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 new 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

A deficiency is associated with myoadenylate deaminase deficiency.

References

  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. 2.0 2.1 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.

Further reading

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