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Literature summary for 3.4.22.27 extracted from

  • Sun, B.G.; Chi, H.
    Cathepsin S of Sciaenops ocellatus identification, transcriptional expression and enzymatic activity (2016), Int. J. Biol. Macromol., 82, 76-82 .
    View publication on PubMed
Search for more literature for 3.4.22.27

Cloned(Commentary)

Cloned (Comment) Organism
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis Sciaenops ocellatus

Protein Variants

Protein Variants Comment Organism
C146A site-directed mutagenesis, inactive active site mutant Sciaenops ocellatus

Inhibitors

Inhibitors Comment Organism Structure
E-64 strong inhibition Sciaenops ocellatus

Organism

Organism UniProt Comment Textmining
Sciaenops ocellatus A0A0K0M968
-
-

Source Tissue

Source Tissue Comment Organism Textmining
kidney
-
 Sciaenops ocellatus
-
liver
-
 Sciaenops ocellatus
-
additional information SoCatS expression is detected in various tissues Sciaenops ocellatus
-
spleen
-
 Sciaenops ocellatus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-benzyloxycarbonyl-Phe-Arg-4-nitroanilide + H2O
-
 Sciaenops ocellatus N-benzyloxycarbonyl-Phe-Arg + 4-nitroaniline
-
 ?

Subunits

Subunits Comment Organism
? x * 37330, sequence calculation Sciaenops ocellatus
More enzyme SoCatS possesses the typical cathepsin S domain architecture, i.e. a signal peptide (residues 1-21), an N-terminal proregion known as protease inhibitor I-29 (residues 34-94), and a C-terminal C1-peptidase domain (residues 122-337) Sciaenops ocellatus

Synonyms

Synonyms Comment Organism
SoCatS
-
 Sciaenops ocellatus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
-
 Sciaenops ocellatus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
 Sciaenops ocellatus

pI Value

Organism Comment pI Value Maximum pI Value
Sciaenops ocellatus sequence calculation
-
 6.07

Expression

Organism Comment Expression
Sciaenops ocellatus SoCatS expression is enhanced by bacterial infection with fish pathogenic Edwardsiella tarda, a fish pathogen. In kidney, significant induction of SoCatS occurs at 4 h (2.31fold) and 8 h (2.55fold) post-infection. In liver, significant induction of SoCatS (3.0fold) is only observed at 24 h post-infection. In spleen, SoCatS expression is significantly upregulated at 12 h post-infection (5.46fold) and at 24 h post-infection (4.23fold) up

General Information

General Information Comment Organism
evolution cathepsin S homologues are papain-like proteases. SoCatS is evolutionally close to the cathepsin S of other teleost fish (with 60-90% overall sequence identities), especially to Miichthys miiuy (Sciaena miiuy), a member of Sciaenidae family like red drum Sciaenops ocellatus
additional information enzyme SoCatS possesses a peptidase domain with four catalytically essential residues, Gln140, Cys146, His285, and Asn305, Asn305, and a characteristic ERWNI/VN motif of cathepsin L family. The catalytic residue is Cys146. Enzyme structure homology modelling, the enzyme structure displays a typical papain-type fold, overview Sciaenops ocellatus