{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2022,4,3]],"date-time":"2022-04-03T22:12:58Z","timestamp":1649023978737},"reference-count":41,"publisher":"Cambridge University Press (CUP)","issue":"10","license":[{"start":{"date-parts":[[2014,5,20]],"date-time":"2014-05-20T00:00:00Z","timestamp":1400544000000},"content-version":"unspecified","delay-in-days":0,"URL":"https:\/\/www.cambridge.org\/core\/terms"}],"content-domain":{"domain":["journals.cambridge.org"],"crossmark-restriction":true},"short-container-title":["Parasitology"],"published-print":{"date-parts":[[2014,9]]},"abstract":"<jats:title>SUMMARY<\/jats:title><jats:p>Guanylate kinase, a nucleoside monophosphate kinase of<jats:italic>Brugia malayi<\/jats:italic>which is involved in reversible transfer of phosphate groups from ATP to GMP, was cloned, expressed and characterized. The native molecular mass of BmGK was found to be 45\u00a0kDa as determined by size exclusion chromatography and glutaraldehyde cross-linking which revealed that the protein is homodimer in nature. This is a unique characteristic among known eukaryotic GKs. GMP and ATP served as the most effective phosphate acceptor and donor, respectively. Recombinant BmGK utilized both GMP and dGMP, as substrates showing K<jats:sub>m<\/jats:sub>values of 30 and 38\u00a0<jats:italic>\u03bc<\/jats:italic><jats:sc>m<\/jats:sc>, respectively. Free Mg<jats:sup>+2<\/jats:sup>(un-complexed to ATP) and GTP play a regulatory role in catalysis of BmGK. The enzyme showed higher catalytic efficiency as compared with human GK and showed ternary complex (BmGK-GMP-ATP) formation with sequential substrate binding. The secondary structure of BmGK consisted of 45%<jats:italic>\u03b1<\/jats:italic>-helices, 18%<jats:italic>\u03b2<\/jats:italic>-sheets as revealed by CD analysis. Homology modelling and docking with GMP revealed conserved substrate binding residues with slight differences. Differences in kinetic properties and oligomerization of BmGK compared with human GK can provide the way for design of parasite-specific inhibitors.<\/jats:p>","DOI":"10.1017\/s0031182014000675","type":"journal-article","created":{"date-parts":[[2014,5,20]],"date-time":"2014-05-20T14:47:41Z","timestamp":1400597261000},"page":"1341-1352","update-policy":"http:\/\/dx.doi.org\/10.1017\/policypage","source":"Crossref","is-referenced-by-count":3,"title":["Purification and characterization of guanylate kinase, a nucleoside monophosphate kinase of<i>Brugia malayi<\/i>"],"prefix":"10.1017","volume":"141","author":[{"given":"SMITA","family":"GUPTA","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"SUNITA","family":"YADAV","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"NIDHI","family":"SINGH","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"ANITA","family":"VERMA","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"IMRAN","family":"SIDDIQI","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"JITENDRA K.","family":"SAXENA","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"56","published-online":{"date-parts":[[2014,5,20]]},"reference":[{"key":"S0031182014000675_ref32","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M204668200"},{"key":"S0031182014000675_ref31","volume-title":"Molecular Cloning: A Laboratory Manual","author":"Sambrook","year":"1989"},{"key":"S0031182014000675_ref28","doi-asserted-by":"crossref","first-page":"5452","DOI":"10.1016\/S0021-9258(18)96451-3","article-title":"Purification and properties of guanylate kinase from Escherichia coli","volume":"241","author":"Oeschger","year":"1966","journal-title":"Journal of Biological Chemistry"},{"key":"S0031182014000675_ref27","doi-asserted-by":"crossref","first-page":"7204","DOI":"10.1016\/S0021-9258(20)79686-9","article-title":"Phosphorylation of acyclovir (acycloguanosine) monophosphate by GMP kinase","volume":"255","author":"Miller","year":"1980","journal-title":"Journal of Biological Chemistry"},{"key":"S0031182014000675_ref24","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.271.45.28038"},{"key":"S0031182014000675_ref22","doi-asserted-by":"publisher","DOI":"10.1046\/j.1432-1327.2000.01045.x"},{"key":"S0031182014000675_ref20","doi-asserted-by":"publisher","DOI":"10.1016\/j.molbiopara.2008.02.004"},{"key":"S0031182014000675_ref19","doi-asserted-by":"publisher","DOI":"10.1002\/jmr.1074"},{"key":"S0031182014000675_ref18","doi-asserted-by":"publisher","DOI":"10.1021\/jm020406h"},{"key":"S0031182014000675_ref16","doi-asserted-by":"publisher","DOI":"10.1002\/prot.20662"},{"key":"S0031182014000675_ref12","doi-asserted-by":"publisher","DOI":"10.1038\/nrd1416"},{"key":"S0031182014000675_ref11","first-page":"22","article-title":"Characterization of guanylate kinase from gram positive and gram negative microorganisms; preliminary results","volume":"66","author":"Eftimie","year":"2007","journal-title":"Roumanian Archives of Microbiology and Immunology"},{"key":"S0031182014000675_ref10","volume-title":"First WHO Report on Neglected Tropical Diseases: Working to Overcome the Global Impact of Neglected Tropical Diseases","author":"Crompton","year":"2010"},{"key":"S0031182014000675_ref9","doi-asserted-by":"publisher","DOI":"10.1124\/jpet.104.078311"},{"key":"S0031182014000675_ref8","doi-asserted-by":"publisher","DOI":"10.1016\/0003-9861(69)90337-3"},{"key":"S0031182014000675_ref7","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.271.28.16734"},{"key":"S0031182014000675_ref6","doi-asserted-by":"publisher","DOI":"10.1016\/0003-2697(76)90527-3"},{"key":"S0031182014000675_ref5","doi-asserted-by":"publisher","DOI":"10.1097\/QCO.0b013e32833fdee5"},{"key":"S0031182014000675_ref4","volume-title":"Biochemistry","author":"Berg","year":"2002"},{"key":"S0031182014000675_ref2","doi-asserted-by":"publisher","DOI":"10.1093\/protein\/6.4.383"},{"key":"S0031182014000675_ref1","doi-asserted-by":"publisher","DOI":"10.1016\/S0076-6879(78)51066-5"},{"key":"S0031182014000675_ref21","doi-asserted-by":"crossref","first-page":"25652","DOI":"10.1016\/S0021-9258(18)35654-0","article-title":"Cloning and expression of the essential gene for guanylate kinase from yeast","volume":"267","author":"Konrad","year":"1992","journal-title":"Journal of Biological Chemistry"},{"key":"S0031182014000675_ref23","doi-asserted-by":"publisher","DOI":"10.1038\/227680a0"},{"key":"S0031182014000675_ref38","doi-asserted-by":"publisher","DOI":"10.1038\/sj.gt.3302794"},{"key":"S0031182014000675_ref15","doi-asserted-by":"publisher","DOI":"10.1016\/j.jmb.2005.07.042"},{"key":"S0031182014000675_ref40","first-page":"103","article-title":"Nucleoside monophosphate kinases: structure, mechanism, and substrate specificity","volume":"73","author":"Yan","year":"1999","journal-title":"Advanced Enzymology Related Areas Molecular Biology"},{"key":"S0031182014000675_ref3","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbrc.2009.07.089"},{"key":"S0031182014000675_ref13","doi-asserted-by":"crossref","first-page":"14316","DOI":"10.1016\/S0021-9258(19)85243-2","article-title":"Guanylate kinase of Escherichia coli K-12","volume":"268","author":"Gentry","year":"1993","journal-title":"Journal of Biological Chemistry"},{"key":"S0031182014000675_ref34","doi-asserted-by":"publisher","DOI":"10.1016\/j.parint.2008.03.004"},{"key":"S0031182014000675_ref17","doi-asserted-by":"publisher","DOI":"10.1016\/j.biochi.2006.04.002"},{"key":"S0031182014000675_ref30","doi-asserted-by":"publisher","DOI":"10.1006\/jmbi.1993.1626"},{"key":"S0031182014000675_ref37","doi-asserted-by":"publisher","DOI":"10.1016\/S0969-2126(01)00181-2"},{"key":"S0031182014000675_ref41","doi-asserted-by":"publisher","DOI":"10.1016\/0167-4838(93)90112-5"},{"key":"S0031182014000675_ref35","doi-asserted-by":"publisher","DOI":"10.1200\/JCO.1989.7.4.499"},{"key":"S0031182014000675_ref36","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M803658200"},{"key":"S0031182014000675_ref29","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.270.27.16464"},{"key":"S0031182014000675_ref33","doi-asserted-by":"publisher","DOI":"10.1111\/j.1432-1033.1971.tb01312.x"},{"key":"S0031182014000675_ref25","doi-asserted-by":"publisher","DOI":"10.1016\/j.molbiopara.2009.06.010"},{"key":"S0031182014000675_ref26","doi-asserted-by":"publisher","DOI":"10.1021\/bi0340043"},{"key":"S0031182014000675_ref14","doi-asserted-by":"publisher","DOI":"10.1021\/bi981087s"},{"key":"S0031182014000675_ref39","volume-title":"Progress Report 2000\u20132009 and Strategic Plan 2010\u20132020 of the Global Programme to Eliminate Lymphatic Filariasis: Halfway Towards Eliminating Lymphatic Filariasis","year":"2010"}],"container-title":["Parasitology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.cambridge.org\/core\/services\/aop-cambridge-core\/content\/view\/S0031182014000675","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,4,3]],"date-time":"2022-04-03T21:29:01Z","timestamp":1649021341000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.cambridge.org\/core\/product\/identifier\/S0031182014000675\/type\/journal_article"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2014,5,20]]},"references-count":41,"journal-issue":{"issue":"10","published-print":{"date-parts":[[2014,9]]}},"alternative-id":["S0031182014000675"],"URL":"https:\/\/doi.org\/10.1017\/s0031182014000675","relation":{},"ISSN":["0031-1820","1469-8161"],"issn-type":[{"value":"0031-1820","type":"print"},{"value":"1469-8161","type":"electronic"}],"subject":[],"published":{"date-parts":[[2014,5,20]]},"assertion":[{"value":"Copyright \u00a9 Cambridge University Press 2014\u00a0","name":"license","label":"License","group":{"name":"copyright_and_licensing","label":"Copyright and Licensing"}}]}}