Asset Details
Do you wish to reserve the book?
A genetically encoded tool for manipulation of NADP+/NADPH in living cells
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?
A genetically encoded tool for manipulation of NADP+/NADPH in living cells
Do you wish to request the book?
A genetically encoded tool for manipulation of NADP+/NADPH in living cells
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
A genetically encoded tool for manipulation of NADP+/NADPH in living cells
2017
Overview
Structure-guided engineering of an NADH oxidase switches its cofactor preference, thus yielding an NADPH oxidase that can be used to tune the cellular NADP
+
/NADPH ratio and to examine the links between mitochondrial NADH and NADPH pools.
The redox coenzymes NADH and NADPH are broadly required for energy metabolism, biosynthesis and detoxification. Despite detailed knowledge of specific enzymes and pathways that utilize these coenzymes, a holistic understanding of the regulation and compartmentalization of NADH- and NADPH-dependent pathways is lacking, partly because of a lack of tools with which to investigate these processes in living cells. We have previously reported the use of the naturally occurring
Lactobacillus brevis
H
2
O-forming NADH oxidase (
Lb
NOX) as a genetic tool for manipulation of the NAD
+
/NADH ratio in human cells. Here, we present triphosphopyridine nucleotide oxidase (TPNOX), a rationally designed and engineered mutant of
Lb
NOX that is strictly specific to NADPH. We characterized the effects of TPNOX expression on cellular metabolism and used it in combination with
Lb
NOX to show how the redox states of mitochondrial NADPH and NADH pools are connected.
Publisher
Nature Publishing Group US,Nature Publishing Group
Subject
