The redox reactions of nicotinamide adenine dinucleotide.
The succinate dehydrogenase complex showing several cofactors, including flavin, iron–sulfur centers, and heme.
A man with pellagra, which is caused by a chronic lack of vitamin B3 in the diet
UV absorption spectra of NAD and NADH.
A simple [Fe2S2] cluster containing two iron atoms and two sulfur atoms, coordinated by four protein cysteine residues.
Niacin, serotonin (5-hydroxytryptamine), and melatonin biosynthesis from tryptophan
Some metabolic pathways that synthesize and consume NAD in vertebrates. The abbreviations are defined in the text.
The redox reactions of nicotinamide adenine dinucleotide.
Inositol hexanicotinate
Salvage pathways use three precursors for NAD+.
Space-filling model of niacin
Rossmann fold in part of the lactate dehydrogenase of Cryptosporidium parvum, showing NAD in red, beta sheets in yellow, and alpha helices in purple.
In this diagram, the hydride acceptor C4 carbon is shown at the top. When the nicotinamide ring lies in the plane of the page with the carboxy-amide to the right, as shown, the hydride donor lies either "above" or "below" the plane of the page. If "above" hydride transfer is class A, if "below" hydride transfer is class B.
A simplified outline of redox metabolism, showing how NAD and NADH link the citric acid cycle and oxidative phosphorylation.
The structure of cyclic ADP-ribose.
Arthur Harden, co-discoverer of NAD

Nicotinamide adenine dinucleotide (NAD) is a coenzyme central to metabolism.

- Nicotinamide adenine dinucleotide

The amide derivative nicotinamide (niacinamide) is a component of the coenzymes nicotinamide adenine dinucleotide (NAD) and nicotinamide adenine dinucleotide phosphate (NADP+).

- Niacin

In organisms, NAD can be synthesized from simple building-blocks (de novo) from either tryptophan or aspartic acid, each a case of an amino acid; alternatively, more complex components of the coenzymes are taken up from nutritive compounds such as niacin; similar compounds are produced by reactions that break down the structure of NAD, providing a salvage pathway that “recycles” them back into their respective active form.

- Nicotinamide adenine dinucleotide

For example, the multienzyme complex pyruvate dehydrogenase at the junction of glycolysis and the citric acid cycle requires five organic cofactors and one metal ion: loosely bound thiamine pyrophosphate (TPP), covalently bound lipoamide and flavin adenine dinucleotide (FAD), cosubstrates nicotinamide adenine dinucleotide (NAD+) and coenzyme A (CoA), and a metal ion (Mg2+).

- Cofactor (biochemistry)

Vitamins can serve as precursors to many organic cofactors (e.g., vitamins B1, B2, B6, B12, niacin, folic acid) or as coenzymes themselves (e.g., vitamin C).

- Cofactor (biochemistry)

Niacin and nicotinamide are both converted into the coenzyme NAD.

- Niacin
The redox reactions of nicotinamide adenine dinucleotide.

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