Biology:AMP deaminase
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AMP deaminase 1 is an enzyme that in humans is encoded by the AMPD1 gene.[1][2]
Adenosine monophosphate deaminase is an enzyme that converts adenosine monophosphate (AMP) to inosine monophosphate (IMP), freeing an ammonia molecule in the process.
Function
Adenosine monophosphate deaminase 1 catalyzes the deamination of AMP to IMP in skeletal muscle and plays an important role in the purine nucleotide cycle. Two other genes have been identified, AMPD2 and AMPD3, for the liver- and erythrocyte-specific isoforms, respectively. Deficiency of the muscle-specific enzyme is apparently a common cause of exercise-induced myopathy and probably the most common cause of metabolic myopathy in the human.[2]
A research report shows that the widely prescribed diabetes medication metformin works on AMP-activated kinase (AMPK) by directly inhibiting AMP deaminase, thereby increasing cellular AMP.[3]
Regulation
It has been shown that in environments with high potassium concentrations, AMP-deaminase is regulated by ATP and ADP through a “Km-type” mechanism. In low potassium ion concentrations, a mixed “Km V-type” of the regulation is observed.[4]
Pathology
AMPD1 deficiency, also known as myoadenylate deaminase deficiency, is a disorder in which the body produces insufficient AMP deaminase.
adenosine monophosphate (AMP)
inosine monophosphate (IMP)
References
- ↑ "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. October 1992. doi:10.1016/S0021-9258(19)36768-7. PMID 1400401.
- ↑ 2.0 2.1 EntrezGene 270
- ↑ "Metformin activates AMP kinase through inhibition of AMP deaminase". J. Biol. Chem. 286 (1): 1–11. January 2011. doi:10.1074/jbc.M110.121806. PMID 21059655.
- ↑ Skladanowski, Andrzej (1979). "Potassium-dependent regulation by ATP and ADP of AMP-deaminase from beef heart". International Journal of Biochemistry 10 (2): 177–181. doi:10.1016/0020-711X(79)90114-9. PMID 428625.
Further reading
- "Myoadenylate deaminase deficiency: a new disease of muscle.". Science 200 (4341): 545–8. 1978. doi:10.1126/science.644316. PMID 644316. Bibcode: 1978Sci...200..545F.
- "Molecular analysis of the myoadenylate deaminase deficiencies.". Neurology 42 (1): 170–9. 1992. doi:10.1212/wnl.42.1.170. PMID 1370861.
- "Molecular basis of AMP deaminase deficiency in skeletal muscle.". Proc. Natl. Acad. Sci. U.S.A. 89 (14): 6457–61. 1992. doi:10.1073/pnas.89.14.6457. PMID 1631143. Bibcode: 1992PNAS...89.6457M.
- "Characterization of the human and rat myoadenylate deaminase genes.". J. Biol. Chem. 265 (16): 9423–33. 1990. doi:10.1016/S0021-9258(19)38866-0. PMID 2345176.
- Dale GL (1989). "Radioisotopic assay for erythrocyte adenosine 5'-monophosphate deaminase.". Clin. Chim. Acta 182 (1): 1–7. doi:10.1016/0009-8981(89)90144-7. PMID 2502331.
- "Myoadenylate deaminase deficiency in a patient with facial and limb girdle myopathy.". J. Neurol. 225 (3): 157–66. 1981. doi:10.1007/BF00313744. PMID 6167680.
- "Enzymological studies in chronic lymphocytic leukemia.". Leuk. Res. 7 (2): 261–7. 1983. doi:10.1016/0145-2126(83)90016-4. PMID 6406772.
- "Familial myoadenylate deaminase deficiency and exertional myalgia.". Neurology 32 (8): 857–63. 1982. doi:10.1212/wnl.32.8.857. PMID 7201581.
- "Myoadenylate deaminase deficiency with severe rhabdomyolysis.". Eur. J. Pediatr. 152 (6): 513–5. 1993. doi:10.1007/BF01955062. PMID 8335021.
- "Functionally distinct elements are required for expression of the AMPD1 gene in myocytes.". Mol. Cell. Biol. 13 (9): 5854–60. 1993. doi:10.1128/MCB.13.9.5854. PMID 8355716.
- "Combined defects of muscle phosphofructokinase and AMP deaminase in a child with myoglobinuria.". Neurology 50 (1): 296–8. 1998. doi:10.1212/wnl.50.1.296. PMID 9443500.
- "Control of AMP deaminase 1 binding to myosin heavy chain.". Am. J. Physiol. 275 (3 Pt 1): C870–81. 1998. doi:10.1152/ajpcell.1998.275.3.C870. PMID 9730972.
- "Elevated adenosine monophosphate deaminase activity in Alzheimer's disease brain.". Neurobiol. Aging 19 (5): 385–91. 1999. doi:10.1016/S0197-4580(98)00083-9. PMID 9880040.
- "Common variant in AMPD1 gene predicts improved clinical outcome in patients with heart failure.". Circulation 99 (11): 1422–5. 1999. doi:10.1161/01.cir.99.11.1422. PMID 10086964.
- "Myoadenylate deaminase deficiency with progressive muscle weakness and atrophy caused by new missense mutations in AMPD1 gene: case report in a Japanese patient.". Neuromuscul. Disord. 10 (7): 472–7. 2000. doi:10.1016/S0960-8966(00)00127-9. PMID 10996775.
- "First missense mutations (R388W and R425H) of AMPD1 accompanied with myopathy found in a Japanese patient.". Hum. Mutat. 16 (6): 467–72. 2001. doi:10.1002/1098-1004(200012)16:6<467::AID-HUMU3>3.0.CO;2-V. PMID 11102975.
- "A G468-T AMPD1 mutant allele contributes to the high incidence of myoadenylate deaminase deficiency in the Caucasian population.". Neuromuscul. Disord. 12 (6): 558–65. 2002. doi:10.1016/S0960-8966(02)00008-1. PMID 12117480.
- "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. 2003. doi:10.1074/jbc.M203473200. PMID 12213808.
External links
- AMP+Deaminase at the US National Library of Medicine Medical Subject Headings (MeSH)
- Human AMPD1 genome location and AMPD1 gene details page in the UCSC Genome Browser.
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