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Literature summary for 3.4.21.109 extracted from

  • Inouye, K.; Yasumoto, M.; Tsuzuki, S.; Mochida, S.; Fushiki, T.
    The optimal activity of a pseudozymogen form of recombinant matriptase under the mildly acidic pH and low ionic strength conditions (2010), J. Biochem., 147, 485-492.
    View publication on PubMed
Search for more literature for 3.4.21.109

Activating Compound

Activating Compound Comment Organism Structure
Triton X-100
-
 Rattus norvegicus

Cloned(Commentary)

Cloned (Comment) Organism
expressed in CHO cells Rattus norvegicus

Protein Variants

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

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

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Posttranslational Modification

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 and Products (Substrate)

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

Synonyms Comment Organism
matriptase
-
 Rattus norvegicus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Rattus norvegicus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
 optimal activity toward the substrate Rattus norvegicus