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Literature summary for 3.4.21.25 extracted from

  • Kaneda, M.; Tominaga, N.
    Isolation and characterization of a proteinase from the sarcocarp of melon fruit (1975), J. Biochem., 78, 1287-1296.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
diisopropyl fluorophosphate completely inactivated by incubation with 0.5 mM for 20 min Cucumis melo
HgCl2 37% inhibition at a concentration of 0.5 mM Cucumis melo
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 Cucumis melo
PMSF 45% inhibition at a concentration of 0.5 mM Cucumis melo

Metals/Ions

Metals/Ions Comment Organism Structure
additional information not affected by CaCl2, CdCl2, MnSO4, CoSO4 and ZnSO4 Cucumis melo

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
51000
-
49000 Da by SDS-PAGE, consists of 475 amino acid residues and at least 7 mol of hexose, gel filtration Cucumis melo

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Protein + H2O Cucumis melo
-
?
-
?

Organism

Organism UniProt Comment Textmining
Cucumis melo
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
side-chain modification glycoprotein, contains 2.4% neutral hexose, 7 mol hexose per mol of enzyme Cucumis melo

Purification (Commentary)

Purification (Comment) Organism
purified to homogeneity Cucumis melo

Source Tissue

Source Tissue Comment Organism Textmining
fruit
-
Cucumis melo
-
sarcocarp
-
Cucumis melo
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
benzyloxycarbonyl-Glu-Phe + H2O weakly hydrolyzed Cucumis melo benzyloxycarbonyl-Glu + Phe
-
?
Benzyloxycarbonyl-Glu-Tyr + H2O weakly hydrolyzed Cucumis melo Benzyloxycarbonyl-Glu + Tyr
-
?
casein + H2O
-
Cucumis melo ?
-
?
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 Cucumis melo ?
-
?
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 Cucumis melo ?
-
?
Protein + H2O
-
Cucumis melo ?
-
?
protein + H2O
-
Cucumis melo hydrolyzed protein
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
70
-
at pH 7.1 Cucumis melo

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
30 90 30°C: 15% of the maximal activity, 90°C: 25% of the maximal activity Cucumis melo

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
20 60 stable up to 60°C Cucumis melo

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
10
-
-
Cucumis melo

pH Range

pH Minimum pH Maximum Comment Organism
5.8 11 pH 5.8: less than 15% of the maximal activity, pH 11: 80% of the maximal activity Cucumis melo

pH Stability

pH Stability pH Stability Maximum Comment Organism
7 10 most stable between pH 7 and pH 10, after 1 h incubation at 60°C Cucumis melo
8 11 most stable between pH 8 and pH 11, after 2 h incubation at 25°C Cucumis melo