Activating Compound | Comment | Organism | Structure |
---|---|---|---|
EDTA | about 3fold activation at 5 mM | Haliotis discus hannai | |
EGTA | about 3fold activation at 5 mM | Haliotis discus hannai |
Cloned (Comment) | Organism |
---|---|
cloned from the hepatopancreas, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree | Haliotis discus hannai |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
benzamidine | 17% inhibition at 5 mM | Haliotis discus hannai | |
chymostatin | 95% inhibition at 0.1 mM | Haliotis discus hannai | |
E-64 | 98% inhibition at 0.01 mM | Haliotis discus hannai | |
leupeptin | 98% inhibition at 0.1 mM | Haliotis discus hannai | |
PMSF | 37.5% inhibition at 5 mM | Haliotis discus hannai |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | the enzyme has a putative signal peptide cleavage site, pro-region cleavage site | Haliotis discus hannai | - |
- |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Haliotis discus hannai | K7QTY9 | - |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
glycoprotein | the enzyme contains a potential N-glycosylation site | Haliotis discus hannai |
proteolytic modification | the pro-enzyme has a pro-region cleavage site for signal peptide cleavage | Haliotis discus hannai |
Purification (Comment) | Organism |
---|---|
native enzyme is purified from the hepatopancreas by ammonium sulfate fractionation, cation exchange chromatography, and preparative gel filtration | Haliotis discus hannai |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
adductor | - |
Haliotis discus hannai | - |
gill | - |
Haliotis discus hannai | - |
hemocyte | - |
Haliotis discus hannai | - |
hepatopancreas | higher expression level | Haliotis discus hannai | - |
mantle | - |
Haliotis discus hannai | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O | - |
Haliotis discus hannai | benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 28000-28500, SDS-PAGE, x * 36700, proenzyme, sequence calculation | Haliotis discus hannai |
More | peptide mass fingerprinting analysis | Haliotis discus hannai |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
35 | - |
- |
Haliotis discus hannai |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
10 | 50 | over 50% of maximal activity within this range, profile overview | Haliotis discus hannai |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
20 | - |
purified native enzyme, pH 5.5, completely stable up to | Haliotis discus hannai |
35 | - |
about, purified native enzyme, pH 5.5, loss of 50% activity | Haliotis discus hannai |
35 | - |
purified native enzyme, pH 5.5, inactivation | Haliotis discus hannai |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
5.5 | - |
- |
Haliotis discus hannai |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
5 | 6 | over 50% of maximal activity within this range, profile overview | Haliotis discus hannai |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
3.5 | 6.6 | over 50% activity remaining, profile overview | Haliotis discus hannai |
Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|
Haliotis discus hannai | sequence calculation | - |
6.7 |
Organism | Comment | Expression |
---|---|---|
Haliotis discus hannai | the expression and enzyme activity of cathepsin L are significantly upregulated in hepatopancreas at 8 h following Vibrio parahaemolyticus infection | up |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme sequence comtains conserved ERFNIN, GNYD, and GCGG motifs, which are characteristics of cathepsin L | Haliotis discus hannai |
additional information | the conserved catalytic triad is formed by residues Cys134, His273, and Asn293. The mature enzyme of abalone contains a Gln128 residue forming an oxyanion hole and a highly conserved catalytic triad, which are crucial for the stabilization of three-dimensional structure of cathepsin L. Six potential substrate binding sites are detected: Leu178, Met179, Ala244, Leu272, Gly274, and Gln320 | Haliotis discus hannai |
physiological function | cathepsin L is an immune-related protein in Pacific abalone. The expression and enzyme activity of cathepsin L are significantly upregulated in hepatopancreas at 8 h following Vibrio parahaemolyticus infection | Haliotis discus hannai |