Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Pyrococcus horikoshii |
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 | Comment | Organism | Structure |
---|---|---|---|
iodoacetamide | strongly inhibits the peptidase activity, confirming that Cys100 is a nucleophilic residue | Pyrococcus horikoshii |
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 Maximum [Da] | Comment | Organism |
---|---|---|---|
240000 | - |
non-denaturing PAGE | Pyrococcus horikoshii |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pyrococcus horikoshii | O59413 | - |
- |
Pyrococcus horikoshii DSM 12428 | O59413 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Pyrococcus horikoshii |
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 | Comment | Organism |
---|---|---|
dodecamer | - |
Pyrococcus horikoshii |
Synonyms | Comment | Organism |
---|---|---|
arginine-specific aminopeptidase | - |
Pyrococcus horikoshii |
PH1704 protease | ambiguous, the recombinant protein is also identified as a cysteine endopeptidase | Pyrococcus horikoshii |