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Chemical Compound Review

SAICAR     (2S)-2-[[5-amino-1- [(2R,3R,4S,5R)-3,4...

Synonyms: SAICAriboside, Succino-AICAR, SureCN73325, AG-E-99788, HMDB00797, ...
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Disease relevance of SAICAR


High impact information on SAICAR

  • Importantly, feedback inhibition by ATP of Ade4p, catalyzing the first step of the pathway, appears to regulate SAICAR synthesis in response to adenine availability [3].
  • Two unrelated patients homozygous for one of the thermostable mutations, R303C, also displayed a much more marked decrease in the activity of fibroblast ADSL with S-AMP than with SAICAR, had S-Ado:SAICA riboside ratios between 3 and 4 in their cerebrospinal fluid and were mildly retarded [4].
  • The competitive inhibition by AICAR and AMP suggests a single active site that binds both SAICAR and SAMP [5].
  • To facilitate the assay for CAIR production, the purC gene product, 5-aminoimidazole-4-N-succinylcarboxamide ribonucleotide (SAICAR) synthetase has also been overexpressed and purified to homogeneity [6].
  • SAICAr and SAdo were prepared by calf intestine alkaline phosphatase-catalysed dephosphorylation of SAICAR and SAMP and isolated on cation- and anion-exchange resin columns [7].

Biological context of SAICAR

  • Upon limitation for purines, the SAICAR/AICAR regulatory signal is transmitted to the nucleus to increase Bas1 and Pho2 interaction, recruiting Pho2 to promoters and freeing the activation domains for transactivation [8].

Anatomical context of SAICAR

  • The assays, performed as prescribed, are facile and notably sensitive; using them, the specific activity of SAICAR synthetase has been measured in acetone powders of the livers of representative members of Vertebrata, and also in the principal viscera of the mouse [9].


  1. Cloning of a chicken liver cDNA encoding 5-aminoimidazole ribonucleotide carboxylase and 5-aminoimidazole-4-N-succinocarboxamide ribonucleotide synthetase by functional complementation of Escherichia coli pur mutants. Chen, Z.D., Dixon, J.E., Zalkin, H. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  2. Structure of SAICAR synthase from Thermotoga maritima at 2.2 angstroms reveals an unusual covalent dimer. Zhang, R., Skarina, T., Evdokimova, E., Edwards, A., Savchenko, A., Laskowski, R., Cuff, M.E., Joachimiak, A. Acta Crystallograph. Sect. F Struct. Biol. Cryst. Commun. (2006) [Pubmed]
  3. Yeast AMP pathway genes respond to adenine through regulated synthesis of a metabolic intermediate. Rébora, K., Desmoucelles, C., Borne, F., Pinson, B., Daignan-Fornier, B. Mol. Cell. Biol. (2001) [Pubmed]
  4. Clinical, biochemical and molecular genetic correlations in adenylosuccinate lyase deficiency. Race, V., Marie, S., Vincent, M.F., Van den Berghe, G. Hum. Mol. Genet. (2000) [Pubmed]
  5. Expression, purification, and kinetic characterization of recombinant human adenylosuccinate lyase. Stone, R.L., Zalkin, H., Dixon, J.E. J. Biol. Chem. (1993) [Pubmed]
  6. Purification and characterization of the purE, purK, and purC gene products: identification of a previously unrecognized energy requirement in the purine biosynthetic pathway. Meyer, E., Leonard, N.J., Bhat, B., Stubbe, J., Smith, J.M. Biochemistry (1992) [Pubmed]
  7. Preparation of 5-amino-4-imidazole-N-succinocarboxamide ribotide, 5-amino-4-imidazole-N-succinocarboxamide riboside and succinyladenosine, compounds usable in diagnosis and research of adenylosuccinate lyase deficiency. Zikánová, M., Krijt, J., Hartmannová, H., Kmoch, S. J. Inherit. Metab. Dis. (2005) [Pubmed]
  8. DNA-bound Bas1 recruits Pho2 to activate ADE genes in Saccharomyces cerevisiae. Som, I., Mitsch, R.N., Urbanowski, J.L., Rolfes, R.J. Eukaryotic Cell (2005) [Pubmed]
  9. Two complementary radiometric methods for the measurement of 5-amino-4-imidazole-N-succinocarboxamide ribonucleotide synthetase (SAICAR synthetase). Tyagi, A.K., Cooney, D.A., Bledsoe, M., Jayaram, H.N. J. Biochem. Biophys. Methods (1980) [Pubmed]
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