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Literature summary extracted from

  • Zhong, C.; Cai, Q.; Liu, G.; Sun, L.; Hara, K.; Su, W.; Cao, M.
    Purification and characterisation of cathepsin L from the skeletal muscle of blue scad (Decapterus maruadsi) and comparison of its role with myofibril-bound serine proteinase in the degradation of myofibrillar proteins (2012), Food Chem., 133, 1560-1568.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.4.22.15 EDTA the enzyme activity increases obviously in the presence of 5 mM EDTA Decapterus maruadsi

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.22.15 chymostatin 93% inhibition at 5 mM Decapterus maruadsi
3.4.22.15 E-64 almost complete inhibition at 0.01 mM Decapterus maruadsi
3.4.22.15 leupeptin about 95% inhibition at 0.1 mM Decapterus maruadsi
3.4.22.15 additional information not inhibited by aprotinin and benzamidine Decapterus maruadsi
3.4.22.15 pefabloc about 30% inhibition at 1 mM Decapterus maruadsi

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.22.15 30000
-
 x * 30000, SDS-PAGE Decapterus maruadsi

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.22.15 casein + H2O Decapterus maruadsi
-
 ?
-
 ?
3.4.22.15 myosin heavy chain + H2O Decapterus maruadsi
-
 ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.22.15 Decapterus maruadsi
-
 blue scad
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.22.15 SP-Sepharose column chromatography, High S Cartridge column chromatography and Concanavalin A-Sepharose 4B affinity column chromatography Decapterus maruadsi

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.22.15 skeletal muscle
-
 Decapterus maruadsi
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.22.15 benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O 100% activity Decapterus maruadsi benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
 ?
3.4.22.15 casein + H2O
-
 Decapterus maruadsi ?
-
 ?
3.4.22.15 additional information 3% with benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin and 1% with both L-Arg-7-amido-4-methylcoumarin and Boc-Phe-Ser-Arg-7-amido-4-methylcoumarin. No activity with Boc-Gln-Arg-Arg-7-amido-4-methylcoumarin and succinyl-Leu-Leu-Tyr-7-amido-4-methylcoumarin Decapterus maruadsi ?
-
 ?
3.4.22.15 myosin heavy chain + H2O
-
 Decapterus maruadsi ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.22.15 ? x * 30000, SDS-PAGE Decapterus maruadsi

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.22.15 55
-
-
 Decapterus maruadsi

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.4.22.15 40 65 more than 50% activity between 40 and 65°C Decapterus maruadsi

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.4.22.15 55
-
 in the absence of bovine serum albumin, the enzyme activity of cathepsin L decreases to around 60% after incubation at 55°C for 10 min, and is about 40% after 30 min. In the presence of 2% bovine serum albumin, the thermal stability of cathepsin L increases significantly Decapterus maruadsi

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.22.15 5.5
-
-
 Decapterus maruadsi

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.4.22.15 4 6.5 more than 50% activity between pH 4.0 and 6.5, cathepsin L has almost no activity at pH values above 7.0 Decapterus maruadsi