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A5251

Sigma-Aldrich

3-Acetylpyridine adenine dinucleotide

≥85%

Sinonimo/i:

3 -Acetyl NAD, APADH, APAD

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About This Item

Formula empirica (notazione di Hill):
C22H28N6O14P2
Numero CAS:
Peso molecolare:
662.44
Numero MDL:
Codice UNSPSC:
41106305
ID PubChem:
NACRES:
NA.51

Origine biologica

Porcine brain

Livello qualitativo

Saggio

≥85%

Forma fisica

powder

Solubilità

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

Temperatura di conservazione

−20°C

Stringa SMILE

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
KPVQNXLUPNWQHM-RBEMOOQDSA-N

Categorie correlate

Descrizione generale

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.

Applicazioni

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.

Azioni biochim/fisiol

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.

Linkage

Analog of NAD

Pittogrammi

Exclamation mark

Avvertenze

Warning

Indicazioni di pericolo

Classi di pericolo

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

Organi bersaglio

Respiratory system

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


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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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