| Tissue Specificity | Predominantly expressed in the liver. A lower expression is seen in the kidney, lung, skeletal muscle, placenta and heart. Not detected in the brain or pancreas. |
| Post Translational Modifications | Deiminated by PADI1 and PADI2. |
| 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. 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. In a developmental context, contributes to low levels of the repressive histone marks that characterize pluripotent embryonic stem cell pre-implantation state. 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. Via its product N1-methylnicotinamide regulates protein acetylation in hepatocytes, by repressing the ubiquitination and increasing the stability of SIRT1 deacetylase. Can also N-methylate other pyridines structurally related to nicotinamide and play a role in xenobiotic detoxification. |
| Protein Name | Nicotinamide N-Methyltransferase |
| Database Links | Reactome: R-HSA-156581Reactome: R-HSA-197264Reactome: R-HSA-2408508 |
| Cellular Localisation | Cytoplasm |
| Alternative Protein Names | Nicotinamide N-Methyltransferase proteinNNMT protein |
Information sourced from Uniprot.org
