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Chemical Compound Review

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

Synonyms: NSC-20275, KST-1A0009, AC1Q5ELH, NSC20275, AR-1A8576, ...
 
 
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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

References

  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]
 
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