Properties of post-proline cleaving enzymes from <Emphasis Type="Italic">Tenebrio molitor</Emphasis> |
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| Authors: | I A Goptar I A Koulemzina I Yu Filippova E N Lysogorskaya E S Oksenoit D P Zhuzhikov Ya E Dunaevsky M A Belozersky E N Elpidina |
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| Institution: | (1) Faculty of Chemistry, Moscow State University, Vorob’evy gory, Moscow, 119991, Russia;(2) Faculty of Bioengineering and Bioinformatics, Moscow State University, Vorob’evy gory, Moscow, 119991, Russia;(3) Faculty of Biology, Moscow State University, Vorob’evy gory, Moscow, 119991, Russia;(4) Belozersky Institute of Physico-Chemical Biology, Moscow State University, Vorob’evy gory, Moscow, 119991, Russia |
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| Abstract: | Two post-proline cleaving peptidases PPCP1 and PPCP2 with molecular masses of 101 and 63 kDa, respectively, hydrolyzing Z-AlaAlaPro-pNA were isolated for the first time from the larval midgut of the yellow mealworm Tenebrio molitor and characterized. PPCP1 was active only in acidic media, with a maximum at pH 5.6, whereas PPCP2, both in acidic and alkaline media with a maximum at pH 7.9. Using inhibitory analysis, both PPCP1 and PPCP2 were shown to belong to serine peptidases. The data obtained indicate that a Cys residue is located close to the PPCP2 substrate binding site. Z-Pro-prolinal, a specific inhibitor of prolyl oligopeptidases, completely inhibited PPCP2 and partially PPCP1. The substrate specificities of the isolated enzymes were studied. Z-Ala-Ala-Pro-pNA was the best substrate for PPCP1, and Z-Ala-Pro-pNA, for PPCP2. The combination of the properties allows characterization of PPCP2 as a proplyl oligopeptidase. |
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| Keywords: | post-proline cleaving enzyme prolyl oligopeptidase yellow mealworm Tenebrio molitor |
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