N6-methyladenosine monophosphate deaminase (MAPDA)

**N6-methyladenosine monophosphate deaminase (MAPDA)** is a recently described **metal-dependent enzyme** found in various organisms including *Arabidopsis thaliana*, humans (as ADAL1), and certain bacteria. This enzyme specifically catalyzes the **hydrolytic deamination of N6-methyladenosine monophosphate (N6-mAMP)** to inosine monophosphate (IMP), distinct from classical adenosine deaminase in substrate specificity as it does not act on unmethylated AMP or adenosine[3][4][5][6]. Structurally, MAPDA possesses a conserved (β/α)\_8 TIM-barrel fold and a zinc-binding site[3][5]. The enzyme is physiologically important for **purine salvage, the control of epigenetic nucleotide modifications, and possibly preventing misincorporation of methylated nucleotides into RNA/DNA**[3][6]. The biological functions and clinical implications of MAPDA are still being explored, with no known drugs or established disease indications as of now[3][5][6]. There is no evidence of use as a direct therapeutic target, but its unique role in nucleotide metabolism may have future relevance as a drug target in metabolic or epigenetic disorders.

Other names

N6-methyl-AMP deaminaseN6-methyladenosine monophosphate aminohydrolaseADAL (ADA-like deaminase)6-methyladenine deaminase (context-dependent)N6-mAMP deaminase

Catalyzes hydrolytic deamination of N6-methyladenosine monophosphate (N6-mAMP) to inosine monophosphate (IMP); removes methyl or alkyl groups from N6-position of purine nucleotides, enabling their recycling or degradation[3][4][6]