[Properties of post-proline cleaving enzymes from Tenebrio molitor].
Two post-proline cleaving enzymes PRE1 and PRE2 with molecular masses of 101 and 62 kDa, respectively, capable of hydrolyzing Z-AlaAlaPro-pNA were isolated for the first time from the midgut of the flour beetle Tenebrio molitor and characterized. PRE1 is active only in acidic media, with a maximum at pH 5.6, whereas PRE2, both in acidic and alkaline media with a maximum at pH 7.9. Using inhibitory analysis, both PRE1 and PRE2 were shown to belong to serine peptidases. Some data indicate that a Cys residue is located close to the PRE2 active site. Z-Pro-prolinal, a specific inhibitor of prolyl oligopeptidases, inhibits completely PRE2 and partially PRE1. The substrate specificities of the isolated enzymes were studied. It was shown that Z-AlaAla-Pro-pNA was the best substrate for PRE1, and Z-AlaPro-pNA, for PRE2. The combination of the studied properties allowed characterization of PRE2 as a prolyl oligopeptidase.
Goptar'
I A
IA
Kulemzina
I A
IA
Filippova
I Iu
IIu
Lysogorskaia
E N
EN
Oksenoĭt
E S
ES
Zhuzhikov
D P
DP
Dunaevskiĭ
Ia E
IaE
Belozerskiĭ
M A
MA
Elpidina
E N
EN
D000814:Aniline Compounds / Q000737:chemistry; D000818:Animals; D002850:Chromatography, Gel; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007814:Larva / Q000201:enzymology; D000085822:Prolyl Oligopeptidases; D012697:Serine Endopeptidases / Q000737:chemistry* / Q000302:isolation & purification; D013379:Substrate Specificity; D013712:Tenebrio / Q000201:enzymology*
D000814:Aniline Compounds; D012697:Serine Endopeptidases; D000085822:Prolyl Oligopeptidases