AMP deaminase

AMP deaminase 1 is an is_associated_with::enzyme that in humans is encoded by the AMPD1 is_associated_with::gene.

Adenosine monophosphate deaminase is an is_associated_with::enzyme that converts is_associated_with::adenosine monophosphate (AMP) to is_associated_with::inosine monophosphate (IMP), freeing an is_associated_with::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 is_associated_with::purine nucleotide cycle. Two other genes have been identified, AMPD2 and is_associated_with::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.

Function
It is a part of the is_associated_with::metabolic process that converts is_associated_with::sugar, is_associated_with::fat, and is_associated_with::protein into cellular energy.

In order to use energy, a cell converts one of the above fuels into is_associated_with::adenosine triphosphate (ATP) via the mitochondria. Cellular processes, especially is_associated_with::muscles, then convert the ATP into is_associated_with::adenosine diphosphate (ADP), freeing the energy to do work.

A new research report shows that the widely-prescribed diabetes medication is_associated_with::metformin works on AMP kinase by directly inhibiting AMP deaminase, thereby increasing cellular AMP.

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.

Pathology
A deficiency is associated with is_associated_with::myoadenylate deaminase deficiency.