Adenosine monophosphate deaminase (AMP deaminase) (AMPD)

Adenosine monophosphate deaminase (AMPD) is a critical regulatory enzyme in the purine nucleotide cycle that catalyzes the hydrolytic deamination of AMP to inosine monophosphate (IMP) and ammonia (UniProt P23109). It exists in three tissue-specific isoforms: AMPD1, primarily expressed in skeletal muscle; AMPD2, found in the liver and brain; and AMPD3, located in erythrocytes (PubMed: 10455118). The enzyme plays a vital role in maintaining cellular energy homeostasis by regulating the AMP:ATP ratio and facilitating the production of IMP, which serves as a precursor for uric acid synthesis (PubMed: 22553255). Genetic deficiency of the AMPD1 isoform is the primary cause of myoadenylate deaminase deficiency, a metabolic myopathy characterized by exercise-induced muscle pain, cramping, and premature fatigue (StatPearls: Myoadenylate Deaminase Deficiency). Conversely, overactivity of the AMPD2 isoform in the liver has been strongly linked to the development of hyperuricemia, obesity, and metabolic syndrome (PubMed: 22553255). While specific FDA-approved drugs targeting AMPD are currently limited, research into small-molecule inhibitors like coformycin analogs is ongoing for the treatment of metabolic and cardiovascular diseases (PubMed: 25100015).

Other names

AMP aminohydrolaseMyoadenylate deaminaseAMPD1AMPD2AMPD3Adenosine monophosphate deaminase 1Adenosine monophosphate deaminase 2Adenosine monophosphate deaminase 3

Inhibition of the catalytic conversion of adenosine monophosphate (AMP) to inosine monophosphate (IMP) and ammonia.