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Literature summary for 3.4.21.109 extracted from
- Role of the stem domain of matriptase in the interaction with its physiological inhibitor, hepatocyte growth factor activator inhibitor type I (2009), J. Biochem., 145, 783-790.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| enterokinase | - |
Rattus norvegicus | |
| additional information | transactivation | Rattus norvegicus |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| two soluble variants, containing the entire extracellular domains, Tyr81 - Val855, and the catalytic domain, Asp603 - Val855, are produced, the vectors pT7blue2 and pSec-ek-MT-SP1 are used | Rattus norvegicus |
| using CHO-K1 cells, secreted variants of rat r-matriptase consisting of the entire extracellular domains (Tyr81-Val855) (HL-matriptase) and of the catalytic domain (and its N-terminal spacer region) (Asp603-Val855) (L-matriptase) are produced. They are activated in vitro by r-enteropeptidase | Rattus norvegicus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D603-V855 | using CHO-K1 cells, a secreted variant of rat r-matriptase consisting of the of the catalytic domain (and its N-terminal spacer region) (Asp603Val855) L-matriptase is produced. HL-matriptase and L-matriptase are inhibited by purified maHAI-1 with a similar extent when t-butyloxycarbonyl-Gln-Ala-Arg-MCA and acetyl-Lys-Thr-Lys-Gln-Leu-Arg-MCA are were used as substrates | Rattus norvegicus |
| Y81-V855 | using CHO-K1 cells, a secreted variant of rat r-matriptase consisting of the entire extracellular domains (Tyr81-Val855) HL-matriptase is produced (variant contains the stem domain). HL-matriptase and L-matriptase are inhibited by purified maHAI-1 with a similar extent when t-butyloxycarbonyl-Gln-Ala-Arg-MCA and acetyl-Lys-Thr-Lys-Gln-Leu-Arg-MCA are were used as substrates. HL-matriptase is inhibited more strongly than L-matriptase by maHAI-1 in the hydrolysis of t-butyloxycarbonyl-[(2S)-2-amino-3-(benzyloxycarbonyl)propionyl]-Pro-Arg-MCA. The stem domain of matriptase facilitates the inhibitory interaction of this protease with maHAI-1 in the hydrolysis of t-butyloxycarbonyl-[(2S)-2-amino-3-(benzyloxycarbonyl)propionyl]-Pro-Arg-MCA | Rattus norvegicus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| hepatocyte growth factor activator inhibitor type I | inhibition activities of a cell membrane-anchored form of recombinant HAI-1 (maHAI-1) against different matriptase variants in the hydrolysis of peptidyl-4-methyl-coumaryl-7-amide (MCA) substrates are compared: stem domain of matriptase affects the interaction between this protease and HAI-1 | Rattus norvegicus |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | - |
Rattus norvegicus | 16020 | - |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| pro-hepatocyte growth factor + H2O | Rattus norvegicus | - |
? | - |
? |  |
| pro-urokinase-type plasminogen activator + H2O | Rattus norvegicus | - |
? | - |
? | |
| prostatin + H2O | Rattus norvegicus | - |
? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rattus norvegicus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Rattus norvegicus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| enterocyte | - |
Rattus norvegicus | - |
| epithelial cell | - |
Rattus norvegicus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| acetyl-L-lysyl-L-threonyl-L-lysyl-L-glutaminyl-L-leucyl-L-arginine-4-methylcoumaryl-7-amide + H2O | - |
Rattus norvegicus | ? | - |
? | |
| acetyl-Lys-Thr-Lys-Gln-Leu-Arg-4-methyl-coumaryl-7-amide + H2O | - |
Rattus norvegicus | acetyl-Lys-Thr-Lys-Gln-Leu-Arg + 7-amino-4-methylcoumarin | - |
? | |
| pro-hepatocyte growth factor + H2O | - |
Rattus norvegicus | ? | - |
? | |
| pro-urokinase-type plasminogen activator + H2O | - |
Rattus norvegicus | ? | - |
? | |
| prostatin + H2O | - |
Rattus norvegicus | ? | - |
? | |
| t-butyloxycarbonyl-Gln-Ala-Arg-4-methyl-coumaryl-7-amide + H2O | - |
Rattus norvegicus | t-butyloxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin | - |
? | |
| t-butyloxycarbonyl-L-glutamyl-L-alanyl-L-arginine-4-methylcoumaryl-7-amide + H2O | - |
Rattus norvegicus | ? | - |
? | |
| t-butyloxycarbonyl-[(2S)-2-amino-3-(benzyloxycarbonyl)propionyl]-L-prolyl-L-arginine-4-methylcoumaryl-7-amide + H2O | - |
Rattus norvegicus | ? | - |
? | |
| t-butyloxycarbonyl-[(2S)-2-amino-3-(benzyloxycarbonyl)propionyl]-Pro-Arg-4-methyl-coumaryl-7-amide + H2O | - |
Rattus norvegicus | t-butyloxycarbonyl-[(2S)-2-amino-3-(benzyloxycarbonyl)propionyl]-Pro-Arg + 7-amino-4-methylcoumarin | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| epithin | - |
Rattus norvegicus |
| matriptase | - |
Rattus norvegicus |
| membrane-type serine protease 1 | - |
Rattus norvegicus |
| r-matripase | - |
Rattus norvegicus |
| suppression of tumorigenecity 14 | - |
Rattus norvegicus |
| type II transmembrane serine protease | - |
Rattus norvegicus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Rattus norvegicus |
| 37 | - |
activity assay | Rattus norvegicus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Rattus norvegicus |
| 7.5 | - |
activity assay | Rattus norvegicus |
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