Disease relevance of Acetylpyridine-adenine dinucleotide

• Dihydrofolate reductase from Escherichia coli: the kinetic mechanism with NADPH and reduced acetylpyridine adenine dinucleotide phosphate as substrates [1].
• In this report we show that the NADP(H)-dependent reduction of acetylpyridine adenine dinucleotide by NADH catalysed by Rhodospirillum rubrum transhydrogenase has 'ping-pong' kinetics, confirming that the reaction is cyclic [2].

High impact information on Acetylpyridine-adenine dinucleotide

• The interaction of 3-acetylpyridine-adenine dinucleotide phosphate, a structural analog of NADPH, with aspartokinase-homoserine dehydrogenase has been studied by fluorescence and activity measurements [3].
• AcPyAD+ provided no protection, and NADH gave partial protection in submitochondrial particles, but not of the purified enzyme [4].
• Structure of Toxoplasma gondii LDH1: active-site differences from human lactate dehydrogenases and the structural basis for efficient APAD+ use [5].
• We have investigated the pre-steady-state kinetics of NADP+ reduction by acetylpyridine adenine dinucleotide (AcPdADH, an analogue of NADH) in complexes formed from the two, separately prepared, recombinant, peripheral subunits of the enzyme: the dI component, which binds NAD+ and NADH, and the dIII component, which binds NADP+ and NADPH [6].
• With membranes, the Km for acetylpyridine adenine dinucleotide during reverse transhydrogenation was 5x and > 6x greater in dI.M239I and dI.M239F, respectively, than in wild-type [7].

Biological context of Acetylpyridine-adenine dinucleotide

• For many animal species this problem can be surmounted by inhibiting NAD hydrolysis with a combination of the anti-tuberculous drug, isonicotinic acid hydrazide, and the NAD analog, 3-acetylpyridine adenine dinucleotide, which act synergistically [8].

Anatomical context of Acetylpyridine-adenine dinucleotide

• Using cytoplasmic membrane vesicles from mutants having elevated activities for transhydrogenation of AcPyAD+ by NADH in the absence of added NADP(H), the kinetics of reduction of AcPyAD+ by NADH and NADPH have been compared [9].
• However, it is shown here that although chromatophore membranes of Rb. capsulatus catalysed the reduction of AcPdAD+ by NADH, the reaction was not associated with the purified H(+)-transhydrogenase [10].

Associations of Acetylpyridine-adenine dinucleotide with other chemical compounds

• In particular, we used isonicotinic acid hydrazide and 3-acetylpyridine adenine dinucleotide to inhibit the potent NAD-glycohydrolase activity of brain membranes, and we used the detergent Triton X-100 (at 0.1%) to improve the accessibility of the toxin and guanine nucleotides used for supporting the ADP-ribosylation [11].
• The reduction of acetylpyridine adenine dinucleotide (AcPdAD+, an NAD+ analogue) by NADPH, in chromatophores treated with valinomycin, was accompanied by alkalinisation of the external medium, as measured by the absorbance change of added cresol red, a simple, non-binding pH indicator [12].
• Characterization of the reduction of 3-acetylpyridine adenine dinucleotide phosphate by benzyl alcohol catalyzed by aldose reductase [13].
• When the two recombinant proteins were mixed with substrates in the stopped-flow spectrophotometer, there was a biphasic burst of hydride transfer from NADPH to the NAD+ analogue, acetylpyridine adenine dinucleotide (AcPdAD+) [14].
• In practical terms, L-lactate synthesis of vesicles incubated in the presence of LDH and APAD was continuously followed by the fluorescence (490 nm) of APADH excited at 410 nm [15].

Gene context of Acetylpyridine-adenine dinucleotide

• Rate constants for the NADPH to 3-acetylpyridine adenine dinucleotide phosphate transhydrogenase activity were similar for all of the Asp139 and His245 mutants and wild-type thioredoxin reductase [16].
• In the GFAT activity assay, the end product reduced acetylpyridine adenine dinucleotide (APADH) was determined at 370 nm directly [17].

Analytical, diagnostic and therapeutic context of Acetylpyridine-adenine dinucleotide

• Reductive titrations of the enzyme with 3-acetylpyridine-adenine dinucleotide, which has a redox potential 72 mV more positive than that of NADH, yield a similar reduced enzyme species [18].
• The reduction of acetylpyridine adenine dinucleotide by NADH: is it a significant reaction of proton-translocating transhydrogenase, or an artefact [19]?

References