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Properties and substrate specificities of proteolytic enzymes from the edible basidiomycete Grifola frondosa(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)
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Nishiwaki Toshikazu
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Asano Satoshi
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Ohyama Takuji
… The ProGF also liberated hydrophobic amino acids, such as valine, leucine, and phenylalanine, using the oxidized insulin B-chain as a substrate. … These results indicate that the ProGF include both endopeptidases recognizing leucine, phenylalanine, and lysine at the P1' position, and aminopeptidases preferentially releasing hydrophobic and aromatic amino acids such as valine, leucine, phenylalanine, and tyrosine. …
Journal of bioscience and bioengineering 107(6), 605-609, 2009-06-00
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