AMPD3

Adenosine monophosphate deaminase (isoform E), also known as AMPD3, is a human gene.cite web | title = Entrez Gene: AMPD3 adenosine monophosphate deaminase (isoform E)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=272| accessdate = ]

PBB_Summary
section_title =
summary_text = 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.cite web | title = Entrez Gene: AMPD3 adenosine monophosphate deaminase (isoform E)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=272| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Zydowo MM |title=Regulatory effects of the lipid-cytosolic enzyme interaction: AMP deaminase. |journal=Acta Biochim. Pol. |volume=40 |issue= 4 |pages= 429–32 |year= 1994 |pmid= 8140814 |doi=
*cite journal | author=Mahnke-Zizelman DK, Sabina RL |title=Cloning of human AMP deaminase isoform E cDNAs. Evidence for a third AMPD gene exhibiting alternatively spliced 5'-exons. |journal=J. Biol. Chem. |volume=267 |issue= 29 |pages= 20866–77 |year= 1992 |pmid= 1400401 |doi=
*cite journal | author=Yamada Y, Goto H, Ogasawara N |title=Cloning and nucleotide sequence of the cDNA encoding human erythrocyte-specific AMP deaminase. |journal=Biochim. Biophys. Acta |volume=1171 |issue= 1 |pages= 125–8 |year= 1992 |pmid= 1420359 |doi=
*cite journal | author=Ogasawara N, Goto H, Yamada Y, "et al." |title=Deficiency of AMP deaminase in erythrocytes. |journal=Hum. Genet. |volume=75 |issue= 1 |pages= 15–8 |year= 1987 |pmid= 3804327 |doi=
*cite journal | author=Yamada Y, Goto H, Murase T, Ogasawara N |title=Molecular basis for human erythrocyte AMP deaminase deficiency: screening for the major point mutation and identification of other mutations. |journal=Hum. Mol. Genet. |volume=3 |issue= 12 |pages= 2243–5 |year= 1995 |pmid= 7881427 |doi=
*cite journal | author=Yamada Y, Goto H, Ogasawara N |title=A point mutation responsible for human erythrocyte AMP deaminase deficiency. |journal=Hum. Mol. Genet. |volume=3 |issue= 2 |pages= 331–4 |year= 1994 |pmid= 8004104 |doi=
*cite journal | author=Mahnke-Zizelman DK, Eddy R, Shows TB, Sabina RL |title=Characterization of the human AMPD3 gene reveals that 5' exon useage is subject to transcriptional control by three tandem promoters and alternative splicing. |journal=Biochim. Biophys. Acta |volume=1306 |issue= 1 |pages= 75–92 |year= 1996 |pmid= 8611627 |doi=
*cite journal | author=Fortuin FD, Morisaki T, Holmes EW |title=Subunit composition of AMPD varies in response to changes in AMPD1 and AMPD3 gene expression in skeletal muscle. |journal=Proc. Assoc. Am. Physicians |volume=108 |issue= 4 |pages= 329–33 |year= 1997 |pmid= 8863347 |doi=
*cite journal | author=Mahnke-Zizelman DK, D'cunha J, Wojnar JM, "et al." |title=Regulation of rat AMP deaminase 3 (isoform C) by development and skeletal muscle fibre type. |journal=Biochem. J. |volume=326 ( Pt 2) |issue= |pages= 521–9 |year= 1997 |pmid= 9291127 |doi=
*cite journal | author=Yamada Y, Goto H, Wakamatsu N, Ogasawara N |title=A rare case of complete human erythrocyte AMP deaminase deficiency due to two novel missense mutations in AMPD3. |journal=Hum. Mutat. |volume=17 |issue= 1 |pages= 78 |year= 2001 |pmid= 11139257 |doi= 10.1002/1098-1004(2001)17:1<78::AID-HUMU21>3.0.CO;2-B |doilabel=10.1002/1098-1004(2001)17:178::AID-HUMU213.0.CO;2-B
*cite journal | author=Mahnke-Zizelman DK, Sabina RL |title=N-terminal sequence and distal histidine residues are responsible for pH-regulated cytoplasmic membrane binding of human AMP deaminase isoform E. |journal=J. Biol. Chem. |volume=277 |issue= 45 |pages= 42654–62 |year= 2003 |pmid= 12213808 |doi= 10.1074/jbc.M203473200
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Tomikura Y, Hisatome I, Tsuboi M, "et al." |title=Coordinate induction of AMP deaminase in human atrium with mitochondrial DNA deletion. |journal=Biochem. Biophys. Res. Commun. |volume=302 |issue= 2 |pages= 372–6 |year= 2003 |pmid= 12604357 |doi=
*cite journal | author=Mahnke DK, Sabina RL |title=Calcium activates erythrocyte AMP deaminase [isoform E (AMPD3)] through a protein-protein interaction between calmodulin and the N-terminal domain of the AMPD3 polypeptide. |journal=Biochemistry |volume=44 |issue= 14 |pages= 5551–9 |year= 2005 |pmid= 15807549 |doi= 10.1021/bi048121p
*cite journal | author=Sabina RL, Waldenström A, Ronquist G |title=The contribution of Ca+ calmodulin activation of human erythrocyte AMP deaminase (isoform E) to the erythrocyte metabolic dysregulation of familial phosphofructokinase deficiency. |journal=Haematologica |volume=91 |issue= 5 |pages= 652–5 |year= 2006 |pmid= 16670071 |doi=

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