Identification of NADH kinase activity in filamentous fungi and structural modelling of the novel enzyme from Fusarium oxysporum

Panagiotou, G; Papadakis, MA; Topakas, E; Olsson, L; Christakopoulos, P

dc.contributor.author	Panagiotou, G	en
dc.contributor.author	Papadakis, MA	en
dc.contributor.author	Topakas, E	en
dc.contributor.author	Olsson, L	en
dc.contributor.author	Christakopoulos, P	en
dc.date.accessioned	2014-03-01T01:28:39Z
dc.date.available	2014-03-01T01:28:39Z
dc.date.issued	2008	en
dc.identifier.issn	1359-5113	en
dc.identifier.uri	https://dspace.lib.ntua.gr/xmlui/handle/123456789/18895
dc.subject	Fungal NADH kinase	en
dc.subject	Fusarium oxysporum	en
dc.subject	Purification	en
dc.subject	Structural modelling	en
dc.subject.classification	Biochemistry & Molecular Biology	en
dc.subject.classification	Biotechnology & Applied Microbiology	en
dc.subject.classification	Engineering, Chemical	en
dc.subject.other	Enzymes	en
dc.subject.other	Food additives	en
dc.subject.other	Nucleic acids	en
dc.subject.other	Filamentous fungus	en
dc.subject.other	Fungal NADH kinase	en
dc.subject.other	Fusarium oxysporum	en
dc.subject.other	Kinase activities	en
dc.subject.other	Phosphotransferase	en
dc.subject.other	Purification	en
dc.subject.other	Structural modelling	en
dc.subject.other	Enzyme activity	en
dc.subject.other	Fungi	en
dc.subject.other	Fusarium oxysporum	en
dc.title	Identification of NADH kinase activity in filamentous fungi and structural modelling of the novel enzyme from Fusarium oxysporum	en
heal.type	journalArticle	en
heal.identifier.primary	10.1016/j.procbio.2008.06.011	en
heal.identifier.secondary	http://dx.doi.org/10.1016/j.procbio.2008.06.011	en
heal.language	English	en
heal.publicationDate	2008	en
heal.abstract	ATP-NADH kinase phosphorylates NADH to produce NADPH at the expense of ATP. The present study describes Fusarium oxysporum NADH kinase (ATP:NADH 2'-phosphotransferase, EC 2.7.1.86), a novel fungal enzyme capable of synthesizing NADPH using NADH as the preferred diphosphonicotinamide (diphosphopyridine) nucleotide donor. NADH kinase was highly purified (similar to 66-fold) and the enzyme was found to be a homodimeric with a subunit of M-r 72,000. Isoelectric focusing in the pH range of 3.0-9.5 of the purified NADH kinase yielded a pl value of about 5.6. The K-m values of NADH kinase for NADH and ATP were found to be 0.13 and 2.59 mM, respectively. Prediction of the secondary structure of the protein was performed in the PSIPRED server while modelling the three-dimensional (3D) structure was accomplished by the use of the HH 3D-structure prediction server. (C) 2008 Elsevier Ltd. All rights reserved.	en
heal.publisher	ELSEVIER SCI LTD	en
heal.journalName	Process Biochemistry	en
dc.identifier.doi	10.1016/j.procbio.2008.06.011	en
dc.identifier.isi	ISI:000259773100014	en
dc.identifier.volume	43	en
dc.identifier.issue	10	en
dc.identifier.spage	1114	en
dc.identifier.epage	1120	en