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Literature summary for 3.4.22.15 extracted from

  • Sun, B.G.; Hu, Y.H.
    Identification, mRNA expression profiling and activity characterization of cathepsin L from red drum (Sciaenops ocellatus) (2015), Fish Physiol. Biochem., 41, 1463-1473 .
    View publication on PubMed
Search for more literature for 3.4.22.15

Cloned(Commentary)

Cloned (Comment) Organism
phylogenetic analysis and tree, quantitative real-time RT-PCR enzyme expression analysis, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Sciaenops ocellatus

Protein Variants

Protein Variants Comment Organism
C143A site-directed mutagenesis Sciaenops ocellatus

Localization

Localization Comment Organism GeneOntology No. Textmining
lysosome
-
 Sciaenops ocellatus 5764
-

Organism

Organism UniProt Comment Textmining
Sciaenops ocellatus A0A0K0M968
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and ultrafiltration Sciaenops ocellatus

Source Tissue

Source Tissue Comment Organism Textmining
blood low expression level Sciaenops ocellatus
-
brain
-
 Sciaenops ocellatus
-
gill
-
 Sciaenops ocellatus
-
heart high expression level Sciaenops ocellatus
-
intestine
-
 Sciaenops ocellatus
-
kidney low expression level Sciaenops ocellatus
-
liver
-
 Sciaenops ocellatus
-
additional information quantitative real-time RT-PCR enzyme SoCatL expression analysis in red drum tissues, overview Sciaenops ocellatus
-
muscle
-
 Sciaenops ocellatus
-
spleen high expression level Sciaenops ocellatus
-

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
? x * 36940, sequence calculation Sciaenops ocellatus
More SoCatL possesses a typical domain arrangement characteristic of cathepsin L, which comprises a proregion and a protease domain with four catalytically essential residues (Gln137, Cys143, His282 and Asn302) conserved in various organisms. The enzyme possesses the typical cathepsin L-like domain architecture, i.e. a signal peptide (residues 1-19), an N-terminal proregion classified as protease inhibitor I-29 (residues 27-87) and a C-terminal C1-peptidase domain (residues 119-334) Sciaenops ocellatus

Synonyms

Synonyms Comment Organism
CatL
-
 Sciaenops ocellatus
SoCatL
-
 Sciaenops ocellatus

Temperature Optimum [°C]

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

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
30 60 over 50% of maximal activity within this range, profile overview Sciaenops ocellatus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
 first peak Sciaenops ocellatus
7
-
 second peak Sciaenops ocellatus

pH Range

pH Minimum pH Maximum Comment Organism
3.5 8 over 25% of maximal activity within this range, profile overview Sciaenops ocellatus

pI Value

Organism Comment pI Value Maximum pI Value
Sciaenops ocellatus sequence calculation
-
 4.87

General Information

General Information Comment Organism
evolution phylogenetic analysis reveals that SoCatL is evolutionally close to fish cathepsin L, especially those belonging to the Perciformes order. The enzyme possesses the typical cathepsin L-like domain architecture, i.e. a signal peptide (residues 1-19), an N-terminal proregion classified as protease inhibitor I-29 (residues 27-87) and a C-terminal C1-peptidase domain (residues 119-334) Sciaenops ocellatus
additional information the activity of rSoCatL requires the catalytic residue Cys143. The homology model of SoCatL shows that it exhibits a structure resembling human cathepsin L. Homology model of mature SoCatL, overview Sciaenops ocellatus
physiological function enzyme SoCatL is a teleost cathepsin L homologue which functions as a cysteine protease and is likely to participate in the host immune response against bacterial infection Sciaenops ocellatus