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{{PBB|geneid=270}}
{{PBB|geneid=270}}


'''AMP deaminase 1''' is an [[enzyme]] that in humans is encoded by the ''AMPD1'' [[gene]].<ref name="pmid1400401">{{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 | month = Nov | pmid = 1400401 | pmc = | doi = }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: AMPD1 adenosine monophosphate deaminase 1 (isoform M)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=270| accessdate = }}</ref>
'''AMP deaminase 1''' is an [[enzyme]] that in humans is encoded by the ''AMPD1'' [[gene]].<ref name="pmid1400401">{{cite journal |pmid=1400401}}</ref><ref name="entrez">{{EntrezGene|270}}</ref>


Adenosine monophosphate deaminase is an [[enzyme]] that converts [[adenosine monophosphate]] (AMP) to [[inosine monophosphate]] (IMP), freeing an [[ammonia]] molecule in the process.
Adenosine monophosphate deaminase is an [[enzyme]] that converts [[adenosine monophosphate]] (AMP) to [[inosine monophosphate]] (IMP), freeing an [[ammonia]] molecule in the process.
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{{PBB_Summary
{{PBB_Summary
| section_title =
| section_title =
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: AMPD1 adenosine monophosphate deaminase 1 (isoform M)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=270| accessdate = }}</ref>
| summary_text = 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.<ref name="entrez"/>
}}
}}


==Function==
==Function==
It is a part of the [[metabolic process]] that converts [[sugar]], [[fat]], and [[protein]] into cellular energy.
It is a part of the [[metabolic process]] that converts [[sugar]], [[fat]], and [[protein]] into cellular energy.{{fact}}


In order to use energy, a [[cell (biology)|cell]] converts one of the above fuels into [[adenosine triphosphate]] (ATP) via the [[mitochondrion|mitochondria]]. Cellular processes, especially [[muscle]]s, then convert the ATP into [[adenosine diphosphate]] (ADP), freeing the energy to do work.
In order to use energy, a [[cell (biology)|cell]] converts one of the above fuels into [[adenosine triphosphate]] (ATP) via the [[mitochondrion|mitochondria]]. Cellular processes, especially [[muscle]]s, then convert the ATP into [[adenosine diphosphate]] (ADP), freeing the energy to do work.{{fact}}


A new research report <ref>http://www.ncbi.nlm.nih.gov/pubmed/21059655</ref> shows that the widely-prescribed diabetes medication metformin http://en.wikipedia.org/wiki/Metformin works on AMP kinase by directly inhibiting AMP deaminase, thereby increasing cellular AMP.
A new research report shows that the widely-prescribed diabetes medication [[metformin]] works on AMP kinase by directly inhibiting AMP deaminase, thereby increasing cellular AMP.<ref>{{cite journal |pmid=21059655}}{{MEDRS}}</ref>


==Pathology==
==Pathology==
A deficiency is associated with [[myoadenylate deaminase deficiency]].
A deficiency is associated with [[myoadenylate deaminase deficiency]].

⚫
<gallery>
⚫
Image:AMP structure.svg|[[adenosine monophosphate]] (AMP)
⚫
Image:Inosine monophosphate.svg|[[inosine monophosphate]] (IMP)
⚫
</gallery>


==References==
==References==
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{{PBB_Further_reading
{{PBB_Further_reading
| citations =
| citations =
*{{cite journal |doi=10.1126/science.644316}}
*{{cite journal | author=Fishbein WN, Armbrustmacher VW, Griffin JL |title=Myoadenylate deaminase deficiency: a new disease of muscle. |journal=Science |volume=200 |issue= 4341 |pages= 545–8 |year= 1978 |pmid= 644316 |doi=10.1126/science.644316 }}
*{{cite journal |pmid=1370861}}
*{{cite journal | author=Sabina RL, Fishbein WN, Pezeshkpour G, ''et al.'' |title=Molecular analysis of the myoadenylate deaminase deficiencies. |journal=Neurology |volume=42 |issue= 1 |pages= 170–9 |year= 1992 |pmid= 1370861 |doi= }}
*{{cite journal |doi=10.1073/pnas.89.14.6457}}
*{{cite journal | author=Morisaki T, Gross M, Morisaki H, ''et al.'' |title=Molecular basis of AMP deaminase deficiency in skeletal muscle. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 14 |pages= 6457–61 |year= 1992 |pmid= 1631143 |doi=10.1073/pnas.89.14.6457 | pmc=49520 }}
*{{cite journal |pmid=2345176}}
*{{cite journal | author=Sabina RL, Morisaki T, Clarke P, ''et al.'' |title=Characterization of the human and rat myoadenylate deaminase genes. |journal=J. Biol. Chem. |volume=265 |issue= 16 |pages= 9423–33 |year= 1990 |pmid= 2345176 |doi= }}
*{{cite journal | author=Dale GL |title=Radioisotopic assay for erythrocyte adenosine 5'-monophosphate deaminase. |journal=Clin. Chim. Acta |volume=182 |issue= 1 |pages= 1–7 |year= 1989 |pmid= 2502331 |doi=10.1016/0009-8981(89)90144-7 }}
*{{cite journal |doi=10.1016/0009-8981(89)90144-7}}
*{{cite journal |doi=10.1007/BF00313744}}
*{{cite journal | author=Mercelis R, Martin JJ, Dehaene I, ''et al.'' |title=Myoadenylate deaminase deficiency in a patient with facial and limb girdle myopathy. |journal=J. Neurol. |volume=225 |issue= 3 |pages= 157–66 |year= 1981 |pmid= 6167680 |doi=10.1007/BF00313744 }}
*{{cite journal |doi=10.1016/0145-2126(83)90016-4}}
*{{cite journal | author=van Laarhoven JP, de Gast GC, Spierenburg GT, de Bruyn CH |title=Enzymological studies in chronic lymphocytic leukemia. |journal=Leuk. Res. |volume=7 |issue= 2 |pages= 261–7 |year= 1983 |pmid= 6406772 |doi=10.1016/0145-2126(83)90016-4 }}
*{{cite journal |pmid=7201581}}
*{{cite journal | author=Kelemen J, Rice DR, Bradley WG, ''et al.'' |title=Familial myoadenylate deaminase deficiency and exertional myalgia. |journal=Neurology |volume=32 |issue= 8 |pages= 857–63 |year= 1982 |pmid= 7201581 |doi= }}
*{{cite journal |doi=10.1007/BF01955062}}
*{{cite journal | author=Baumeister FA, Gross M, Wagner DR, ''et al.'' |title=Myoadenylate deaminase deficiency with severe rhabdomyolysis. |journal=Eur. J. Pediatr. |volume=152 |issue= 6 |pages= 513–5 |year= 1993 |pmid= 8335021 |doi=10.1007/BF01955062 }}
*{{cite journal |pmid=8355716}}
*{{cite journal | author=Morisaki T, Holmes EW |title=Functionally distinct elements are required for expression of the AMPD1 gene in myocytes. |journal=Mol. Cell. Biol. |volume=13 |issue= 9 |pages= 5854–60 |year= 1993 |pmid= 8355716 |doi= | pmc=360332 }}
*{{cite journal |pmid= 9443500}}
*{{cite journal | author=Bruno C, Minetti C, Shanske S, ''et al.'' |title=Combined defects of muscle phosphofructokinase and AMP deaminase in a child with myoglobinuria. |journal=Neurology |volume=50 |issue= 1 |pages= 296–8 |year= 1998 |pmid= 9443500 |doi= }}
*{{cite journal |pmid=9730972}}
*{{cite journal | author=Hisatome I, Morisaki T, Kamma H, ''et al.'' |title=Control of AMP deaminase 1 binding to myosin heavy chain. |journal=Am. J. Physiol. |volume=275 |issue= 3 Pt 1 |pages= C870–81 |year= 1998 |pmid= 9730972 |doi= }}
*{{cite journal |doi=10.1016/S0197-4580(98)00083-9}}
*{{cite journal | author=Sims B, Powers RE, Sabina RL, Theibert AB |title=Elevated adenosine monophosphate deaminase activity in Alzheimer's disease brain. |journal=Neurobiol. Aging |volume=19 |issue= 5 |pages= 385–91 |year= 1999 |pmid= 9880040 |doi=10.1016/S0197-4580(98)00083-9 }}
*{{cite journal |pmid=10086964}}
*{{cite journal | author=Loh E, Rebbeck TR, Mahoney PD, ''et al.'' |title=Common variant in AMPD1 gene predicts improved clinical outcome in patients with heart failure. |journal=Circulation |volume=99 |issue= 11 |pages= 1422–5 |year= 1999 |pmid= 10086964 |doi= }}
*{{cite journal |doi=10.1016/S0960-8966(00)00127-9}}
*{{cite journal | author=Abe M, Higuchi I, Morisaki H, ''et al.'' |title=Myoadenylate deaminase deficiency with progressive muscle weakness and atrophy caused by new missense mutations in AMPD1 gene: case report in a Japanese patient. |journal=Neuromuscul. Disord. |volume=10 |issue= 7 |pages= 472–7 |year= 2000 |pmid= 10996775 |doi=10.1016/S0960-8966(00)00127-9 }}
*{{cite journal | author=Morisaki H, Higuchi I, Abe M, ''et al.'' |title=First missense mutations (R388W and R425H) of AMPD1 accompanied with myopathy found in a Japanese patient. |journal=Hum. Mutat. |volume=16 |issue= 6 |pages= 467–72 |year= 2001 |pmid= 11102975 |doi= 10.1002/1098-1004(200012)16:6<467::AID-HUMU3>3.0.CO;2-V }}
*{{cite journal |doi=10.1002/1098-1004(200012)16:6<467::AID-HUMU3>3.0.CO;2-V}}
*{{cite journal |doi=10.1016/S0960-8966(02)00008-1}}
*{{cite journal | author=Gross M, Rötzer E, Kölle P, ''et al.'' |title=A G468-T AMPD1 mutant allele contributes to the high incidence of myoadenylate deaminase deficiency in the Caucasian population. |journal=Neuromuscul. Disord. |volume=12 |issue= 6 |pages= 558–65 |year= 2002 |pmid= 12117480 |doi=10.1016/S0960-8966(02)00008-1 }}
*{{cite journal |doi=10.1074/jbc.M203473200}}
*{{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 |doi=10.1073/pnas.242603899}}
*{{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 | pmc=139241 }}
}}
}}
{{refend}}
{{refend}}

⚫
<gallery>
⚫
Image:AMP structure.svg|[[adenosine monophosphate]] (AMP)
⚫
Image:Inosine monophosphate.svg|[[inosine monophosphate]] (IMP)
⚫
</gallery>


==External links==
==External links==

Revision as of 16:18, 20 January 2012

Template:PBB

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.

Template:PBB Summary

Function

It is a part of the metabolic process that converts sugar, fat, and protein into cellular energy.[citation needed]

In order to use energy, a cell converts one of the above fuels into adenosine triphosphate (ATP) via the mitochondria. Cellular processes, especially muscles, then convert the ATP into adenosine diphosphate (ADP), freeing the energy to do work.[citation needed]

A new research report shows that the widely-prescribed diabetes medication metformin works on AMP kinase by directly inhibiting AMP deaminase, thereby increasing cellular AMP.[3]

Pathology

A deficiency is associated with myoadenylate deaminase deficiency.

References

  1. ^ . PMID 1400401. {{cite journal}}: Cite journal requires |journal= (help); Missing or empty |title= (help)
  2. ^ EntrezGene 270
  3. ^ . PMID 21059655. {{cite journal}}: Cite journal requires |journal= (help); Missing or empty |title= (help)[unreliable medical source?]

Further reading

Template:PBB Further reading

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