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{{Short description|Mammalian protein found in Homo sapiens}}
{{PBB|geneid=270}}
{{Infobox_gene}}


'''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 = October | pmid = 1400401 | doi = }}</ref><ref name="entrez">{{EntrezGene|270}}</ref>
'''AMP deaminase 1''' is an [[enzyme]] that in humans is encoded by the ''AMPD1'' [[gene]].<ref name="pmid1400401">{{cite journal | vauthors = 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 |date=October 1992 | doi = 10.1016/S0021-9258(19)36768-7 | pmid = 1400401 | doi-access = free }}</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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== Function ==
== 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.<ref name="entrez"/>
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"/>


⚫
A research report shows that the widely prescribed diabetes medication [[metformin]] works on [[AMP-activated protein kinase|AMP-activated kinase]] (AMPK) by directly inhibiting AMP deaminase, thereby increasing cellular AMP.<ref name="pmid21059655">{{cite journal | vauthors = Ouyang J, Parakhia RA, Ochs RS | title = Metformin activates AMP kinase through inhibition of AMP deaminase | journal = J. Biol. Chem. | volume = 286 | issue = 1 | pages = 1–11 |date=January 2011 | pmid = 21059655 | pmc = 3012963 | doi = 10.1074/jbc.M110.121806 | doi-access = free }}</ref>
==Function==
It is a part of the [[metabolic process]] that converts [[sugar]], [[fat]], and [[protein]] into cellular energy.{{Citation needed|date=January 2012}}


==Regulation==
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.{{Citation needed|date=January 2012}}
It has been shown that in environments with high potassium concentrations, AMP-deaminase is regulated by ATP and ADP through a “K<sub>m</sub>-type” mechanism. In low potassium ion concentrations, a mixed “K<sub>m</sub> V-type” of the regulation is observed.<ref>{{cite journal|last1=Skladanowski|first1=Andrzej|title=Potassium-dependent regulation by ATP and ADP of AMP-deaminase from beef heart|journal=International Journal of Biochemistry|date=1979|volume=10|issue=2|pages=177–181|doi=10.1016/0020-711X(79)90114-9|pmid=428625}}</ref>


⚫
==Pathology==
⚫
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 name="pmid21059655">{{cite journal | author = Ouyang J, Parakhia RA, Ochs RS | title = Metformin activates AMP kinase through inhibition of AMP deaminase | journal = J. Biol. Chem. | volume = 286 | issue = 1 | pages = 1–11 | year = 2011 | month = January | pmid = 21059655 | pmc = 3012963 | doi = 10.1074/jbc.M110.121806 }}{{Unreliable medical source|date=January 2012}}</ref>
[[myoadenylate deaminase deficiency|AMPD1 deficiency]], also known as '''myoadenylate deaminase deficiency''', is a disorder in which the body produces insufficient AMP deaminase.

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


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


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==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
*{{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 | vauthors=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 |bibcode=1978Sci...200..545F }}
*{{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 | vauthors=Sabina RL, Fishbein WN, Pezeshkpour G |title=Molecular analysis of the myoadenylate deaminase deficiencies. |journal=Neurology |volume=42 |issue= 1 |pages= 170–9 |year= 1992 |pmid= 1370861 |doi= 10.1212/wnl.42.1.170|s2cid=11221341 |display-authors=etal}}
*{{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 | vauthors=Morisaki T, Gross M, Morisaki H |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 |bibcode=1992PNAS...89.6457M |display-authors=etal|doi-access=free }}
*{{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 | vauthors=Sabina RL, Morisaki T, Clarke P |title=Characterization of the human and rat myoadenylate deaminase genes. |journal=J. Biol. Chem. |volume=265 |issue= 16 |pages= 9423–33 |year= 1990 |doi=10.1016/S0021-9258(19)38866-0 |pmid= 2345176 |display-authors=etal|doi-access=free }}
*{{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 | 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 | 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 | vauthors=Mercelis R, Martin JJ, Dehaene I |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 |s2cid=29588220 |display-authors=etal}}
*{{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 | vauthors=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 | 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 | vauthors=Kelemen J, Rice DR, Bradley WG |title=Familial myoadenylate deaminase deficiency and exertional myalgia. |journal=Neurology |volume=32 |issue= 8 |pages= 857–63 |year= 1982 |pmid= 7201581 |doi= 10.1212/wnl.32.8.857|s2cid=39331402 |display-authors=etal}}
*{{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 | vauthors=Baumeister FA, Gross M, Wagner DR |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 |s2cid=32249030 |display-authors=etal}}
*{{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 | vauthors=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= 10.1128/MCB.13.9.5854| pmc=360332 }}
*{{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 | vauthors=Bruno C, Minetti C, Shanske S |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= 10.1212/wnl.50.1.296|s2cid=23521698 |display-authors=etal}}
*{{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 | vauthors=Hisatome I, Morisaki T, Kamma H |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= 10.1152/ajpcell.1998.275.3.C870|display-authors=etal}}
*{{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 | vauthors=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 |s2cid=23996226 }}
*{{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 | vauthors=Loh E, Rebbeck TR, Mahoney PD |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= 10.1161/01.cir.99.11.1422|display-authors=etal|doi-access=free }}
*{{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 | vauthors=Abe M, Higuchi I, Morisaki H |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 |s2cid=21449661 |display-authors=etal}}
*{{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 | vauthors=Morisaki H, Higuchi I, Abe M |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 |s2cid=32543488 |display-authors=etal|doi-access=free }}
*{{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 | vauthors=Gross M, Rötzer E, Kölle P |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 |s2cid=8380610 |display-authors=etal}}
*{{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 | vauthors=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 |doi-access= free }}
{{refend}}
{{refend}}


==External links==
==External links==
* {{MeshName|AMP+Deaminase}}
* {{MeshName|AMP+Deaminase}}
* {{UCSC gene info|AMPD1}}


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{{Carbon-nitrogen non-peptide hydrolases}}
{{Nucleotide metabolism}}
{{Nucleotide metabolism}}
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{{Carbon-nitrogen non-peptide hydrolases}}
{{Enzymes}}
{{Portal bar|Biology|border=no}}


[[Category:EC 3.5.4]]


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{{hydrolase-stub}}


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{{3.5-enzyme-stub}}
[[fi:AMP-deaminaasi]]

Latest revision as of 00:26, 30 January 2023

AMPD1
Identifiers
AliasesAMPD1, MAD, MADA, MMDD, adenosine monophosphate deaminase 1, AMP deaminase, AMPD
External IDsOMIM: 102770; MGI: 88015; HomoloGene: 20; GeneCards: AMPD1; OMA:AMPD1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez

270

229665

Ensembl

ENSG00000116748

ENSMUSG00000070385

UniProt

P23109

Q3V1D3

RefSeq (mRNA)

NM_001172626
NM_000036

NM_001033303

RefSeq (protein)

NP_000027
NP_001166097

NP_001028475

Location (UCSC)Chr 1: 114.67 – 114.7 MbChr 3: 102.98 – 103.01 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

AMP deaminase 1 is an enzyme that in humans is encoded by the AMPD1 gene.[5][6]

Adenosine monophosphate deaminase is an enzyme that converts adenosine monophosphate (AMP) to inosine monophosphate (IMP), freeing an ammonia molecule in the process.

Function

[edit]

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.[6]

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.[7]

Regulation

[edit]

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.[8]

Pathology

[edit]

AMPD1 deficiency, also known as myoadenylate deaminase deficiency, is a disorder in which the body produces insufficient AMP deaminase.

References

[edit]
  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000116748 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000070385 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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". J. Biol. Chem. 267 (29): 20866–77. doi:10.1016/S0021-9258(19)36768-7. PMID 1400401.
  6. ^ a b EntrezGene 270
  7. ^ Ouyang J, Parakhia RA, Ochs RS (January 2011). "Metformin activates AMP kinase through inhibition of AMP deaminase". J. Biol. Chem. 286 (1): 1–11. doi:10.1074/jbc.M110.121806. PMC 3012963. PMID 21059655.
  8. ^ 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

[edit]
[edit]


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