Activating Compound | Comment | Organism | Structure |
---|---|---|---|
EDTA | the enzyme activity increases obviously in the presence of 5 mM EDTA | Decapterus maruadsi |
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 Maximum [Da] | Comment | Organism |
---|---|---|---|
30000 | - |
x * 30000, SDS-PAGE | Decapterus maruadsi |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
casein + H2O | Decapterus maruadsi | - |
? | - |
? | |
myosin heavy chain + H2O | Decapterus maruadsi | - |
? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Decapterus maruadsi | - |
blue scad | - |
Purification (Comment) | Organism |
---|---|
SP-Sepharose column chromatography, High S Cartridge column chromatography and Concanavalin A-Sepharose 4B affinity column chromatography | Decapterus maruadsi |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
skeletal muscle | - |
Decapterus maruadsi | - |
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 | Comment | Organism |
---|---|---|
? | x * 30000, SDS-PAGE | Decapterus maruadsi |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
55 | - |
- |
Decapterus maruadsi |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
40 | 65 | more than 50% activity between 40 and 65°C | Decapterus maruadsi |
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 Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
5.5 | - |
- |
Decapterus maruadsi |
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 |