AMP deaminase

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Adenosine monophosphate deaminase 1
External IDs OMIM102770 MGI88015 HomoloGene20 ChEMBL: 2869 GeneCards: AMPD1 Gene
EC number
RNA expression pattern
PBB GE AMPD1 206121 at tn.png
More reference expression data
Species Human Mouse
Entrez 270 229665
Ensembl ENSG00000116748 ENSMUSG00000070385
UniProt P23109 Q3V1D3
RefSeq (mRNA) NM_000036 NM_001033303
RefSeq (protein) NP_000027 NP_001028475
Location (UCSC) Chr 1:
114.67 – 114.7 Mb
Chr 3:
103.07 – 103.1 Mb
PubMed search [1] [2]

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.


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]


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]


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]


A deficiency is associated with myoadenylate deaminase deficiency.


  1. ^ 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. 
  2. ^ a b EntrezGene 270
  3. ^ 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. [unreliable medical source?]
  4. ^ 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. 

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