To install click the Add extension button. That's it.

The source code for the WIKI 2 extension is being checked by specialists of the Mozilla Foundation, Google, and Apple. You could also do it yourself at any point in time.

4,5
Kelly Slayton
Congratulations on this excellent venture… what a great idea!
Alexander Grigorievskiy
I use WIKI 2 every day and almost forgot how the original Wikipedia looks like.
Live Statistics
English Articles
Improved in 24 Hours
Added in 24 Hours
What we do. Every page goes through several hundred of perfecting techniques; in live mode. Quite the same Wikipedia. Just better.
.
Leo
Newton
Brights
Milds

NADPH dehydrogenase (quinone)

From Wikipedia, the free encyclopedia

In enzymology, a NADPH dehydrogenase (quinone) (EC 1.6.5.10) is an enzyme that catalyzes the chemical reaction

NADPH + H+ + acceptor NADP+ + reduced acceptor

The 3 substrates of this enzyme are NADPH, H+, and acceptor, whereas its two products are NADP+ and reduced acceptor.

This enzyme belongs to the family of oxidoreductases, specifically those acting on NADH or NADPH with other acceptors. The systematic name of this enzyme class is NADPH:(quinone-acceptor) oxidoreductase. Other names in common use include reduced nicotinamide adenine dinucleotide phosphate (quinone), dehydrogenase, NADPH oxidase, and NADPH2 dehydrogenase (quinone). It has 2 cofactors: FAD, and Flavoprotein. Several compounds are known to inhibit this enzyme, including Folate, and Dicumarol.

YouTube Encyclopedic

  • 1/3
    Views:
    70 617
    15 104
    23 366
  • Electron Transport Chain ETC Made Easy
  • Biological redox reactions of alcohols and phenols | Chemical Processes | MCAT | Khan Academy
  • Electron Transport Chain ETC Part 2

Transcription

Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1F5V.

See also

References

  • Koli AK, Yearby C, Scott W, Donaldson KO (1969). "Purification and properties of three separate menadione reductases from hog liver". J. Biol. Chem. 244 (4): 621–9. PMID 4388793.


This page was last edited on 26 August 2023, at 15:08
Basis of this page is in Wikipedia. Text is available under the CC BY-SA 3.0 Unported License. Non-text media are available under their specified licenses. Wikipedia® is a registered trademark of the Wikimedia Foundation, Inc. WIKI 2 is an independent company and has no affiliation with Wikimedia Foundation.