interactions between Mycobacterium tuberculosis caseinolytic protease C1 (ClpC1) and ecumicin.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
turnover number is pH-dependent and increases by a factor 6 upon going from pH 5 to pH 6
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00002
cucumisin propeptide
Cucumis melo
-
pH and temperature not specified in the publication
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
activity of the immobilized enzyme is 41% of that of the soluble enzyme
additional information
-
enzyme from crude latex shows a specific activity of 23.99 units/mg at pH 8.0 and 37°C. After 2.29fold purification, the enzyme shows a specific activity of 55.01 units/mg at pH 8.0 and 37°C. One unit of enzyme activity is defined as the amount of enzyme that gives rise to an increase in one unit of absorbance at 280 nm per min of casein digestion
additional information
-
activity during seed germination, activity also determined in two stages of protein storage vacuole development during seed maturation, acidic conditions for activity required, acridine orange used as an indicator of acidic compartments, enzyme activity determined in relation to staining intensities of major