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Literature summary for 3.4.11.B7 extracted from
- Characterization of the PH1704 protease from Pyrococcus horikoshii OT3 and the critical functions of Tyr120 (2014), PLoS One, 9, e103902.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Pyrococcus horikoshii |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| Y120P | kat and kat/Km of the mutant enzyme with L-Arg-7-amino-4-methylcoumarin are about 7 and 7.8times higher than that of the wild type enzyme, respectively | Pyrococcus horikoshii |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| iodoacetamide | strongly inhibits the peptidase activity, confirming that Cys100 is a nucleophilic residue | Pyrococcus horikoshii |  |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | 5 mM, 29% inhibition of protease activity | Pyrococcus horikoshii | |
| Co2+ | 0.2 mM, 75% inhibition of protease activity | Pyrococcus horikoshii | |
| Cu2+ | 0.2 mM, 57% inhibition of protease activity | Pyrococcus horikoshii | |
| Fe3+ | 0.2 mM, 27% inhibition of protease activity | Pyrococcus horikoshii | |
| K+ | 5 mM, 19% inhibition of protease activity | Pyrococcus horikoshii | |
| Mg2+ | 5 mM, 10% inhibition of protease activity | Pyrococcus horikoshii | |
| Mn2+ | 5 mM, 81% inhibition of protease activity | Pyrococcus horikoshii | |
| Na+ | 5 mM, 28% inhibition of protease activity | Pyrococcus horikoshii | |
| Ni2+ | 0.2 mM, 84% inhibition of protease activity | Pyrococcus horikoshii | |
| Zn2+ | 0.2 mM, 63% inhibition of protease activity | Pyrococcus horikoshii | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 240000 | - |
non-denaturing PAGE | Pyrococcus horikoshii |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pyrococcus horikoshii | O59413 | - |
- |
| Pyrococcus horikoshii DSM 12428 | O59413 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Pyrococcus horikoshii |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-Ala-7-amido-4-methylcoumarin + H2O | the specific activity for hydrolyzing L-Arg-7-amido-4-methylcoumarin is 90times to 300times higher than those hydrolyzing L-Asp-7-amido-4-methylcoumarin, L-Ala-7-amido-4-methylcoumarin, L-Val-7-amido-4-methylcoumarin, L-Phe-7-amido-4-methylcoumarin or L-Ser-7-amido-4-methylcoumarin. Arginine, phenylalanine, alanine, valine, aspartate, and serine substrates are hydrolyzed with decreasing efficiency, in that order | Pyrococcus horikoshii | L-Ala + 7-amino-4-methylcoumarin | - |
? | |
| L-Ala-7-amido-4-methylcoumarin + H2O | the specific activity for hydrolyzing L-Arg-7-amido-4-methylcoumarin is 90times to 300times higher than those hydrolyzing L-Asp-7-amido-4-methylcoumarin, L-Ala-7-amido-4-methylcoumarin, L-Val-7-amido-4-methylcoumarin, L-Phe-7-amido-4-methylcoumarin or L-Ser-7-amido-4-methylcoumarin. Arginine, phenylalanine, alanine, valine, aspartate, and serine substrates are hydrolyzed with decreasing efficiency, in that order | Pyrococcus horikoshii DSM 12428 | L-Ala + 7-amino-4-methylcoumarin | - |
? | |
| L-Ala-7-amido-4-methylcoumarin + H2O | the specific activity for hydrolyzing L-Arg-7-amido-4-methylcoumarin is 90times to 300times higher than those hydrolyzing L-Asp-7-amido-4-methylcoumarin, L-Ala-7-amido-4-methylcoumarin, L-Val-7-amido-4-methylcoumarin, L-Phe-7-amido-4-methylcoumarin or L-Ser-7-amido-4-methylcoumarin. Arginine, phenylalanine, alanine, valine, aspartate, and serine substrates are hydrolyzed with decreasing efficiency, in that order | Pyrococcus horikoshii OT-3 | L-Ala + 7-amino-4-methylcoumarin | - |
? | |
| L-Arg-7-amido-4-methylcoumarin + H2O | the enzyme is also identified as an cysteine endopeptidase. Activity with the endopeptidase substrate Ala-Ala-Phe-Arg-7-amido-4-methylcoumarin is 10% compared to the activity with the aminopeptidase substrate L-Arg-7-amido-4-methylcoumarin. The enzyme exhibits primal aminopeptidase activity. The specific activity for hydrolyzing L-Arg-7-amido-4-methylcoumarin is 90times to 300times higher than those hydrolyzing L-Asp-7-amido-4-methylcoumarin, L-Ala-7-amido-4-methylcoumarin, L-Val-7-amido-4-methylcoumarin, L-Phe-7-amido-4-methylcoumarin or L-Ser-7-amido-4-methylcoumarin. Arginine, phenylalanine, alanine, valine, aspartate, and serine substrates are hydrolyzed with decreasing efficiency, in that order | Pyrococcus horikoshii | L-Arg + 7-amino-4-methylcoumarin | - |
? | |
| L-Arg-7-amido-4-methylcoumarin + H2O | the enzyme is also identified as an cysteine endopeptidase. Activity with the endopeptidase substrate Ala-Ala-Phe-Arg-7-amido-4-methylcoumarin is 10% compared to the activity with the aminopeptidase substrate L-Arg-7-amido-4-methylcoumarin. The enzyme exhibits primal aminopeptidase activity. The specific activity for hydrolyzing L-Arg-7-amido-4-methylcoumarin is 90times to 300times higher than those hydrolyzing L-Asp-7-amido-4-methylcoumarin, L-Ala-7-amido-4-methylcoumarin, L-Val-7-amido-4-methylcoumarin, L-Phe-7-amido-4-methylcoumarin or L-Ser-7-amido-4-methylcoumarin. Arginine, phenylalanine, alanine, valine, aspartate, and serine substrates are hydrolyzed with decreasing efficiency, in that order | Pyrococcus horikoshii DSM 12428 | L-Arg + 7-amino-4-methylcoumarin | - |
? | |
| L-Arg-7-amido-4-methylcoumarin + H2O | the enzyme is also identified as an cysteine endopeptidase. Activity with the endopeptidase substrate Ala-Ala-Phe-Arg-7-amido-4-methylcoumarin is 10% compared to the activity with the aminopeptidase substrate L-Arg-7-amido-4-methylcoumarin. The enzyme exhibits primal aminopeptidase activity. The specific activity for hydrolyzing L-Arg-7-amido-4-methylcoumarin is 90times to 300times higher than those hydrolyzing L-Asp-7-amido-4-methylcoumarin, L-Ala-7-amido-4-methylcoumarin, L-Val-7-amido-4-methylcoumarin, L-Phe-7-amido-4-methylcoumarin or L-Ser-7-amido-4-methylcoumarin. Arginine, phenylalanine, alanine, valine, aspartate, and serine substrates are hydrolyzed with decreasing efficiency, in that order | Pyrococcus horikoshii OT-3 | L-Arg + 7-amino-4-methylcoumarin | - |
? | |
| L-Asp-7-amido-4-methylcoumarin + H2O | the specific activity for hydrolyzing L-Arg-7-amino-4-methylcoumarin is 90times to 300times higher than those hydrolyzing L-Asp-7-amino-4-methylcoumarin, L-Ala-7-amino-4-methylcoumarin, L-Val-7-amino-4-methylcoumarin, L-Phe-7-amino-4-methylcoumarin or L-Ser-7-amino-4-methylcoumarin. Arginine, phenylalanine, alanine, valine, aspartate, and serine substrates are hydrolyzed with decreasing efficiency, in that order | Pyrococcus horikoshii | L-Asp + 7-amino-4-methylcoumarin | - |
? | |
| L-Asp-7-amido-4-methylcoumarin + H2O | the specific activity for hydrolyzing L-Arg-7-amino-4-methylcoumarin is 90times to 300times higher than those hydrolyzing L-Asp-7-amino-4-methylcoumarin, L-Ala-7-amino-4-methylcoumarin, L-Val-7-amino-4-methylcoumarin, L-Phe-7-amino-4-methylcoumarin or L-Ser-7-amino-4-methylcoumarin. Arginine, phenylalanine, alanine, valine, aspartate, and serine substrates are hydrolyzed with decreasing efficiency, in that order | Pyrococcus horikoshii DSM 12428 | L-Asp + 7-amino-4-methylcoumarin | - |
? | |
| L-Asp-7-amido-4-methylcoumarin + H2O | the specific activity for hydrolyzing L-Arg-7-amino-4-methylcoumarin is 90times to 300times higher than those hydrolyzing L-Asp-7-amino-4-methylcoumarin, L-Ala-7-amino-4-methylcoumarin, L-Val-7-amino-4-methylcoumarin, L-Phe-7-amino-4-methylcoumarin or L-Ser-7-amino-4-methylcoumarin. Arginine, phenylalanine, alanine, valine, aspartate, and serine substrates are hydrolyzed with decreasing efficiency, in that order | Pyrococcus horikoshii OT-3 | L-Asp + 7-amino-4-methylcoumarin | - |
? | |
| L-Phe-7-amido-4-methylcoumarin + H2O | the specific activity for hydrolyzing L-Arg-7-amido-4-methylcoumarin is 90times to 300times higher than those hydrolyzing L-Asp-7-amido-4-methylcoumarin, L-Ala-7-amido-4-methylcoumarin, L-Val-7-amido-4-methylcoumarin, L-Phe-7-amido-4-methylcoumarin or L-Ser-7-amido-4-methylcoumarin. Arginine, phenylalanine, alanine, valine, aspartate, and serine substrates are hydrolyzed with decreasing efficiency, in that order | Pyrococcus horikoshii | L-Phe + 7-amino-4-methylcoumarin | - |
? | |
| L-Phe-7-amido-4-methylcoumarin + H2O | the specific activity for hydrolyzing L-Arg-7-amido-4-methylcoumarin is 90times to 300times higher than those hydrolyzing L-Asp-7-amido-4-methylcoumarin, L-Ala-7-amido-4-methylcoumarin, L-Val-7-amido-4-methylcoumarin, L-Phe-7-amido-4-methylcoumarin or L-Ser-7-amido-4-methylcoumarin. Arginine, phenylalanine, alanine, valine, aspartate, and serine substrates are hydrolyzed with decreasing efficiency, in that order | Pyrococcus horikoshii DSM 12428 | L-Phe + 7-amino-4-methylcoumarin | - |
? | |
| L-Phe-7-amido-4-methylcoumarin + H2O | the specific activity for hydrolyzing L-Arg-7-amido-4-methylcoumarin is 90times to 300times higher than those hydrolyzing L-Asp-7-amido-4-methylcoumarin, L-Ala-7-amido-4-methylcoumarin, L-Val-7-amido-4-methylcoumarin, L-Phe-7-amido-4-methylcoumarin or L-Ser-7-amido-4-methylcoumarin. Arginine, phenylalanine, alanine, valine, aspartate, and serine substrates are hydrolyzed with decreasing efficiency, in that order | Pyrococcus horikoshii OT-3 | L-Phe + 7-amino-4-methylcoumarin | - |
? | |
| L-Ser-7-amido-4-methylcoumarin + H2O | the specific activity for hydrolyzing L-Arg-7-amino-4-methylcoumarin is 90times to 300times higher than those hydrolyzing L-Asp-7-amido-4-methylcoumarin, L-Ala-7-amido-4-methylcoumarin, L-Val-7-amido-4-methylcoumarin, L-Phe-7-amido-4-methylcoumarin or L-Ser-7-amido-4-methylcoumarin. Arginine, phenylalanine, alanine, valine, aspartate, and serine substrates are hydrolyzed with decreasing efficiency, in that order | Pyrococcus horikoshii | L-Ser + 7-amino-4-methylcoumarin | - |
? | |
| L-Ser-7-amido-4-methylcoumarin + H2O | the specific activity for hydrolyzing L-Arg-7-amino-4-methylcoumarin is 90times to 300times higher than those hydrolyzing L-Asp-7-amido-4-methylcoumarin, L-Ala-7-amido-4-methylcoumarin, L-Val-7-amido-4-methylcoumarin, L-Phe-7-amido-4-methylcoumarin or L-Ser-7-amido-4-methylcoumarin. Arginine, phenylalanine, alanine, valine, aspartate, and serine substrates are hydrolyzed with decreasing efficiency, in that order | Pyrococcus horikoshii DSM 12428 | L-Ser + 7-amino-4-methylcoumarin | - |
? | |
| L-Ser-7-amido-4-methylcoumarin + H2O | the specific activity for hydrolyzing L-Arg-7-amino-4-methylcoumarin is 90times to 300times higher than those hydrolyzing L-Asp-7-amido-4-methylcoumarin, L-Ala-7-amido-4-methylcoumarin, L-Val-7-amido-4-methylcoumarin, L-Phe-7-amido-4-methylcoumarin or L-Ser-7-amido-4-methylcoumarin. Arginine, phenylalanine, alanine, valine, aspartate, and serine substrates are hydrolyzed with decreasing efficiency, in that order | Pyrococcus horikoshii OT-3 | L-Ser + 7-amino-4-methylcoumarin | - |
? | |
| L-Val-7-amido-4-methylcoumarin + H2O | the specific activity for hydrolyzing L-Arg-7-amido-4-methylcoumarin is 90times to 300times higher than those hydrolyzing L-Asp-7-amido-4-methylcoumarin, L-Ala-7-amido-4-methylcoumarin, L-Val-7-amido-4-methylcoumarin, L-Phe-7-amido-4-methylcoumarin or L-Ser-7-amido-4-methylcoumarin. Arginine, phenylalanine, alanine, valine, aspartate, and serine substrates are hydrolyzed with decreasing efficiency, in that order | Pyrococcus horikoshii | L-Val + 7-amino-4-methylcoumarin | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dodecamer | - |
Pyrococcus horikoshii |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| arginine-specific aminopeptidase | - |
Pyrococcus horikoshii |
| PH1704 protease | ambiguous, the recombinant protein is also identified as a cysteine endopeptidase | Pyrococcus horikoshii |
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