Asset Details
Do you wish to reserve the book?
NADPH regulates human NAD kinase, a NADP.sup.+-biosynthetic enzyme
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
NADPH regulates human NAD kinase, a NADP.sup.+-biosynthetic enzyme
Do you wish to request the book?
NADPH regulates human NAD kinase, a NADP.sup.+-biosynthetic enzyme
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
NADPH regulates human NAD kinase, a NADP.sup.+-biosynthetic enzyme
2011
Overview
NAD kinase (NADK, EC 2.7.1.23) is the sole [NADP.sup.+]-biosynthetic enzyme that catalyzes phosphorylation of [NAD.sup.+] to yield [NADP.sup.+] using ATP as a phosphoryl donor, and thus, plays a vital role in the cell and represents a potentially powerful antimicrobial drug target. Although methods for expression and purification of human NADK have been previously established (Lerner et al. Biochem Biophys Res Commun 288:69-74, 2001), the purification procedure could be significantly improved. In this study, we improved the method for expression and purification of human NADK in Escherichia coli and obtained a purified homogeneous enzyme only through heat treatment and single column chromatography. Using the purified human NADK, we revealed a sigmoidal kinetic behavior toward ATP and the inhibitory effects of NADPH and NADH, but not of [NADP.sup.+], on the catalytic activity of the enzyme. These inhibitory effects provide insight into the regulation of intracellular NADPH synthesis. Furthermore, these attributes may provide a clue to design a novel drug against Mycobacterium tuberculosis in which this bacterial NADK is potently inhibited by [NADP.sup.+]. Keywords NAD kinase * Human * Drug design * [NADP.sup.+] NADPH NADH
Publisher
Springer
Subject
