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EC Number Substrates Commentary Substrates Organism Products Commentary (Products) Reversibility
Display the reaction diagram Show all sequences 3.4.11.B7Ala-Ala-Phe-Arg-7-amido-4-methylcoumarin + H2O Glu12 is responsible for substrate binding Pyrococcus horikoshii Ala-Ala-Phe-Arg + 7-amino-4-methylcoumarin - ?
Display the reaction diagram Show all sequences 3.4.11.B7Ala-Ala-Phe-Arg-7-amido-4-methylcoumarin + H2O Glu12 is responsible for substrate binding Pyrococcus horikoshii DSM 12428 Ala-Ala-Phe-Arg + 7-amino-4-methylcoumarin - ?
Display the reaction diagram Show all sequences 3.4.11.B7L-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 - ?
Display the reaction diagram Show all sequences 3.4.11.B7L-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 - ?
Display the reaction diagram Show all sequences 3.4.11.B7L-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 - ?
Display the reaction diagram Show all sequences 3.4.11.B7L-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 - ?
Display the reaction diagram Show all sequences 3.4.11.B7L-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 - ?
Display the reaction diagram Show all sequences 3.4.11.B7L-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 - ?
Display the reaction diagram Show all sequences 3.4.11.B7L-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 - ?
Display the reaction diagram Show all sequences 3.4.11.B7L-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 - ?
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