BRENDA - Enzyme Database show

Nicotinamide N-methyltransferase regulates hepatic nutrient metabolism through Sirt1 protein stabilization

Hong, S.; Moreno-Navarrete, J.M.; Wei, X.; Kikukawa, Y.; Tzameli, I.; Prasad, D.; Lee, Y.; Asara, J.M.; Fernandez-Real, J.M.; Maratos-Flier, E.; Pissios, P.; Nat. Med. 21, 887-894 (2015)

Data extracted from this reference:

Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2.1.1.1
S-adenosyl-L-methionine + nicotinamide
Mus musculus
-
S-adenosyl-L-homocysteine + 1-methylnicotinamide
-
-
?
2.1.1.1
S-adenosyl-L-methionine + nicotinamide
Mus musculus C57Bl6/J
-
S-adenosyl-L-homocysteine + 1-methylnicotinamide
-
-
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
2.1.1.1
Mus musculus
-
-
-
2.1.1.1
Mus musculus C57Bl6/J
-
-
-
Source Tissue
EC Number
Source Tissue
Commentary
Organism
Textmining
2.1.1.1
hepatocyte
primary
Mus musculus
-
2.1.1.1
liver
hepatic expression of Nnmt is highly variable and correlates with multiple metabolic parameters in humans
Mus musculus
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2.1.1.1
S-adenosyl-L-methionine + nicotinamide
-
734757
Mus musculus
S-adenosyl-L-homocysteine + 1-methylnicotinamide
-
-
-
?
2.1.1.1
S-adenosyl-L-methionine + nicotinamide
-
734757
Mus musculus C57Bl6/J
S-adenosyl-L-homocysteine + 1-methylnicotinamide
-
-
-
?
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
2.1.1.1
S-adenosyl-L-methionine
-
Mus musculus
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
2.1.1.1
S-adenosyl-L-methionine
-
Mus musculus
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2.1.1.1
S-adenosyl-L-methionine + nicotinamide
Mus musculus
-
S-adenosyl-L-homocysteine + 1-methylnicotinamide
-
-
?
2.1.1.1
S-adenosyl-L-methionine + nicotinamide
Mus musculus C57Bl6/J
-
S-adenosyl-L-homocysteine + 1-methylnicotinamide
-
-
?
Source Tissue (protein specific)
EC Number
Source Tissue
Commentary
Organism
Textmining
2.1.1.1
hepatocyte
primary
Mus musculus
-
2.1.1.1
liver
hepatic expression of Nnmt is highly variable and correlates with multiple metabolic parameters in humans
Mus musculus
-
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2.1.1.1
S-adenosyl-L-methionine + nicotinamide
-
734757
Mus musculus
S-adenosyl-L-homocysteine + 1-methylnicotinamide
-
-
-
?
2.1.1.1
S-adenosyl-L-methionine + nicotinamide
-
734757
Mus musculus C57Bl6/J
S-adenosyl-L-homocysteine + 1-methylnicotinamide
-
-
-
?
Expression
EC Number
Organism
Commentary
Expression
2.1.1.1
Mus musculus
hepatic expression of Nnmt is highly variable and correlates with multiple metabolic parameters in mice
additional information
General Information
EC Number
General Information
Commentary
Organism
2.1.1.1
malfunction
suppression of hepatic Nnmt expression in vivo alters glucose and cholesterol metabolism. Primary hepatocytes with Nnmt knockdown have signifi­cantly lower hepatocyte glucose output (50%) and significantly lower expression of genes encoding both catalytic glucose-6-phosphatase (20%) and cytosolic phosphoenolpyruvate carboxykinase 1 (40%) compared with control hepatocytes. In contrast, primary hepatocytes in which Nnmt is overexpressed have 1.4fold higher glucose output, threefold higher expression of glucose-6-phosphatase and fourfold higher expression of phosphoenolpyruvate carboxykinase compared with control hepatocytes
Mus musculus
2.1.1.1
metabolism
enzyme Nnmt regulates glucose and cholesterol metabolism. Sirt1 is required for the metabolic actions of the enzyme, which regulates Sirt1 stability
Mus musculus
2.1.1.1
physiological function
nicotinamide N-methyltransferase is a metabolic regulator in adipocytes and also regulates hepatic nutrient metabolism through Sirt1 protein stabilization, the metabolic effects of the enzyme in the liver are mediated by its product 1-methylnicotinamide. Nnmt is a positive regulator of gluconeogenesis in primary hepatocytes. Methylation of nicotinamide by Nnmt is a major pathway for the clear­ance of excess vitamin B3 from the body
Mus musculus
General Information (protein specific)
EC Number
General Information
Commentary
Organism
2.1.1.1
malfunction
suppression of hepatic Nnmt expression in vivo alters glucose and cholesterol metabolism. Primary hepatocytes with Nnmt knockdown have signifi­cantly lower hepatocyte glucose output (50%) and significantly lower expression of genes encoding both catalytic glucose-6-phosphatase (20%) and cytosolic phosphoenolpyruvate carboxykinase 1 (40%) compared with control hepatocytes. In contrast, primary hepatocytes in which Nnmt is overexpressed have 1.4fold higher glucose output, threefold higher expression of glucose-6-phosphatase and fourfold higher expression of phosphoenolpyruvate carboxykinase compared with control hepatocytes
Mus musculus
2.1.1.1
metabolism
enzyme Nnmt regulates glucose and cholesterol metabolism. Sirt1 is required for the metabolic actions of the enzyme, which regulates Sirt1 stability
Mus musculus
2.1.1.1
physiological function
nicotinamide N-methyltransferase is a metabolic regulator in adipocytes and also regulates hepatic nutrient metabolism through Sirt1 protein stabilization, the metabolic effects of the enzyme in the liver are mediated by its product 1-methylnicotinamide. Nnmt is a positive regulator of gluconeogenesis in primary hepatocytes. Methylation of nicotinamide by Nnmt is a major pathway for the clear­ance of excess vitamin B3 from the body
Mus musculus
Expression (protein specific)
EC Number
Organism
Commentary
Expression
2.1.1.1
Mus musculus
hepatic expression of Nnmt is highly variable and correlates with multiple metabolic parameters in mice
additional information