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

Glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+)

From Wikipedia, the free encyclopedia

In enzymology, a glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (EC 1.2.1.59) is an enzyme that catalyzes the chemical reaction

D-glyceraldehyde 3-phosphate + phosphate + NAD(P)+ 3-phospho-D-glyceroyl phosphate + NAD(P)H + H+

The 4 substrates of this enzyme are D-glyceraldehyde 3-phosphate, phosphate, NAD+, and NADP+, whereas its 4 products are 3-phospho-D-glyceroyl phosphate, NADH, NADPH, and H+.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-glyceraldehyde 3-phosphate:NAD(P)+ oxidoreductase (phosphorylating). Other names in common use include (phosphorylating), triosephosphate dehydrogenase (NAD(P)), and glyceraldehyde-3-phosphate dehydrogenase (NAD(P)) (phosphorylating).

YouTube Encyclopedic

  • 1/3
    Views:
    191 849
    679
    22 965
  • Pentose phosphate pathway - Cyclic structures and anomers | Biomolecules | MCAT | Khan Academy
  • Glyceraldehyde 3-phosphate PO4 PartII 28jun2010
  • #21 Biochemistry Glycolysis Lecture for Kevin Ahern's BB 450/550

Transcription

Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2CZC.

References

  • P. Mathis (Ed.), Photosynthesis: From Light to Biosphere, vol. 1, Kluwer Academic Publishers, 1995, p. 959-962.
  • Valverde F, Losada M, Serrano A (1997). "Functional complementation of an Escherichia coli gap mutant supports an amphibolic role for NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase of Synechocystis sp. strain PCC 6803". J. Bacteriol. 179 (14): 4513–22. doi:10.1128/jb.179.14.4513-4522.1997. PMC 179286. PMID 9226260.


This page was last edited on 26 August 2023, at 14:19
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.