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Literature summary for 3.4.22.15 extracted from

  • Shen, J.D.; Cai, Q.F.; Yan, L.J.; Du, C.H.; Liu, G.M.; Su, W.J.; Ke, C.; Cao, M.J.
    Cathepsin L is an immune-related protein in Pacific abalone (Haliotis discus hannai) - purification and characterization (2015), Fish Shellfish Immunol., 47, 986-995 .
    View publication on PubMed

Activating Compound

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(Commentary)

Cloned (Comment) Organism
cloned from the hepatopancreas, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree Haliotis discus hannai

Inhibitors

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

Localization Comment Organism GeneOntology No. Textmining
extracellular the enzyme has a putative signal peptide cleavage site, pro-region cleavage site Haliotis discus hannai
-
-

Organism

Organism UniProt Comment Textmining
Haliotis discus hannai K7QTY9
-
-

Posttranslational Modification

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 (Commentary)

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

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 and Products (Substrate)

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

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 [°C] Temperature Optimum Maximum [°C] Comment Organism
35
-
-
Haliotis discus hannai

Temperature Range [°C]

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 [°C]

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

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5
-
-
Haliotis discus hannai

pH Range

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 pH Stability Maximum Comment Organism
3.5 6.6 over 50% activity remaining, profile overview Haliotis discus hannai

pI Value

Organism Comment pI Value Maximum pI Value
Haliotis discus hannai sequence calculation
-
6.7

Expression

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

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