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Literature summary for 3.4.22.15 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

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

Inhibitors

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Decapterus maruadsi
-
blue scad
-

Purification (Commentary)

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

Source Tissue

Source Tissue Comment Organism Textmining
skeletal muscle
-
Decapterus maruadsi
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O 100% activity Decapterus maruadsi benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
?
casein + H2O
-
Decapterus maruadsi ?
-
?
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 ?
-
?
myosin heavy chain + H2O
-
Decapterus maruadsi ?
-
?

Subunits

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

Temperature Optimum [°C]

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

Temperature Range [°C]

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

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
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

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5
-
-
Decapterus maruadsi

pH Range

pH Minimum pH Maximum Comment Organism
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