BEHAVIOR OF TRYPSIN AND RELATED ENZYMES TOWARD AMIDINOPHENYL ESTERS

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概要

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• Kinetics of the hydrolysis of amidinophenyl esters catalyzed by urokinase, kallikrein, plasmin and trypsins from various origins were studied. p-Amidinophenyl esters in which the arrangement of the specific group for bovine trypsin (charged amidinium) is reversed to that of normal substrates were characterized as specific substrates for the enzyme and named"inverse substrates" (K. Tanizawa, Y. Kasaba and Y. Kanaoka, J. Am. Chem. Soc., 99,4485-4488). Behavior of these enzymes toward amidinophenyl esters was demonstrated to be very similar to that of bovine trypsin. These observations account for the structural similarity of their active sites. p-Amidinophenyl esters were found to be hydrolyzed also by clostripain which is known as a thiol protease with trypsin-like specificity. This is the first example of the "inverse substrates" for a thiol enzyme.

• 公益社団法人日本薬学会の論文

著者

• Kanaoka Yuichi

  Faculty Of Pharmaceutical Sciences Hokkaido University

• TANIZAWA Kazutaka

  Faculty of Pharmaceutical Sciences, Health Sciences University of Hokkaido

• NOZAWA MASAYUKI

  Faculty of Pharmaceutical Sciences, Hokkaido University

• MORIYA HIROSHI

  Faculty of Pharmaceutical Sciences, Science University of Tokyo

• Moriya Hiroshi

  Faculty Of Pharmaceutical Sciences Science University Of Tokyo

• KANAOKA Yuichi

  Faculty of Pharmaceutical Sciences, Hokkaido University

関連論文

• Trypsin-Catalyzed Synthesis of Dipeptide Containing α-Aminoisobutylic Acid Using p- and m-(Amidinomethyl)phenyl Esters as Acyl Donor
• A Facile Synthesis of p- and m-(Amidinomethyl)phenyl Esters Derived from Amino Acid and Tryptic Hydrolysis of These Synthetic Inverse Substrates
• Kinetic Properties of Three Isoforms of Trypsin Isolated from the Pyloric Caeca of Chum Salmon (Oncorhynchus keta)(Analytical Biochemistry)
• Amidino-Containing Schiff Base Copper(II) and Iron(III) Chelates as a Thrombin Inhibitor
• Synthesis and Evaluation of Guanidine-Containing Schiff Base Copper(II), Zinc(II), and Iron(III) Chelates as Trypsin Inhibitors
• Application of Various Inverse Substrates to Thrombin-Catalyzed Peptide Synthesis
• Application of Schiff Base Copper(II) and Iron(III) Chelates to Site-Specific Cleavage of a Trypsin
• The Structural Requirements for an Inverse Substrate for Enzymatic Peptide Synthesis : Position Isomers of Guanidinonaphthyl Esters as the Acyl Donor Component
• Enzymatic Peptide Synthesis with p-Guanidinophenyl and p-(Guanidinomethyl)phenyl Esters as Acyl Donors
• Tripsin-Catalyzed Peptide Synthesis with Various p-Guanidinophenyl Esters as Acyl Donors
• Synthesis and Triptic Hydrolysis of p-Guanidinophenyl Esters Derived from Amino Acids and Peptides
• Application of Spontaneous Schiff Base Copper Chelates Formation Process to the Design of a Trypsin Inhibitor
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• Heterocycles Related to Nucleotides. XI. An Organomercurial Column Chromatography for Thiouridine
• Heterocycles Related to Nucleotides. X. Reaction of Thiouridine with 2-Chloromercurio-4-nitrophenol
• Comparative Studies on the Structure of Active Sites--Behavior of "Inverse Substrates" toward Trypsin and Related Enzymes
• BEHAVIOR OF TRYPSIN AND RELATED ENZYMES TOWARD AMIDINOPHENYL ESTERS
• NEW CHROMOGENIC AND FLUOROGENIC SUBSTRATES FOR THE DETERMINATION OF BUTYRYLCHOLINESTERASE AND ARYLESTERASE ACTIVITIES
• "INVERSE SUBSTRATES" FOR TRYPSIN-LIKE ENZYMES
• Fluorogenic Bimane Substrates with Dabsyl Group for Endopeptidases : Chymotrypsin, Collagenase and Thermolysin

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