| AMPD3 | |||||||||||||||||||||||||||||||||||||||||||||||||||
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| Aliases | AMPD3, adenosine monophosphate deaminase 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 102772 MGI: 1096344 HomoloGene: 408 GeneCards: AMPD3 | ||||||||||||||||||||||||||||||||||||||||||||||||||
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AMP deaminase 3 is an enzyme that in humans is encoded by the AMPD3 gene.[5][6]
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.[6]
References
- 1 2 3 GRCh38: Ensembl release 89: ENSG00000133805 - Ensembl, May 2017
- 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000005686 - Ensembl, May 2017
- ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ↑ Mahnke-Zizelman DK, Sabina RL (October 1992). "Cloning of human AMP deaminase isoform E cDNAs. Evidence for a third AMPD gene exhibiting alternatively spliced 5'-exons". The Journal of Biological Chemistry. 267 (29): 20866–77. doi:10.1016/S0021-9258(19)36768-7. PMID 1400401.
- 1 2 "Entrez Gene: AMPD3 adenosine monophosphate deaminase (isoform E)".
External links
- Human AMPD3 genome location and AMPD3 gene details page in the UCSC Genome Browser.
Further reading
- Zydowo MM (1994). "Regulatory effects of the lipid-cytosolic enzyme interaction: AMP deaminase". Acta Biochimica Polonica. 40 (4): 429–32. doi:10.18388/abp.1993_4780. PMID 8140814.
- Yamada Y, Goto H, Ogasawara N (November 1992). "Cloning and nucleotide sequence of the cDNA encoding human erythrocyte-specific AMP deaminase". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1171 (1): 125–8. doi:10.1016/0167-4781(92)90153-Q. PMID 1420359.
- Ogasawara N, Goto H, Yamada Y, Nishigaki I, Itoh T, Hasegawa I, Park KS (January 1987). "Deficiency of AMP deaminase in erythrocytes". Human Genetics. 75 (1): 15–8. doi:10.1007/BF00273831. PMID 3804327. S2CID 13377262.
- Yamada Y, Goto H, Murase T, Ogasawara N (December 1994). "Molecular basis for human erythrocyte AMP deaminase deficiency: screening for the major point mutation and identification of other mutations". Human Molecular Genetics. 3 (12): 2243–5. doi:10.1093/hmg/3.12.2243. PMID 7881427.
- Yamada Y, Goto H, Ogasawara N (February 1994). "A point mutation responsible for human erythrocyte AMP deaminase deficiency". Human Molecular Genetics. 3 (2): 331–4. doi:10.1093/hmg/3.2.331. PMID 8004104.
- Mahnke-Zizelman DK, Eddy R, Shows TB, Sabina RL (April 1996). "Characterization of the human AMPD3 gene reveals that 5' exon usage is subject to transcriptional control by three tandem promoters and alternative splicing". Biochimica et Biophysica Acta. 1306 (1): 75–92. doi:10.1016/0167-4781(95)00231-6. PMID 8611627.
- Fortuin FD, Morisaki T, Holmes EW (July 1996). "Subunit composition of AMPD varies in response to changes in AMPD1 and AMPD3 gene expression in skeletal muscle". Proceedings of the Association of American Physicians. 108 (4): 329–33. PMID 8863347.
- Mahnke-Zizelman DK, D'cunha J, Wojnar JM, Brogley MA, Sabina RL (September 1997). "Regulation of rat AMP deaminase 3 (isoform C) by development and skeletal muscle fibre type". The Biochemical Journal. 326 ( Pt 2) (2): 521–9. doi:10.1042/bj3260521. PMC 1218700. PMID 9291127.
- 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". Human Mutation. 17 (1): 78. doi:10.1002/1098-1004(2001)17:1<78::AID-HUMU21>3.0.CO;2-B. PMID 11139257. S2CID 13267360.
- Mahnke-Zizelman DK, Sabina RL (November 2002). "N-terminal sequence and distal histidine residues are responsible for pH-regulated cytoplasmic membrane binding of human AMP deaminase isoform E". The Journal of Biological Chemistry. 277 (45): 42654–62. doi:10.1074/jbc.M203473200. PMID 12213808. S2CID 25657474.
- Tomikura Y, Hisatome I, Tsuboi M, Yamawaki M, Shimoyama M, Yamamoto Y, Sasaki N, Ogino K, Igawa O, Shigemasa C, Ishiguro S, Ohgi S, Nanba E, Shiota G, Morisaki H, Morisaki T, Kitakaze M (March 2003). "Coordinate induction of AMP deaminase in human atrium with mitochondrial DNA deletion" (PDF). Biochemical and Biophysical Research Communications. 302 (2): 372–6. doi:10.1016/S0006-291X(03)00160-8. PMID 12604357. Archived from the original (PDF) on 2022-03-13. Retrieved 2020-09-01.
- Mahnke DK, Sabina RL (April 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 (May 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.
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