Action of Serine Carboxypeptidase from Aspergillus saitoi on Carboxyterminal Amidated Peptides(Biological Chemistry)

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概要

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• The specificity of the serine carboxypeptidase from Aspergillus saitoi (EC 3.4.16.1) was investigated on carboxyterminal amidated peptides such as benzyloxycarbonyl(Z)-Ala-Phe-NH_2, gastrin-related peptide, molluscan cardioexcitatory neuropeptide, eledoisin-related peptide, and (D-Ala^2,Met^5)-enkephalinamide. The enzyme did not hydrolyze Z-Ala-Phe-NH_2. It acted only as a carboxyamidase for the carboxyterminal peptide bond of gastrin-related peptide and as an amidase for enkephalinamide. The enzyme had both carboxyamidase activity and amidase activity for molluscan cardioexcitatory neuropeptide and eledoisin-related peptide. Whether the enzyme acts as an amidase or carboxyamidase, the hydrophobicity of P_3 and P_4 positions of the substrate may be important. After removal of the carboxyterminal amino acid amide and/or ammonia, the enzyme catalyzed the sequential liberation of the amino acid from the carboxyterminus of the substrate.

• 社団法人日本農芸化学会の論文
• 1989-09-23

著者

• ICHISHIMA Eiji

  Laboratory of molecular Enzymology, Department of Applied Biological Chemistry, Faculty of Agricultu

• Ichishima Eiji

  Laboratory Of Enzymology And Microbial Chemistry Tokyo University Of Agriculture And Technology

• TAKEUCHI Michio

  Laboratory Enzymology and Microbial Chemistry, Tokyo University of Agriculture and Technology

• Takeuchi Michio

  Laboratory Enzymology And Microbial Chemistry Tokyo University Of Agriculture And Technology

• Ichishima Eiji

  Laboratory Of Enzymology And Microbial Chemistry Tokyo Noko University

• TAKEUCHI Michio

  Laboratory of Enzymology and Microbial Chemistry, Tokyo University of Agriculture and Technology

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