3-Acetylpyridine-adenine dinucleotides

Fig. 15. pH dependence of NADPH oxidase, NADPH to 3-acetylpyridine adenine dinucleotide (AP-DPN) transhydrogenase, and NADH oxidase activities of submito-chondrial particles (ETP). Conditions oxidase activities were measured in the presence of 2 mM NADH or NADPH, 0.25 M sucrose, 100 mM sodium phosphate for pH values 6-0, and 100 mM sodium acetate for pH values 5.0 and 5.5. ETP concentration was 2.16 mg/ml for the NADPH oxidase, and 0.216 mg/ml for the NADH oxidase assays. The transhydrogenase reaction was measured by the Aminco-Chance spectrophotometer at 400 minus 450 nm. The extinction coefficient used for reduced 3-acetylpyridine adenine dinucleotide at 400 nm was 2300 liters mole" cm" . Media were the same as in the oxidase assays. Dotted lines indicate uncertainty about the pH 5 rates because of possible acidity damage to ETP. The ordinate refers to nanomoles of NADPH or NADH oxidized min" x mg" of ETP protein at 30°. From Hatefi and Hanstein (,S0). 

Fig. 17. Effect of trypsin on the NADH oxidase, NADPH oxidase and the NADPH-to-NAD transhydrogenase activities of submitochondnal particles. The particles suspended in 0.26 M sucrose and 100 mAf sodium phosphate, pH 7.0, were treated with 0.1 mg trypsin per mg particle protein and incubated at (a) 0° or (b) 30°. At the intervals shown samples were removed and assayed at pH 6.0 and 7.0 for the activities shown. Transhydrogenase activity was measured either directly by reduction of 3-acetylpyridine adenine dinucleotide at 376 nm in the presence of cyanide-treated particles or by the increase in the rate of NADPH oxidation by submitochondrial particles after the addition of NAD. (A) NADH —> O2, ( ) NADPH —> Oi, and (O) NADPH —> NAD. From Djavadi-Ohaniance and Hatefi...

D-Glucitol dehydrogenase has broad substrate-specificity. The enzyme oxidizes D-glucitol, L-iditol, ribitol, and xylitol in the presence of NAD+ cofactor.414 424 NAD+ can be replaced by 3-acetylpyridine adenine dinucleotide (AcPyAD), 3-thionicotinamide adenine dinucleotide (TNAD), or nicotinamide hypoxanthine dinucleotide (NHD).414... 

Oxidized 3-acetylpyridine adenine dinucleotide phosphate. Oxidized 3-acetylpyridine adenine dinucleotide. 

Acetylpyridine adenine dinucleotide 3-Acetyl NAD C22H28N6O14P2 86-08-8 662.436 solid ... 

Acetylpyridine adenine dinucleotide, A-23 3-Acetylpyridine NAD, A-23 i -Acetyl-D-quinovosamine, A-380 i -Acetyl-L-quinovosamine, A-380... 

Acetylpyridine adenine dinucleotide, A-23 Adenosine cyclic 2, 3 -(hydrogen phosphate), A-32 Adenosine diphosphate ucose. A-36 Adenosine diphosphate ribose, A-37 Adenosine diphosphate, A-33... 

In enzymic assays, 3-acetylpyridine adenine dinucleotide (3-APAD) can replace NAD as substrate. No one has as yet succeeded in the direct bromination to form 3-bromo-APAD, although 3-chloro-APAD has been synthesized. If the ribose of the functional moiety of 3-APAD is replaced by a hydrocarbon chain, the redox potential is altered to —320 mV, a magnitude close to that of NAD+ Compounds of this structure can be easily labeled by using methyl or carbonyl-labeled acetylpyridine for synthesis. 

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