Prolyl endopeptidases from the midgut of the yellow mealworm Tenebrio molitorстатьяТезисы
Информация о цитировании статьи получена из
Web of Science
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Дата последнего поиска статьи во внешних источниках: 27 мая 2015 г.
Аннотация:Prolyl endopeptidases or post-proline cleaving enzymes are specific
endopeptidases hydrolyzing peptide bond on the carboxyl
Abstracts
154
side of proline residues. These enzymes were found in mammals,
several higher plants, fungi and bacteria. It is suggested
that the enzymes participate in the in vivo regulation of the
action of biologically active peptides. We for the first time
report about two prolyl endopeptidases in the larval midgut of
a stored product pest yellow mealworm Tenebrio molitor where
they can participate in the proteolysis of one of the main dietary
proteins of T. molitor larvae – rich in proline prolamines.
Characteristics of two prolyl endopeptidases are significantly different.
Optimum for hydrolysis of the substrate Z-Ala-Ala-PropNA
(N-Carbobenzoxy-l-alanyl-l-alanyl-l-prolyl-p-nitroanilide)
by prolyl endopeptidase 1 was at pH 8.5, and prolyl endopeptidase
2 – at pH 5.6. Prolyl endopeptidase 1 displayed high pHstability
in the pH range 7.0–10.0 and the rate of hydrolysis
increased in the presence of KCl and CaCl2. Prolyl endopeptidase
2 demonstrated low stability in the whole pH range, the
rate of hydrolysis strongly decreased in the presence of above
mentioned salts, but increased in the presence of high concentrations
of EDTA.