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acetyl-Ala-Ala-Ala-p-nitroanilide + H2O
?
-
1% of the activity with benzyloxycarbonyl-Tyr-nitrophenyl ester
-
-
?
Ala-Ala-Pro-Ala-p-nitroanilide + H2O
?
-
-
-
-
?
Ala-Ala-Pro-Glu-p-nitroanilide + H2O
?
-
-
-
-
?
Ala-Ala-Pro-Gly-p-nitroanilide + H2O
?
-
-
-
-
?
Ala-Ala-Pro-L-diaminopropionic acid-p-nitroanilide + H2O
?
-
-
-
-
?
Ala-Ala-Pro-Leu-p-nitroanilide + H2O
?
-
-
-
-
?
Ala-Ala-Pro-Lys-p-nitroanilide + H2O
?
-
-
-
-
?
Ala-Ala-Pro-Phe-p-nitroanilide + H2O
?
-
-
-
-
?
Ala-Ala-Pro-Val-p-nitroanilide + H2O
?
-
-
-
-
?
alpha-mating factor + H2O
?
-
cleaves at one site, Glu-Leu
-
-
?
angiotensin I + H2O
?
-
cleaves at two sites, Tyr-Ile and Phe-His
-
-
?
benzoyl-Tyr-ethyl ester + H2O
benzoyl-Tyr + ethanol
-
24% of the activity with benzyloxycarbonyl-Tyr-nitrophenyl ester
-
-
?
benzyloxycarbonyl-Ala-Ala-Ala-SCH2C6H5 + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Arg-SCH2C6H5 + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Asp-SCH2C6H5 + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Glu-SCH2C6H5 + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Leu-SCH2C6H5 + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Ala-Ala-norleucine-SCH2C6H5 + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Ala-Ala-norvaline-SCH2C6H5 + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Phe-SCH2C6H5 + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Ser-SCH2C6H5 + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Val-SCH2C6H5 + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Ala-Asn-SCH2C6H5 + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Glu-Phe + H2O
benzyloxycarbonyl-Glu + Phe
-
weakly hydrolyzed
-
-
?
Benzyloxycarbonyl-Glu-Tyr + H2O
Benzyloxycarbonyl-Glu + Tyr
benzyloxycarbonyl-Tyr-4-nitrophenyl ester + H2O
benzyloxycarbonyl-Tyr + 4-nitrophenyl ester
-
best synthetic substrate
-
-
?
beta-conglycinin storage protein + H2O
?
-
-
-
?
bovine casein + H2O
L-tyrosine + ?
-
-
-
-
?
bovine skimmed milk powder + H2O
?
-
-
-
-
?
Cytochrome c + H2O
?
-
initial cleavage site, Glu-Lys and Ala-Ala
-
-
?
delta sleep-inducing peptide + H2O
?
-
cleaves at one site, Ala-Ser
-
-
?
glutaryl-Ala-Ala-Pro-Leu-p-nitroanilide + H2O
?
-
-
-
-
?
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
-
-
-
-
?
insulin + H2O
?
-
initial cleavage site, Gln-His
-
-
?
KVEKEESEE + H2O
KVEKE + ESEE
-
-
-
?
L-alanyl-4-nitroanilide + H2O
L-alanine + 4-nitroaniline
-
-
-
-
?
L-alanyl-L-alanyl-4-nitroanilide + H2O
L-alanyl-L-alanine + 4-nitroaniline
-
-
-
-
?
L-gamma-glutamyl-4-nitroanilide + H2O
L-glutamate + 4-nitroaniline
-
-
-
-
?
L-leucyl-4-nitroanilide + H2O
L-leucine + 4-nitroaniline
-
-
-
-
?
Leu-Leu-Leu-Leu-Pro-Glu-Ala-Leu + H2O
Leu-Leu-Leu-Leu-Pro-Glu + Ala-Leu
-
-
-
?
Leu-Leu-Leu-Pro-Glu-Ala-Leu + H2O
Leu-Leu-Leu-Pro-Glu + Ala-Leu
-
-
-
?
Leu-Leu-Pro-Ala-Ala-Leu + H2O
Leu-Leu-Pro-Ala + Ala-Leu
-
-
-
?
Leu-Leu-Pro-Arg-Ala-Leu + H2O
Leu-Leu-Pro-Arg + Ala-Leu
-
low activity
-
?
Leu-Leu-Pro-Asn-Ala-Leu + H2O
Leu-Leu-Pro-Asn + Ala-Leu
-
-
-
?
Leu-Leu-Pro-Asp-Ala-Leu + H2O
Leu-Leu-Pro-Asp + Ala-Leu
-
-
-
?
Leu-Leu-Pro-Gln-Ala-Leu + H2O
Leu-Leu-Pro-Gln + Ala-Leu
-
-
-
?
Leu-Leu-Pro-Glu-Ala + H2O
Leu-Leu-Pro-Glu + Ala
-
low activity
-
?
Leu-Leu-Pro-Glu-Ala-Leu + H2O
Leu-Leu-Pro-Glu + Ala-Leu
-
low activity
-
?
Leu-Leu-Pro-Glu-Ala-Leu-Leu + H2O
Leu-Leu-Pro-Glu + Ala-Leu-Leu
-
-
-
?
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-Gly-Leu + H2O
Leu-Leu-Pro-Glu + Gly-Leu
-
-
-
?
Leu-Leu-Pro-Glu-Lys-Leu + H2O
Leu-Leu-Pro-Glu + Lys-Leu
-
-
-
?
Leu-Leu-Pro-Glu-Phe-Leu + H2O
Leu-Leu-Pro-Glu + Phe-Leu
-
low activity
-
?
Leu-Leu-Pro-Glu-Ser-Leu + H2O
Leu-Leu-Pro-Glu + Ser-Leu
-
-
-
?
Leu-Leu-Pro-His-Ala-Leu + H2O
Leu-Leu-Pro-His + Ala-Leu
-
-
-
?
Leu-Leu-Pro-Leu-Ala-Leu + H2O
Leu-Leu-Pro-Leu + Ala-Leu
-
-
-
?
Leu-Leu-Pro-Lys-Ala-Leu + H2O
Leu-Leu-Pro-Lys + Ala-Leu
-
low activity
-
?
Leu-Leu-Pro-Met-Ala-Leu + H2O
Leu-Leu-Pro-Met + Ala-Leu
Leu-Leu-Pro-Phe-Ala-Leu + H2O
Leu-Leu-Pro-Phe + Ala-Leu
-
-
-
?
Leu-Leu-Pro-Ser-Ala-Leu + H2O
Leu-Leu-Pro-Ser + Ala-Leu
-
-
-
?
Leu-Leu-Pro-Thr-Ala-Leu + H2O
Leu-Leu-Pro-Thr + Ala-Leu
-
-
-
?
Leu-Leu-Pro-Trp-Ala-Leu + H2O
Leu-Leu-Pro-Trp + Ala-Leu
-
-
-
?
Leu-Pro-Glu-Ala-Leu + H2O
Leu-Pro-Glu + Ala-Leu
-
low activity
-
?
Myoglobin + H2O
?
-
initial cleavage site, Asp-Ile and Glu-Ala
-
-
?
N-acetyl-L-alanyl-L-alanyl-alpha-azaalanine p-nitrophenyl ester + H2O
?
-
-
-
-
?
ovalbumin + H2O
?
-
initial cleavage site, Asn-Ala
-
-
?
peptidyl-p-nitroanilide + H2O
p-nitroaniline + peptide
-
-
-
-
?
Protein + H2O
?
-
-
95347, 95348, 95349, 95350, 95351, 95352, 95353, 95354, 95355, 95356, 95357, 95358 -
-
?
protein + H2O
hydrolyzed protein
-
-
95347, 95348, 95349, 95350, 95351, 95352, 95353, 95354, 95355, 95356, 95357, 95358 -
-
?
skim milk + H2O
?
-
-
-
-
?
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
-
-
-
-
?
succinyl-Ala-Ala-Ala-p-nitroanilide + H2O
?
-
-
-
-
?
succinyl-Ala-Ala-p-nitroanilide + H2O
?
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
?
-
-
-
-
?
succinyl-Ala-p-nitroanilide + H2O
succinyl-Ala + 4-nitroaniline
-
-
-
-
?
succinyl-Ala-Pro-Ala-p-nitroanilide + H2O
?
-
-
-
-
?
superoxide dismutase + H2O
?
-
initial cleavage site, His-Gly and Leu-Ala
-
-
?
TMA-lysozyme BrCN fragment + H2O
?
-
cleaves at two sites, Cys-Lys and Arg-Gly
-
-
?
additional information
?
-
Benzyloxycarbonyl-Glu-Tyr + H2O
Benzyloxycarbonyl-Glu + Tyr
-
-
-
-
?
Benzyloxycarbonyl-Glu-Tyr + H2O
Benzyloxycarbonyl-Glu + Tyr
-
weakly hydrolyzed
-
-
?
casein + H2O
?
-
-
-
-
?
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
-
-
-
?
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
-
-
?
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
-
-
?
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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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
-
butanol
-
68.24% residual activity at 50% (v/v)
Cd2+
-
about 8% residual activity at 5 mM
chymostatin
-
2.45% residual activity at 5 mM
Co2+
-
about 15% 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)
EDTA
-
68% residual activity at 2 mM
EGTA
-
72% residual activity at 2 mM
ethanol
-
75.09% residual activity at 50% (v/v)
Fe2+
-
about 55% residual activity at 5 mM
phenylmethylsulfonyl fluoride
Phenylmethylsulfonylfluoride
-
strong inhibition
propeptide
77.7% inhibition at 200 mM
-
Zn2+
-
about 10% residual activity at 5 mM
ZnCl2
-
11% inhibition by 2 mM
diisopropyl fluorophosphate
-
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
diisopropyl fluorophosphate
-
completely inactivated at 0.5 mM for 10 min
diisopropyl fluorophosphate
-
complete inhibition by 2 mM
diisopropyl fluorophosphate
-
complete inhibition by 1 mM
HgCl2
-
37% inhibition at a concentration of 0.5 mM
HgCl2
-
10% inhibition by 0.5 mM
phenylmethylsulfonyl fluoride
-
7.04% residual activity at 0.5 mM
phenylmethylsulfonyl fluoride
-
5.12% residual activity at 5 mM
PMSF
-
45% inhibition at a concentration of 0.5 mM
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 iodoacetamide and pepstatin
-
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
-
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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Kaneda, M.; Tominaga, N.
Properties of a new plant serine protease cucumisin
Agric. Biol. Chem.
51
489-492
1987
Cucumis melo
-
brenda
Kaneda, M.; Uchikoba, T.; Tominaga, N.
Photochemical oxidation of cucumisin, a serine proteinase from Cucumis melo
Agric. Biol. Chem.
51
1159-1161
1987
Cucumis melo
-
brenda
Kaneda, M.; Minematsu, Y.; Powers, J.C.; Tominaga, N.
Active site titration of the serine protease cucumisin from Cucumis melo
Phytochemistry
25
2407-2408
1986
Cucumis melo
-
brenda
Kaneda, M.; Ohmine, H.; Yonezawa, H.; Tominaga, N.
Amino acid sequence around the reactive serine of cucumisin from melon fruit
J. Biochem.
95
825-829
1984
Cucumis melo
brenda
Kaneda, M.; Tominaga, N.
Isolation and characterization of a proteinase from the sarcocarp of melon fruit
J. Biochem.
78
1287-1296
1975
Cucumis melo
brenda
Kaneda, M.; Minematsu, Y.; Powers, J.C.; Tominaga, N.
Specificity of cucumisin in hydrolysis of peptide thiobenzyl esters
Agric. Biol. Chem.
50
1075-1076
1986
Cucumis melo
-
brenda
Yamagata, H.; Masuzawa, T.; Nagaoka, Y.; Ohnishi, T.; Iwasaki, T.
Cucumisin, a serine protease from melon fruits, shares structural homology with subtilisin and is generated from a large precursor
J. Biol. Chem.
269
32725-32731
1994
Cucumis melo
brenda
Yamagata, H.; Ueno, S.; Iwasaki, T.
Isolation and characterization of a possible native cucumisin from developing melon fruits and its limited autolysis to cucumisin
Agric. Biol. Chem.
53
1009-1017
1989
Cucumis melo
-
brenda
Kaneda, M.; Yonezawa, H.; Uchikoba, T.
Purification and some properties of a protease from the sarcocarp of musk melon fruit
Biosci. Biotechnol. Biochem.
61
2100-2102
1997
Cucumis melo
brenda
Uchikoba, T.; Kaneda, M.
Milk-clotting activity of cucumisin, a plant serine protease from melon fruit
Appl. Biochem. Biotechnol.
56
325-330
1996
Cucumis melo
brenda
Kaneda, M.; Yonezawa, H.; Uchikoba, T.
Improved isolation, stability and substrate specificity of cucumisin, a plant serine endopeptidase
Biotechnol. Appl. Biochem.
22
215-222
1995
Cucumis melo
brenda
Uchikoba, T.; Yonezawa, H.; Kaneda, M.
Cleavage specificity of cucumisin, a plant serine protease
J. Biochem.
117
1126-1130
1995
Cucumis melo
brenda
Yonezawa, H.; Kaizuka, H.; Uchikoba, T.; Arima, K.; Kaneda, M.
Substrate specificity of cucumisin on synthetic peptides
Biosci. Biotechnol. Biochem.
64
2104-2108
2000
Cucumis melo
brenda
Choi, J.W.; Kimi, G.B.; Huh, Y.C.; Kwon, M.R.; Mok, I.G.; Kim, J.W.; Lee, T.S.; Kim, S.; Im, K.H.
Cloning of genes differentially expressed during the initial stage of fruit development in melon (Cucumis melo cv. Reticulatus)
Mol. Cells
17
237-241
2004
Cucumis melo
brenda
Asif-Ullah, M.; Kim, K.S.; Yu, Y.G.
Purification and characterization of a serine protease from Cucumis trigonus Roxburghi
Phytochemistry
67
870-875
2006
Cucumis trigonus
brenda
He, F.; Huang, F.; Wilson, K.A.; Tan-Wilson, A.
Protein storage vacuole acidification as a control of storage protein mobilization in soybeans
J. Exp. Bot.
58
1059-1070
2007
Glycine max
brenda
Sankian, M.; Talebi, F.; Moghadam, M.; Vahedi, F.; Azad, F.J.; Varasteh, A.R.
Molecular cloning and expression of Cucumisin (Cuc m 1), a subtilisin-like protease of Cucumis melo in Escherichia coli
Allergol. Int.
60
61-67
2011
Cucumis melo
brenda
Nakagawa, M.; Ueyama, M.; Tsuruta, H.; Uno, T.; Kanamaru, K.; Mikami, B.; Yamagata, H.
Functional analysis of the cucumisin propeptide as a potent inhibitor of its mature enzyme
J. Biol. Chem.
285
29797-29807
2010
Cucumis melo
brenda
Murayama, K.; Kato-Murayama, M.; Hosaka, T.; Sotokawauchi, A.; Yokoyama, S.; Arima, K.; Shirouzu, M.
Crystal structure of cucumisin, a subtilisin-like endoprotease from Cucumis melo L.
J. Mol. Biol.
423
386-396
2012
Cucumis melo (Q39547), Cucumis melo
brenda
Tan-Wilson, A.; Bandak, B.; Prabu-Jeyabalan, M.
The PA domain is crucial for determining optimum substrate length for soybean protease C1: structure and kinetics correlate with molecular function
Plant Physiol. Biochem.
53
27-32
2012
Glycine max (Q9ZTT3), Glycine max
brenda
Sharma, A.; Kumari, M.; Jagannadham, M.
Religiosin C, a cucumisin-like serine protease from Ficus religiosa
Process Biochem.
47
914-921
2012
Ficus religiosa
-
brenda
Gagaoua, M.; Ziane, F.; Nait Rabah, S.; Boucherba, N.; Ait Kaki El-Hadef El-Okki, A.; Bouanane-Darenfed, A.; Hafid, K.
Three phase partitioning, a scalable method for the purification and recovery of cucumisin, a milk-clotting enzyme, from the juice of Cucumis melo var. reticulatus
Int. J. Biol. Macromol.
102
515-525
2017
Cucumis melo
brenda
Sotokawauchi, A.; Kato-Murayama, M.; Murayama, K.; Hosaka, T.; Maeda, I.; Onjo, M.; Ohsawa, N.; Kato, D.I.; Arima, K.; Shirouzu, M.
Structural basis of cucumisin protease activity regulation by its propeptide
J. Biochem.
161
45-53
2017
Cucumis melo (Q39547), Cucumis melo
brenda