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A5251

Sigma-Aldrich

3-Acetylpyridine adenine dinucleotide

≥85%

Synonyme(s) :

3 -Acetyl NAD, APADH, APAD

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About This Item

Formule empirique (notation de Hill):
C22H28N6O14P2
Numéro CAS:
Poids moléculaire :
662.44
Numéro MDL:
Code UNSPSC :
41106305
ID de substance PubChem :
Nomenclature NACRES :
NA.51

Source biologique

Porcine brain

Niveau de qualité

Pureté

≥85%

Forme

powder

Solubilité

water: 50 mg/mL, clear, colorless to faintly yellow

Température de stockage

−20°C

Chaîne SMILES 

CC(=O)c1ccc[n+](c1)[C@@H]2O[C@H](COP([O-])(=O)OP(O)(=O)OC[C@H]3O[C@H]([C@H](O)[C@@H]3O)n4cnc5c(N)ncnc45)[C@@H](O)[C@H]2O

InChI

1S/C22H28N6O14P2/c1-10(29)11-3-2-4-27(5-11)21-17(32)15(30)12(40-21)6-38-43(34,35)42-44(36,37)39-7-13-16(31)18(33)22(41-13)28-9-26-14-19(23)24-8-25-20(14)28/h2-5,8-9,12-13,15-18,21-22,30-33H,6-7H2,1H3,(H3-,23,24,25,34,35,36,37)/t12-,13-,15-,16-,17-,18-,21-,22-/m1/s1

Clé InChI

KPVQNXLUPNWQHM-RBEMOOQDSA-N

Catégories apparentées

Description générale

3-Acetylpyridine adenine dinucleotide is a crystalline solid. 3-Acetylpyridine adenine dinucleotide is a prominent electron transporter in various enzymatic activities in which it is alternately oxidized. APAD has a more significant oxidation potential than NAD. NAD analogues, APAD, were electrochemically more effectively reduced than genuine NAD, and the stability of their reduced products was also significantly higher than NADH. In transhydrogenation processes with NADH or NADPH, APAD also operates as a proton acceptor.

Application

Many molecules use 3-Acetylpyridine adenine dinucleotide as a signaling molecule, cofactor, or substrate. Various dehydrogenase processes use APAD instead of NAD as a hydrogen-accepting cofactor. The oxidative phosphorylation can be studied with ADAP. ADAP can also be used as a suitable substrate.

Actions biochimiques/physiologiques

APAD is an NAD analog with higher oxidation potential than NAD. It can substitute for NAD as a hydrogen-accepting cofactor in many dehydrogenase reactions; e.g. lactate dehydrogenase from Toxoplasma, Clonorchis, and Plasmodium, bacterial lipoamide dehydrogenase, as well as mammalian dehydrogenases. It can also act as a proton acceptor in various transhydrogenation reactions with NADH or NADPH.

Liaison

Analog of NAD

Pictogrammes

Exclamation mark

Mention d'avertissement

Warning

Mentions de danger

Classification des risques

Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3

Organes cibles

Respiratory system

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


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Consulter la Bibliothèque de documents

A model of Plasmodium falciparum lactate dehydrogenase and its implications for the design of improved antimalarials and the enhanced detection of parasitaemia.
R B Sessions et al.
Protein engineering, 10(4), 301-306 (1997-04-01)
Guang Yang et al.
Parasitology research, 99(1), 55-64 (2006-02-16)
From a Clonorchis sinensis adult worm cDNA library, we isolated a cDNA clone encoding a novel lactate dehydrogenase (LDH) gene which encoded a putative protein with a predicted molecular weight of 35.6 kDa. The optimum pH and temperature for the
T Bizouarn et al.
European journal of biochemistry, 267(11), 3281-3288 (2000-05-29)
Nicotinamide nucleotide transhydrogenase from Escherichia coli is composed of two subunits, the alpha and the beta subunits, each of which contains a hydrophilic domain, domain I and III, respectively, as well as several transmembrane helices, collectively denoted domain II. The
N V Zakharova
Biochemistry. Biokhimiia, 67(6), 651-661 (2002-07-20)
The kinetics of the NADH-->3;-acetylpyridine adenine dinucleotide (APAD+) transhydrogenase reaction (DD-reaction) catalyzed by different preparations of mitochondrial NADH-dehydrogenase (submitochondrial particles (SMP), purified Complex I, and three-subunit fragment of Complex I (FP)) have been studied. Complex I (in SMP or in
C Diggle et al.
European journal of biochemistry, 241(1), 162-170 (1996-10-01)
Transhydrogenase comprises three domains. Domains I and III are peripheral to the membrane and possess the NAD(H)- and NADP(H)-binding sites, respectively, and domain II spans the membrane. Domain III of transhydrogenase from Rhodospirillum rubrum was expressed at high levels in

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