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Gene Review

AMPD3  -  adenosine monophosphate deaminase 3

Homo sapiens

Synonyms: AMP deaminase 3, AMP deaminase isoform E, Erythrocyte AMP deaminase
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Disease relevance of AMPD3


High impact information on AMPD3


Biological context of AMPD3

  • RNase protection analyses and the partial characterization of human AMPD3 genomic clones demonstrate alternative splicing of three different 5'-terminal exons [7].
  • Nucleotide sequence alignments between AMPD3 cDNAs isolated from several human libraries indicate three different extreme 5'-ends [7].
  • Alternate forms of the AMPD3 cDNAs contain a common 2301-bp open reading frame (ORF) and 3'-untranslated region of 1245 bp [7].
  • Examination of relative rat AMPD3 gene expression shows (1) variable patterns of alternative mRNA abundance across adult tissues, (2) developmental regulation in skeletal muscle and liver, and (3) greater mRNA abundance in adult red (soleus) than in mixed (plantaris) and white (outer gastrocnemius) skeletal muscle [8].
  • Across the region that is common to all rat and human AMPD3 cDNA species, nucleotide and predicted amino acid sequences are 89% and 93% identical respectively, although the rat open reading frame is lacking two separate in-frame codons in the 5' end [8].

Anatomical context of AMPD3

  • This study uses erythrocyte ghosts to characterize the reversible cytoplasmic membrane association of human full-sized recombinant isoform E (AMPD3) [6].
  • These results suggest that expression of the AMPD1 and AMPD3 genes may be coordinated in myocytes to effect production of an AMPD holoenzyme of varying subunit composition [9].
  • The same point mutation was detected in both of the two B-lymphoblast cell lines derived from the complete deficiency of human erythrocyte AMP deaminase: a single nucleotide substitution of C to T resulted in an amino acid change of Arg to Cys at the codon 573 [5].

Associations of AMPD3 with chemical compounds


Other interactions of AMPD3

  • This study identifies a third human AMP deaminase gene, AMPD3 [7].
  • Conversely, residues 129-183 in the AMPD2 polypeptide reduce actomyosin binding of isoform L. In addition, residues 1-48 in the AMPD3 polypeptide dramatically suppress contractile protein binding of isoform E, thus allowing this enzyme to participate in other intracellular interactions [11].
  • Exposure to a calmodulin antagonist significantly slows IMP accumulation during experimental energy imbalance in patients' cells to levels that are similar to those in untreated controls, implying that Ca2+-calmodulin is involved in erythrocyte AMP deaminase activation in familial phosphofructokinase deficiency [12].

Analytical, diagnostic and therapeutic context of AMPD3

  • Western blot analyses detect anti-E-specific immunoreactivity in affinity-purified extracts derived from the bacterial expression of a truncated AMPD3 cDNA [7].
  • Four separate DNA fragments covering the entire coding region of AMPD-3 cDNA were amplified using polymerase chain reaction (PCR) technique and sequenced directly [5].


  1. Calcium activates erythrocyte AMP deaminase [isoform E (AMPD3)] through a protein-protein interaction between calmodulin and the N-terminal domain of the AMPD3 polypeptide. Mahnke, D.K., Sabina, R.L. Biochemistry (2005) [Pubmed]
  2. Remote Reperfusion Lung Injury is Associated With AMP Deaminase 3 Activation and Attenuated by Inosine Monophosphate. Li, P., Ogino, K., Hoshikawa, Y., Morisaki, H., Cheng, J., Toyama, K., Morisaki, T., Hashimoto, K., Ninomiya, H., Tomikura-Shimoyama, Y., Igawa, O., Shigemasa, C., Hisatome, I. Circ. J. (2007) [Pubmed]
  3. Gene expression profiling following constitutive activation of MEK1 and transformation of rat intestinal epithelial cells. Komatsu, K., Buchanan, F.G., Otaka, M., Jin, M., Odashima, M., Horikawa, Y., Watanabe, S., Dubois, R.N. Mol. Cancer (2006) [Pubmed]
  4. Regulation of the interaction of purified human erythrocyte AMP deaminase and the human erythrocyte membrane. Pipoly, G.M., Nathans, G.R., Chang, D., Deuel, T.F. J. Clin. Invest. (1979) [Pubmed]
  5. A point mutation responsible for human erythrocyte AMP deaminase deficiency. Yamada, Y., Goto, H., Ogasawara, N. Hum. Mol. Genet. (1994) [Pubmed]
  6. N-terminal sequence and distal histidine residues are responsible for pH-regulated cytoplasmic membrane binding of human AMP deaminase isoform E. Mahnke-Zizelman, D.K., Sabina, R.L. J. Biol. Chem. (2002) [Pubmed]
  7. Cloning of human AMP deaminase isoform E cDNAs. Evidence for a third AMPD gene exhibiting alternatively spliced 5'-exons. Mahnke-Zizelman, D.K., Sabina, R.L. J. Biol. Chem. (1992) [Pubmed]
  8. Regulation of rat AMP deaminase 3 (isoform C) by development and skeletal muscle fibre type. Mahnke-Zizelman, D.K., D'cunha, J., Wojnar, J.M., Brogley, M.A., Sabina, R.L. Biochem. J. (1997) [Pubmed]
  9. Subunit composition of AMPD varies in response to changes in AMPD1 and AMPD3 gene expression in skeletal muscle. Fortuin, F.D., Morisaki, T., Holmes, E.W. Proc. Assoc. Am. Physicians (1996) [Pubmed]
  10. Regulation of AMP deaminase by phosphoinositides. Sims, B., Mahnke-Zizelman, D.K., Profit, A.A., Prestwich, G.D., Sabina, R.L., Theibert, A.B. J. Biol. Chem. (1999) [Pubmed]
  11. Localization of N-terminal sequences in human AMP deaminase isoforms that influence contractile protein binding. Mahnke-Zizelman, D.K., Sabina, R.L. Biochem. Biophys. Res. Commun. (2001) [Pubmed]
  12. The contribution of Ca+ calmodulin activation of human erythrocyte AMP deaminase (isoform E) to the erythrocyte metabolic dysregulation of familial phosphofructokinase deficiency. Sabina, R.L., Waldenström, A., Ronquist, G. Haematologica (2006) [Pubmed]
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