NAD References

NAD accelerates several important reactions that are involved in energy production. It is one of the major electron carries in the oxidation of fuel molecules and is also an important cofactor in redox reactions. In glycolysis, the enzyme glyceraldehyde-3-phosphate dehydrogenase catalysis the conversion of glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate by the reduction of NAD to NADH. Lactate dehydrogenase ensure there's enough NAD for glycolysis by oxidizing NADH through the conversion of pyruvate to lactate. NAD is also the cofactor for alcohol dehydrogenase which detoxifies ethanol in the body. Electron transfer by NAD is essential for life.

References

1.) Energetics of Multistep versus One-step Hydride Transfer Reactions of Reduced Nicotinamide Adenine Dinucleotide (NADH) Models with Organic Cations and p-Quinones.

Cheng JP, Lu Y, Zhu X, Mu L.

Department of Chemistry, Nankai University, Tianjin 300071, China.

J Org Chem 1998 Sep 4;63(18):6108-6114

http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11672236&dopt=Abstract

2.) A Compact Chemical Miniature of a Holoenzyme, Coenzyme NADH Linked Dehydrogenase. Design and Synthesis of Bridged NADH Models and Their Highly Enantioselective Reduction1

Nobuhiro Kanomata* and Tadashi Nakata

J. Am. Chem. Soc., 122 (19), 4563 -4568, 2000.

http://pubs.acs.org/CHECKCCIP-1006825722/isubscribe/journals/jacsat/jtext.cgi?jacsat/122/19/html/ja992990y.html

3.) The Structure and Biochemistry of NADH-Dependent Cytochrome b5 Reductase Are Now Consistent

Maria C. Bewley,* Christopher C. Marohnic, and Michael J. Barber

Biology Department, Brookhaven National Laboratory, Upton, New York 11973, and Department of Biochemistry and Molecular Biology, College of Medicine, University of South Florida, and H. Lee Moffitt Cancer Center and Research Institute, Tampa, Florida 33612

Biochemistry, 40 (45), 13574 -13582, 2001.

http://pubs.acs.org/isubscribe/journals/bichaw/jtext.cgi?bichaw/40/45/html/bi0106336.html

4.) Characterization of the Overproduced NADH Dehydrogenase Fragment of the NADH:Ubiquinone Oxidoreductase (Complex I) from Escherichia coli

Matthias Braun, Stefanie Bungert, and Thorsten Friedrich

Institut für Biochemie, Heinrich-Heine-Universität, Universitätsstrasse 1, D-40225 Düsseldorf, Germany

Biochemistry, 37 (7), 1861 -1867, 1998.

http://pubs.acs.org/isubscribe/journals/alljournals/jtext.cgi?bichaw/37/7/abs/bi971176p.html

5.) Transient-State and Steady-State Kinetic Studies of the Mechanism of NADH-Dependent Aldehyde Reduction Catalyzed by Xylose Reductase from the Yeast Candida tenuis

Bernd Nidetzky, Mario Klimacek, and Peter Mayr

Division of Biochemical Engineering, Institute of Food Technology, Universität für Bodenkultur (BOKU), Muthgasse 18, A-1190 Vienna, Austria

Biochemistry, 40 (34), 10371 -10381, 2001.

http://pubs.acs.org/isubscribe/journals/bichaw/jtext.cgi?bichaw/40/34/html/bi010148a.html

6.) Caged NADP and NAD. Synthesis and Characterization of Functinally Distinct Caged Compounds.

Bruce E Cohen, Barry L. Stoddard, and Daniel E. Koshland Jr.

Department of Chemistry and Molecular and Cell Biology. University of California, Lawrence Berkeley Laboratory, Berkeley,CA.

Biochemistry, 36 (29), 9035-9044, 1997.

http://www.fhcrc.org/labs/stoddard/cohen_etal_biochem97.pdf

7. ) Purification and characterisation of two isoenzymes of DL-glycerol 3-phosphatase from Saccharomyces cerevisiae. Identification of the corresponding genes and evidence for osmotic regulation of one of the iso-forms by the osmosensing MAP kinase signal transduction pathway.

Norbeck, J., Påhlman, A-K., Akhtar, N., Blomberg, A. and Adler, L.

J. Biol. Chem. 271, 13875 - 13881. (1996)

8.) The two isoenzymes for yeast NAD dependent glycerol 3-phosphate dehydrogenase encoded by GPD1 and GPD2 have distinct roles in osmoadaptation and redox regulation.

Ansell, R., S. Hohmann, K. Granath, J. Thevelein, and L. Adler.

EMBO J. 16, 2179-2187. (1997)

9.) Stereospecific Oxidation of Secondary Alcohols by Human Alcohol Dehydrogenases.

Stone, C., Ting-Kai, L., and Bosron, W.

The Journal of Biological Chemistry. Vol. 264, No. 19. July 1989. pp.11112-1116.

http://www.jbc.org/cgi/reprint/264/19/11112.pdf

10.) Inhibition of lactate dehydrogenase activity by polymeric NAD derivatives with different NAD densities.

European Journal of Biochemistry, Vol 114, 101-104,1981.

Links to more information of NAD

http://www.ultranet.com/~jkimball/BiologyPages/N/NAD.html

http://alpha2.bmc.uu.se/hicup/NAD/

http://www.prosci.uci.edu/Articles/Vol8/issue9/PDF/1725.pdf