AMP deaminase

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AliasesAMPD1, MAD, MADA, MMDD, adenosine monophosphate deaminase 1, AMP deaminase, AMPD
External IDsOMIM: 102770 MGI: 88015 HomoloGene: 20 GeneCards: AMPD1
Gene location (Human)
Chromosome 1 (human)
Chr.Chromosome 1 (human)[1]
Chromosome 1 (human)
Genomic location for AMPD1
Genomic location for AMPD1
Band1p13.2Start114,673,090 bp[1]
End114,695,618 bp[1]
RNA expression pattern
PBB GE AMPD1 206121 at fs.png
More reference expression data
RefSeq (mRNA)



RefSeq (protein)



Location (UCSC)Chr 1: 114.67 – 114.7 MbChr 3: 103.07 – 103.1 Mb
PubMed search[3][4]
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.


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]


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]


A deficiency is associated with myoadenylate deaminase deficiency.


  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. 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.

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