Specificity of Proteinase K from Tritirachium album Limber for Synthetic Peptides |
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Authors: | Kazuyuki Morihara Hiroshige Tsuzuki |
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Institution: | 1. Shionogi Research Laboratory, Shionogi &2. Co., Ltd., Fukushima-ku, Osaka 553 |
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Abstract: | The specificity of proteinase K from Tritirachium album Limber was determined using various synthetic peptide substrates. The esterase activity against N-acylated amino acid esters indicated that the enzyme is primarily specific against aromatic or hydrophobic amino acid residues at the carboxyl side of the splitting point. Secondary interaction for hydrolysis was also studied using peptide esters or others, which showed that the enzyme activity is markedly promoted by elongating the peptide chain to the N-terminal from the splitting point. Thus, peptide chloromethyl ketone derivatives such as Cbz-Ala-Gly-PheCH2Cl inactivated the enzyme activity markedly. |
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Keywords: | olive oil adrenal corticosterone water-immersion restraint glycogen synthesis serine dehydratase |
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