Recombinant Human NNMT protein

Specifications

Form

Liquid

Additional notes

ab198647 was expressed in E.coli as inclusion bodies, refolded using unique “temperature shift inclusion body refolding” technology, chromatographically purified and sterile filtered.

General info

Function

Catalyzes the N-methylation of nicotinamide using the universal methyl donor S-adenosyl-L-methionine to form N1-methylnicotinamide and S-adenosyl-L-homocysteine, a predominant nicotinamide/vitamin B3 clearance pathway (PubMed : 21823666, PubMed : 23455543, PubMed : 8182091). Plays a central role in regulating cellular methylation potential, by consuming S-adenosyl-L-methionine and limiting its availability for other methyltransferases. Actively mediates genome-wide epigenetic and transcriptional changes through hypomethylation of repressive chromatin marks, such as H3K27me3 (PubMed : 23455543, PubMed : 26571212, PubMed : 31043742). In a developmental context, contributes to low levels of the repressive histone marks that characterize pluripotent embryonic stem cell pre-implantation state (PubMed : 26571212). Acts as a metabolic regulator primarily on white adipose tissue energy expenditure as well as hepatic gluconeogenesis and cholesterol biosynthesis. In white adipocytes, regulates polyamine flux by consuming S-adenosyl-L-methionine which provides for propylamine group in polyamine biosynthesis, whereas by consuming nicotinamide controls NAD(+) levels through the salvage pathway (By similarity). Via its product N1-methylnicotinamide regulates protein acetylation in hepatocytes, by repressing the ubiquitination and increasing the stability of SIRT1 deacetylase (By similarity). Can also N-methylate other pyridines structurally related to nicotinamide and play a role in xenobiotic detoxification (PubMed : 30044909).

Sequence similarities

Belongs to the class I-like SAM-binding methyltransferase superfamily. NNMT/PNMT/TEMT family.

Post-translational modifications

Deiminated by PADI1 and PADI2.