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

Paper ID Volume ID Publish Year Pages File Format Full-Text
35463 45091 2008 7 PDF Available
Title
Identification of NADH kinase activity in filamentous fungi and structural modelling of the novel enzyme from Fusarium oxysporum
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 (∼66-fold) and the enzyme was found to be a homodimeric with a subunit of Mr 72,000. Isoelectric focusing in the pH range of 3.0–9.5 of the purified NADH kinase yielded a pI value of about 5.6. The Km 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.

Keywords
Fungal NADH kinase; Fusarium oxysporum; Purification; Structural modelling
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Identification of NADH kinase activity in filamentous fungi and structural modelling of the novel enzyme from Fusarium oxysporum
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 43, Issue 10, October 2008, Pages 1114–1120
Authors
, , , , ,
Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us