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Literature summary 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

EC Number Inhibitors Comment Organism Structure
3.4.21.25 diisopropyl fluorophosphate completely inactivated by incubation with 0.5 mM for 20 min Cucumis melo
3.4.21.25 HgCl2 37% inhibition at a concentration of 0.5 mM Cucumis melo
3.4.21.25 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
3.4.21.25 PMSF 45% inhibition at a concentration of 0.5 mM Cucumis melo

Metals/Ions

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.21.25 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)

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

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.25 Cucumis melo
-
-
-

Posttranslational Modification

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

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.21.25 purified to homogeneity Cucumis melo

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.21.25 fruit
-
 Cucumis melo
-
3.4.21.25 sarcocarp
-
 Cucumis melo
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.25 benzyloxycarbonyl-Glu-Phe + H2O weakly hydrolyzed Cucumis melo benzyloxycarbonyl-Glu + Phe
-
 ?
3.4.21.25 Benzyloxycarbonyl-Glu-Tyr + H2O weakly hydrolyzed Cucumis melo Benzyloxycarbonyl-Glu + Tyr
-
 ?
3.4.21.25 casein + H2O
-
 Cucumis melo ?
-
 ?
3.4.21.25 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 ?
-
 ?
3.4.21.25 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 ?
-
 ?
3.4.21.25 Protein + H2O
-
 Cucumis melo ?
-
 ?
3.4.21.25 protein + H2O
-
 Cucumis melo hydrolyzed protein
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.21.25 70
-
 at pH 7.1 Cucumis melo

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.4.21.25 30 90 30°C: 15% of the maximal activity, 90°C: 25% of the maximal activity Cucumis melo

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.4.21.25 20 60 stable up to 60°C Cucumis melo

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.21.25 10
-
-
 Cucumis melo

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.4.21.25 5.8 11 pH 5.8: less than 15% of the maximal activity, pH 11: 80% of the maximal activity Cucumis melo

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.4.21.25 7 10 most stable between pH 7 and pH 10, after 1 h incubation at 60°C Cucumis melo
3.4.21.25 8 11 most stable between pH 8 and pH 11, after 2 h incubation at 25°C Cucumis melo