3.4.11.B7: arginyl aminopeptidase PH1704
This is an abbreviated version!
For detailed information about arginyl aminopeptidase PH1704, go to the full flat file.
Reaction
the enzyme is an aminopeptidase with limited specificity, mainly releasing the N-terminal L-arginine and hardly cleaving other amino acids. L-Arg-7-amido-4-methylcoumarin is the best artificial substrate =
Synonyms
arginine-specific aminopeptidase, PH1704, PH1704 protease
ECTree
3.4.11.B7 arginyl aminopeptidase PH1704Advanced search results
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Substrates Products on EC 3.4.11.B7 - arginyl aminopeptidase PH1704
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-Val-7-amido-4-methylcoumarin + H2O
L-Val + 7-amino-4-methylcoumarin
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
-
-
?
Ala-Ala-Phe-Arg-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe-Arg + 7-amino-4-methylcoumarin
Glu12 is responsible for substrate binding
-
-
?
Ala-Ala-Phe-Arg-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe-Arg + 7-amino-4-methylcoumarin
Glu12 is responsible for substrate binding
-
-
?
L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala + 7-amino-4-methylcoumarin
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
-
-
?
L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala + 7-amino-4-methylcoumarin
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
-
-
?
L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala + 7-amino-4-methylcoumarin
-
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
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
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
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
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
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
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
-
-
?
L-Asp-7-amido-4-methylcoumarin + H2O
L-Asp + 7-amino-4-methylcoumarin
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
-
-
?
L-Asp-7-amido-4-methylcoumarin + H2O
L-Asp + 7-amino-4-methylcoumarin
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
-
-
?
L-Asp-7-amido-4-methylcoumarin + H2O
L-Asp + 7-amino-4-methylcoumarin
-
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
-
-
?
L-Phe-7-amido-4-methylcoumarin + H2O
L-Phe + 7-amino-4-methylcoumarin
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
-
-
?
L-Phe-7-amido-4-methylcoumarin + H2O
L-Phe + 7-amino-4-methylcoumarin
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
-
-
?
L-Phe-7-amido-4-methylcoumarin + H2O
L-Phe + 7-amino-4-methylcoumarin
-
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
-
-
?
L-Ser-7-amido-4-methylcoumarin + H2O
L-Ser + 7-amino-4-methylcoumarin
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
-
-
?
L-Ser-7-amido-4-methylcoumarin + H2O
L-Ser + 7-amino-4-methylcoumarin
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
-
-
?
L-Ser-7-amido-4-methylcoumarin + H2O
L-Ser + 7-amino-4-methylcoumarin
-
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
-
-
?
