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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 deficiency type 1 or AMPD1, is a human metabolic disorder in which the body consistently lacks the enzyme AMP deaminase, [1] in sufficient quantities. This may result in exercise intolerance, muscle pain and muscle cramping. The disease was formerly known as myoadenylate deaminase deficiency (MADD).
AMP can be converted into inosine monophosphate by the enzyme myoadenylate deaminase, freeing an ammonia group. In a catabolic pathway, the purine nucleotide cycle , adenosine monophosphate can be converted to uric acid , which is excreted from the body in mammals.
AMP deaminase deficiency (formally known as myoadenylate deaminase deficiency or MADD) is a metabolic myopathy which results in excessive AMP buildup brought on by exercise. AMP deaminase is needed to convert AMP into IMP in the purine nucleotide cycle.
AMP deaminase 3 is an enzyme that in humans is encoded by the AMPD3 gene. [5] [6]This gene encodes a member of the AMP deaminase gene family. The encoded protein is a highly regulated enzyme that catalyzes the hydrolytic deamination of adenosine monophosphate to inosine monophosphate, a branch point in the adenylate catabolic pathway.
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A nucleotidase creates adenosine, then adenosine deaminase creates inosine; Alternatively, AMP deaminase creates inosinic acid, then a nucleotidase creates inosine; Purine nucleoside phosphorylase acts upon inosine to create hypoxanthine; Xanthine oxidase catalyzes the biotransformation of hypoxanthine to xanthine