Dimethyl-L-arginine

Asymmetric dimethylarginine (ADMA) is a non-proteinogenic L-alpha-amino acid, that belongs to the guanidines and serves as a derivative of L-arginine. This dimethylarginine functions as an endogenous inhibitor of nitric oxide synthase (NOS) and acts as a biomarker for endothelial dysfunction in various pathological states.

Asymmetric dimethylarginine (ADMA) is a naturally occurring chemical found in blood plasma. It is a metabolic by-product of continual protein modification processes in the cytoplasm of all human cells. It is closely related to L-arginine, a conditionally-essential amino acid. ADMA interferes with L-arginine in the production of nitric oxide, a key chemical to endothelial and hence cardiovascular health. Asymmetric dimethylarginine is created in protein methylation, a common mechanism of post-translational protein modification. This reaction is catalyzed by an enzyme set called S-adenosylmethionine protein N-methyltransferases (protein methylases I and II). The methyl groups transferred to create ADMA are derived from the methyl group donor S-adenosylmethionine, an intermediate in the metabolism of homocysteine. (Homocysteine is an important blood chemical, because it is also a marker of cardiovascular disease). After synthesis, ADMA migrates into the extracellular space and then into blood plasma.

Asymmetric dimethylarginine is a versatile compound that finds application in biochemical and metabolomics research.

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