The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Chemical Compound Review

AcPyAD     [5-(6-aminopurin-9-yl)-3,4- dihydroxy...

Synonyms: NSC-20275, KST-1A0009, AC1Q5ELH, NSC20275, AR-1A8576, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of Acetylpyridine-adenine dinucleotide


High impact information on Acetylpyridine-adenine dinucleotide


Biological context of Acetylpyridine-adenine dinucleotide


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


Gene context of Acetylpyridine-adenine dinucleotide


Analytical, diagnostic and therapeutic context of Acetylpyridine-adenine dinucleotide


  1. Dihydrofolate reductase from Escherichia coli: the kinetic mechanism with NADPH and reduced acetylpyridine adenine dinucleotide phosphate as substrates. Stone, S.R., Morrison, J.F. Biochemistry (1988) [Pubmed]
  2. Mutations at tyrosine-235 in the mobile loop region of domain I protein of transhydrogenase from Rhodospirillum rubrum strongly inhibit hydride transfer. Bizouarn, T., Grimley, R., Diggle, C., Thomas, C.M., Jackson, J.B. Biochim. Biophys. Acta (1997) [Pubmed]
  3. The interaction between Escherichia coli aspartokinase-homoserine dehydrogenase and 3-acetylpyridine-adenine dinucleotide phosphate (reduced), an analog of NADPH. Müller, K., Garel, J.R. J. Biol. Chem. (1984) [Pubmed]
  4. Dicyclohexylcarbodiimide modification of bovine heart mitochondrial transhydrogenase. Pennington, R.M., Fisher, R.R. J. Biol. Chem. (1981) [Pubmed]
  5. Structure of Toxoplasma gondii LDH1: active-site differences from human lactate dehydrogenases and the structural basis for efficient APAD+ use. Kavanagh, K.L., Elling, R.A., Wilson, D.K. Biochemistry (2004) [Pubmed]
  6. A shift in the equilibrium constant at the catalytic site of proton-translocating transhydrogenase: significance for a 'binding-change' mechanism. Venning, J.D., Jackson, J.B. Biochem. J. (1999) [Pubmed]
  7. Role of methionine-239, an amino acid residue in the mobile-loop region of the NADH-binding domain (domain I) of proton-translocating transhydrogenase. Grimley, R.L., Quirk, P.G., Bizouarn, T., Thomas, C.M., Jackson, J.B. Biochemistry (1997) [Pubmed]
  8. ADP-ribosylation of membrane proteins by bacterial toxins in the presence of NAD glycohydrolase. Gill, D.M., Coburn, J. Biochim. Biophys. Acta (1988) [Pubmed]
  9. Mechanism of hydride transfer during the reduction of 3-acetylpyridine adenine dinucleotide by NADH catalyzed by the pyridine nucleotide transhydrogenase of Escherichia coli. Bragg, P.D. FEBS Lett. (1996) [Pubmed]
  10. Purification and properties of the H(+)-nicotinamide nucleotide transhydrogenase from Rhodobacter capsulatus. Lever, T.M., Palmer, T., Cunningham, I.J., Cotton, N.P., Jackson, J.B. Eur. J. Biochem. (1991) [Pubmed]
  11. ADP-ribosylation by cholera toxin of membranes derived from brain modifies the interaction of adenylate cyclase with guanine nucleotides and NaF. Tamir, A., Gill, D.M. J. Neurochem. (1988) [Pubmed]
  12. The ratio of protons translocated/hydride ion equivalent transferred by nicotinamide nucleotide transhydrogenase in chromatophores from Rhodospirillum rubrum. Bizouarn, T., Jackson, J.B. Eur. J. Biochem. (1993) [Pubmed]
  13. Characterization of the reduction of 3-acetylpyridine adenine dinucleotide phosphate by benzyl alcohol catalyzed by aldose reductase. Griffin, B.W., McNatt, L.G. Arch. Biochem. Biophys. (1986) [Pubmed]
  14. Stopped-flow kinetics of hydride transfer between nucleotides by recombinant domains of proton-translocating transhydrogenase. Venning, J.D., Bizouarn, T., Cotton, N.P., Quirk, P.G., Jackson, J.B. Eur. J. Biochem. (1998) [Pubmed]
  15. Continuous enzyme-linked fluorometric detection of L-(+)-lactate released from rat brain vesicles under anoxic conditions. Gleitz, J., Tosch, C., Peters, T. J. Neurosci. Methods (1996) [Pubmed]
  16. Potential active-site base of thioredoxin reductase from Escherichia coli: examination of histidine245 and aspartate139 by site-directed mutagenesis. Mulrooney, S.B., Williams, C.H. Biochemistry (1994) [Pubmed]
  17. A simple and sensitive method for glutamine:fructose-6-phosphate amidotransferase assay. Ye, F., Maegawa, H., Morino, K., Kashiwagi, A., Kikkawa, R., Xie, M., Shen, Z. J. Biochem. Biophys. Methods (2004) [Pubmed]
  18. The streptococcal flavoprotein NADH oxidase. II. Interactions of pyridine nucleotides with reduced and oxidized enzyme forms. Ahmed, S.A., Claiborne, A. J. Biol. Chem. (1989) [Pubmed]
  19. The reduction of acetylpyridine adenine dinucleotide by NADH: is it a significant reaction of proton-translocating transhydrogenase, or an artefact? Stilwell, S.N., Bizouarn, T., Jackson, J.B. Biochim. Biophys. Acta (1997) [Pubmed]
WikiGenes - Universities