{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,7]],"date-time":"2025-11-07T12:55:29Z","timestamp":1762520129167,"version":"3.40.4"},"reference-count":60,"publisher":"Cambridge University Press (CUP)","issue":"9","license":[{"start":{"date-parts":[[2017,5,9]],"date-time":"2017-05-09T00:00:00Z","timestamp":1494288000000},"content-version":"unspecified","delay-in-days":0,"URL":"https:\/\/www.cambridge.org\/core\/terms"}],"content-domain":{"domain":["www.cambridge.org"],"crossmark-restriction":true},"short-container-title":["Parasitology"],"published-print":{"date-parts":[[2017,8]]},"abstract":"<jats:title>SUMMARY<\/jats:title><jats:p>Phosphoenolpyruvate carboxykinase (PEPCK) is involved in glycolysis in the cestode parasite, <jats:italic>Raillietina echinobothrida<\/jats:italic>; whereas, it executes a gluconeogenic role in its host, <jats:italic>Gallus domesticus<\/jats:italic>. Because of its differing primary function in the cestode parasite and its host, this enzyme is regarded as a plausible anthelmintic target. Hence, the biological significance of PEPCK in the parasite was analysed using siRNA against PEPCK from <jats:italic>R. echinobothrida<\/jats:italic> (RePEPCK). In order to find out the functional differences between RePEPCK and GdPEPCK (PEPCK from its host, <jats:italic>G. domesticus<\/jats:italic>), PEPCK genes from both sources were cloned, over-expressed, characterized, and some properties of the purified enzymes were compared. RePEPCK and GdPEPCK showed a standard Michaelis-Menten kinetics with <jats:italic>K<\/jats:italic><jats:sub>mapp<\/jats:sub> of 46.9 and 22.9 <jats:italic>\u00b5<\/jats:italic><jats:sc>m<\/jats:sc>, respectively, for phosphoenolpyruvate and <jats:italic>K<\/jats:italic><jats:sub>mapp<\/jats:sub> of 15.4 <jats:italic>\u00b5<\/jats:italic><jats:sc>m<\/jats:sc> for oxaloacetate in GdPEPCK decarboxylation reaction. Here, we report antagonist behaviours of recombinant PEPCKs derived from the parasite and its host. In search of possible modulators for PEPCK, few phytoestrogens were examined on the purified enzymes and their inhibitory constants were determined and discussed. This study stresses the potential of these findings to validate PEPCK as the anthelmintic drug target for parasitism management.<\/jats:p>","DOI":"10.1017\/s0031182017000518","type":"journal-article","created":{"date-parts":[[2017,5,9]],"date-time":"2017-05-09T10:01:11Z","timestamp":1494324071000},"page":"1264-1274","update-policy":"https:\/\/doi.org\/10.1017\/policypage","source":"Crossref","is-referenced-by-count":4,"title":["Biological significance of phosphoenolpyruvate carboxykinase in a cestode parasite, <i>Raillietina echinobothrida<\/i> and effect of phytoestrogens on the enzyme from the parasite and its host, <i>Gallus domesticus<\/i>"],"prefix":"10.1017","volume":"144","author":[{"family":"RAMNATH","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"ASIM KUMAR","family":"DUTTA","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"BARILIN","family":"DKHAR","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"VEENA","family":"TANDON","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"BIDYADHAR","family":"DAS","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"56","published-online":{"date-parts":[[2017,5,9]]},"reference":[{"key":"S0031182017000518_ref59","doi-asserted-by":"publisher","DOI":"10.1016\/0020-7519(82)90012-1"},{"key":"S0031182017000518_ref58","doi-asserted-by":"publisher","DOI":"10.2307\/3280707"},{"key":"S0031182017000518_ref57","doi-asserted-by":"publisher","DOI":"10.1021\/ja01099a522"},{"key":"S0031182017000518_ref56","doi-asserted-by":"publisher","DOI":"10.1007\/s004360050286"},{"key":"S0031182017000518_ref55","doi-asserted-by":"publisher","DOI":"10.1016\/j.ymeth.2007.01.005"},{"key":"S0031182017000518_ref52","doi-asserted-by":"publisher","DOI":"10.1186\/2049-9957-2-5"},{"key":"S0031182017000518_ref51","doi-asserted-by":"publisher","DOI":"10.1002\/jcb.25543"},{"key":"S0031182017000518_ref49","doi-asserted-by":"publisher","DOI":"10.1016\/0010-406X(69)91296-1"},{"key":"S0031182017000518_ref48","doi-asserted-by":"crossref","first-page":"13049","DOI":"10.1016\/S0021-9258(18)69269-5","article-title":"Purification and characterization of phosphoenolpyruvate carboxykinase from the parasitic helminth Ascaris suum","volume":"261","author":"Rohrer","year":"1986","journal-title":"Journal of Biological Chemistry"},{"key":"S0031182017000518_ref46","first-page":"343","volume-title":"Biology of the Eucestoda, Vol II","author":"Roberts","year":"1983"},{"key":"S0031182017000518_ref44","doi-asserted-by":"publisher","DOI":"10.1016\/0304-4165(68)90161-X"},{"key":"S0031182017000518_ref42","doi-asserted-by":"publisher","DOI":"10.1016\/j.ijpara.2009.10.012"},{"key":"S0031182017000518_ref39","doi-asserted-by":"crossref","first-page":"2259","DOI":"10.1016\/S0021-9258(19)67962-7","article-title":"Mammalian liver phospoenolpyruvate carboxykinase activities","volume":"238","author":"Nordlie","year":"1963","journal-title":"Journal of Biological Chemistry"},{"key":"S0031182017000518_ref38","doi-asserted-by":"crossref","first-page":"9099","DOI":"10.1016\/S0021-9258(19)40698-4","article-title":"Decarboxylation of oxalacetate to pyruvate by purified avian liver phosphoenolpyruvate carboxykinase","volume":"250","author":"Noce","year":"1975","journal-title":"Journal of Biological Chemistry"},{"key":"S0031182017000518_ref36","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.00578-06"},{"key":"S0031182017000518_ref34","doi-asserted-by":"publisher","DOI":"10.1016\/0006-291X(79)91890-4"},{"key":"S0031182017000518_ref60","doi-asserted-by":"publisher","DOI":"10.1016\/j.molbiopara.2004.08.003"},{"key":"S0031182017000518_ref1","doi-asserted-by":"publisher","DOI":"10.1016\/S0166-6851(03)00092-6"},{"key":"S0031182017000518_ref23","doi-asserted-by":"publisher","DOI":"10.1016\/j.pep.2015.09.004"},{"key":"S0031182017000518_ref7","doi-asserted-by":"publisher","DOI":"10.1016\/0020-7519(75)90031-4"},{"key":"S0031182017000518_ref12","doi-asserted-by":"publisher","DOI":"10.1002\/dmrr.780"},{"key":"S0031182017000518_ref45","doi-asserted-by":"publisher","DOI":"10.1016\/0305-0491(80)90300-4"},{"key":"S0031182017000518_ref43","doi-asserted-by":"publisher","DOI":"10.1016\/0020-7519(76)90039-4"},{"key":"S0031182017000518_ref27","doi-asserted-by":"crossref","first-page":"5515","DOI":"10.1016\/S0021-9258(19)83807-3","article-title":"Phosphoenolpyruvate carboxykinase. 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