Carboxyl Proteinase from the Wood Deteriorating Basidiomycete Pycnoporus coccineus: Substrate Specificity with Oxidized Insulin Peptide B1-B16 and B15-B24, Angiotensin and Proangiotensin
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概要
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The specificity of highly purified carboxyl proteinase from Pycnoporus coccineus (formerly designated Trametes sanguined) was investigated with oligopeptides at pH 2.7. Hydrolysis of oxidized insulin peptide B1-B16 was observed at two peptide bonds (His10-Leu11 and Ala14-Leu15) during 3-hr incubation. The enzyme did not hydrolyze oxidized insulin peptide B15-B24. Hydrolysis of angiotensin (formerly designated angiotensin II) was observed at the Tyr4-Ile5 bond. Hydrolysis of proangiotensin (formerly designated angiotensin I) was also at the Tyr4-Ile5 bond. In conclusion, peptide bonds which have a hydrophobic amino acid in the P1 position (as defined by Schechter and Berger, Biochem. Biophys. Res. Commun., 27, 157 (1967)) are preferentially cleaved by the trypsinogen activating carboxyl proteinase of Pycnoporus coccineus.
- 社団法人 日本農芸化学会の論文
著者
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Majima Eiji
Laboratory Of Enzymology And Microbial Chemistry Tokyo University
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Ichishima Eiji
Laboratory Of Enzymology And Microbial Chemistry Tokyo Noko University
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MATSUE Masashi
Laboratory of Enzymology and Microbial Chemistry, Tokyo Noko University
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MAJIMA Eiji
Laboratory of Enzymology and Microbial Chemistry, Tokyo Noko University
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KUMAGAI Hiroyuki
Laboratory of Enzymology and Microbial Chemistry, Tokyo Noko University
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TOMODA Katsumi
Research Laboratories of Fermentation Products, Takeda Chemical Industries
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