AMPD3

Adenosine monophosphate deaminase (isoform E)
Identifiers
Symbols	AMPD3 ;
External IDs	Template:OMIM5 Template:MGI HomoloGene: 408
Gene ontology Molecular function Template:GNF GO Template:GNF GO Biological process Template:GNF GO Template:GNF GO Template:GNF GO
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Adenosine monophosphate deaminase (isoform E), also known as AMPD3, is a human gene.

This gene encodes a member of the AMP deaminase gene family. The encoded protein is a highly regulated enzyme that catalyzes the hydrolytic deamination of adenosine monophosphate to inosine monophosphate, a branch point in the adenylate catabolic pathway. This gene encodes the erythrocyte (E) isoforms, whereas other family members encode isoforms that predominate in muscle (M) and liver (L) cells. Mutations in this gene lead to the clinically asymptomatic, autosomal recessive condition erythrocyte AMP deaminase deficiency. Alternatively spliced transcript variants encoding different isoforms of this gene have been described.

Further reading

• Zydowo MM (1994). "Regulatory effects of the lipid-cytosolic enzyme interaction: AMP deaminase". Acta Biochim. Pol. 40 (4): 429–32. PMID 8140814.
• Mahnke-Zizelman DK, Sabina RL (1992). "Cloning of human AMP deaminase isoform E cDNAs. Evidence for a third AMPD gene exhibiting alternatively spliced 5'-exons". J. Biol. Chem. 267 (29): 20866–77. PMID 1400401.
• Yamada Y, Goto H, Ogasawara N (1992). "Cloning and nucleotide sequence of the cDNA encoding human erythrocyte-specific AMP deaminase". Biochim. Biophys. Acta. 1171 (1): 125–8. PMID 1420359.CS1 maint: Multiple names: authors list (link)
• Ogasawara N, Goto H, Yamada Y; et al. (1987). "Deficiency of AMP deaminase in erythrocytes". Hum. Genet. 75 (1): 15–8. PMID 3804327.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Yamada Y, Goto H, Murase T, Ogasawara N (1995). "Molecular basis for human erythrocyte AMP deaminase deficiency: screening for the major point mutation and identification of other mutations". Hum. Mol. Genet. 3 (12): 2243–5. PMID 7881427.CS1 maint: Multiple names: authors list (link)
• Yamada Y, Goto H, Ogasawara N (1994). "A point mutation responsible for human erythrocyte AMP deaminase deficiency". Hum. Mol. Genet. 3 (2): 331–4. PMID 8004104.CS1 maint: Multiple names: authors list (link)
• Mahnke-Zizelman DK, Eddy R, Shows TB, Sabina RL (1996). "Characterization of the human AMPD3 gene reveals that 5' exon useage is subject to transcriptional control by three tandem promoters and alternative splicing". Biochim. Biophys. Acta. 1306 (1): 75–92. PMID 8611627.CS1 maint: Multiple names: authors list (link)
• Fortuin FD, Morisaki T, Holmes EW (1997). "Subunit composition of AMPD varies in response to changes in AMPD1 and AMPD3 gene expression in skeletal muscle". Proc. Assoc. Am. Physicians. 108 (4): 329–33. PMID 8863347.CS1 maint: Multiple names: authors list (link)
• Mahnke-Zizelman DK, D'cunha J, Wojnar JM; et al. (1997). "Regulation of rat AMP deaminase 3 (isoform C) by development and skeletal muscle fibre type". Biochem. J. 326 ( Pt 2): 521–9. PMID 9291127.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Yamada Y, Goto H, Wakamatsu N, Ogasawara N (2001). "A rare case of complete human erythrocyte AMP deaminase deficiency due to two novel missense mutations in AMPD3". Hum. Mutat. 17 (1): 78. doi:10.1002/1098-1004(2001)17:1<78::AID-HUMU21>3.0.CO;2-B. PMID 11139257.CS1 maint: Multiple names: authors list (link)
• Mahnke-Zizelman DK, Sabina RL (2003). "N-terminal sequence and distal histidine residues are responsible for pH-regulated cytoplasmic membrane binding of human AMP deaminase isoform E.". J. Biol. Chem. 277 (45): 42654–62. doi:10.1074/jbc.M203473200. PMID 12213808.
• Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Tomikura Y, Hisatome I, Tsuboi M; et al. (2003). "Coordinate induction of AMP deaminase in human atrium with mitochondrial DNA deletion". Biochem. Biophys. Res. Commun. 302 (2): 372–6. PMID 12604357.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Mahnke DK, Sabina RL (2005). "Calcium activates erythrocyte AMP deaminase [isoform E (AMPD3)] through a protein-protein interaction between calmodulin and the N-terminal domain of the AMPD3 polypeptide". Biochemistry. 44 (14): 5551–9. doi:10.1021/bi048121p. PMID 15807549.
• Sabina RL, Waldenström A, Ronquist G (2006). "The contribution of Ca+ calmodulin activation of human erythrocyte AMP deaminase (isoform E) to the erythrocyte metabolic dysregulation of familial phosphofructokinase deficiency". Haematologica. 91 (5): 652–5. PMID 16670071.CS1 maint: Multiple names: authors list (link)