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Biochemical and in silico Characterization of Recombinant L-Lactate Dehydrogenase of Theileria annulata

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dc.contributor.authorMUTLU, ÖZAL
dc.contributor.authorsNural, Belma; Erdemir, Aysegul; Mutlu, Ozal; Yakarsonmez, Sinem; Danis, Ozkan; Topuzogullari, Murat; Turgut-Balik, Dilek
dc.date.accessioned2022-03-12T20:28:58Z
dc.date.available2022-03-12T20:28:58Z
dc.date.issued2016
dc.description.abstractTheileria annulata is a parasite that causes theileriosis in cattle. Reports about drug resistance made essential to develop new drug. LDH of Theileria schizonts is the vital enzyme for its anaerobic metabolism. TaLDH gene was first cloned into pGEM-T cloning vector with two introns in our previous study. Here we report cloning of TaLDH without introns into pLATE 31 vector in E. coli BL21(DE3). Protein was in an inactive form. Two mutations were fixed to express the active protein. Protein was purified by affinity chromatography and evaluated by SDS-PAGE and size exclusion chromatography. Optimum pH of enzyme was performed in pH 7.5, and enzyme was stabilized at 20-40 A degrees C. Enzyme kinetics of recombinant TaLDH were found to be in the direction of pyruvate to lactate K (m) 0.1324 and K (i) 4.295 mM, k (cat) , 44.55/s and k (cat) /K (m) , 3.3693 x 10(5)/M/s. 3D structure of TaLDH was predicted, and possible drug binding sites were determined by homology modelling.
dc.identifier.doi10.1007/s12033-016-9924-3
dc.identifier.eissn1559-0305
dc.identifier.issn1073-6085
dc.identifier.pubmed26921192
dc.identifier.urihttps://hdl.handle.net/11424/234003
dc.identifier.wosWOS:000372925200005
dc.language.isoeng
dc.publisherHUMANA PRESS INC
dc.relation.ispartofMOLECULAR BIOTECHNOLOGY
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectLDH
dc.subjectTheileria annulata
dc.subjectThermostability
dc.subjectSubstrate inhibition
dc.subjectHomology modelling
dc.subjectPLASMODIUM-FALCIPARUM
dc.subjectTOXOPLASMA-GONDII
dc.subjectSUBSTRATE-INHIBITION
dc.subjectKINETIC-PROPERTIES
dc.subjectBINDING DOMAINS
dc.subjectDESIGN
dc.subjectBUPARVAQUONE
dc.subjectPARASITES
dc.subjectGENE
dc.subjectANTIMALARIALS
dc.titleBiochemical and in silico Characterization of Recombinant L-Lactate Dehydrogenase of Theileria annulata
dc.typearticle
dspace.entity.typePublication
local.avesis.idaf941763-47db-4cd7-8c97-9392feac7d7a
local.import.packageSS17
local.indexed.atWOS
local.indexed.atSCOPUS
local.indexed.atPUBMED
local.journal.numberofpages12
local.journal.quartileQ3
oaire.citation.endPage267
oaire.citation.issue4
oaire.citation.startPage256
oaire.citation.titleMOLECULAR BIOTECHNOLOGY
oaire.citation.volume58
relation.isAuthorOfPublication7a1f8128-8f83-44b5-8eb0-9bc61e75943d
relation.isAuthorOfPublication.latestForDiscovery7a1f8128-8f83-44b5-8eb0-9bc61e75943d

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