Activating Compound | Comment | Organism | Structure |
---|---|---|---|
Triton X-100 | - |
Rattus norvegicus |
Cloned (Comment) | Organism |
---|---|
expressed in CHO cells | Rattus norvegicus |
Protein Variants | Comment | Organism |
---|---|---|
additional information | preparation of a matriptase pseudozymogen (HL-matriptase zymogen): secreted variant of matriptase consisting of the entire extracellular domain (Tyr81 to Val855), activation-cleavage sequence (Thr-Lys-Gln-Ala-Arg614) is replaced with the enterokinase recognition sequence (Asp-Asp-Asp-Asp-Lys). Pseudozymogen is converted to HL-matriptase enzyme (activated) by incubation with enterokinase. Pseudozymogen exhibits optimal activity toward substrate acetyl-Lys-Thr-Lys-Gln-Leu-Arg-methyl-coumaryl-7-amide at pH 6.0 (mildly acidic). Substrate hydrolysis at pH 6.0 with 145 mM NaCl is inhibited. In a buffer of pH 6.0 containing 5 mM NaCl (low ionic strength), the activity of pseudozymogen is only 30times lower than that of the respective two-chain form (activated form after enterokinase treatment). This finding indicates that the in vivo activation of matriptase occurs via a mechanism involving the activity of zymogen | Rattus norvegicus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Na+ | in a buffer containing 5 mM NaCl the activity of a pseudozymogen form of recombinant matriptase (HL-matriptase) is only 30times lower than that of the respective two-chain form (activated form after enterokinase treatment) | Rattus norvegicus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rattus norvegicus | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
proteolytic modification | matriptase is first synthesized as a zymogen comprising 855 amino-acid residues, which requires processing by cleavage between Arg614 and Val615 (activation cleavage) to generate the disulfide-linked-two-chain fully active enzyme. In vivo activation of matriptase occurs via a mechanism involving the activity of zymogen | Rattus norvegicus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetyl-Lys-Thr-Lys-Gln-Leu-Arg-4-methylcoumarin-7-amide + H2O | substrate almost matches the P5 to P1 residues of matriptase zymogen: P5(Thr)-P4(Lys)-P3(Gln)-P2(Ala)-P1(Arg). The hydrolysis of the substrate is expected to mimic the situation of activation cleavage of matriptase zymogen | Rattus norvegicus | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
matriptase | - |
Rattus norvegicus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Rattus norvegicus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | - |
optimal activity toward the substrate | Rattus norvegicus |