BRENDA - Enzyme Database show

Nicotinamide N-methyltransferase increases complex I activity in SH-SY5Y cells via sirtuin 3

Liu, K.Y.; Mistry, R.J.; Aguirre, C.A.; Fasouli, E.S.; Thomas, M.G.; Klamt, F.; Ramsden, D.B.; Parsons, R.B.; Biochem. Biophys. Res. Commun. 467, 491-496 (2015)

Data extracted from this reference:

Cloned(Commentary)
EC Number
Commentary
Organism
2.1.1.1
recombinant stable expression of NNMT-V5 in SH-SY5Y cells increases complex I activity via sirtuin 3
Homo sapiens
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
Homo sapiens
-
S-adenosyl-L-homocysteine + 1-methylnicotinamide
-
-
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
2.1.1.1
Homo sapiens
-
-
-
Source Tissue
EC Number
Source Tissue
Commentary
Organism
Textmining
2.1.1.1
brain
the enzyme is significantly overexpressed in a variety of diseases ranging from cancer to hepatic cirrhosis
Homo sapiens
-
2.1.1.1
additional information
SH-SY5Y human neuroblastoma cells have no endogenous expression of enzyme NNMT
Homo sapiens
-
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
-
733279
Homo sapiens
S-adenosyl-L-homocysteine + 1-methylnicotinamide
-
-
-
?
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
2.1.1.1
S-adenosyl-L-methionine
-
Homo sapiens
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
2.1.1.1
recombinant stable expression of NNMT-V5 in SH-SY5Y cells increases complex I activity via sirtuin 3
Homo sapiens
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
2.1.1.1
S-adenosyl-L-methionine
-
Homo sapiens
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
Homo sapiens
-
S-adenosyl-L-homocysteine + 1-methylnicotinamide
-
-
?
Source Tissue (protein specific)
EC Number
Source Tissue
Commentary
Organism
Textmining
2.1.1.1
brain
the enzyme is significantly overexpressed in a variety of diseases ranging from cancer to hepatic cirrhosis
Homo sapiens
-
2.1.1.1
additional information
SH-SY5Y human neuroblastoma cells have no endogenous expression of enzyme NNMT
Homo sapiens
-
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
-
733279
Homo sapiens
S-adenosyl-L-homocysteine + 1-methylnicotinamide
-
-
-
?
General Information
EC Number
General Information
Commentary
Organism
2.1.1.1
additional information
in vitro overexpression of the enzyme has revealed many cytoprotective effects of NNMT, in particular increased complex I activity and ATP synthesis. siRNA-mediated silencing of sirtuin 3 expression decreases complex I activity in NNMT-expressing SH-SY5Y cells to that observed in wild-type SH-SY5Y, and significantly reduces cellular ATP content also
Homo sapiens
2.1.1.1
physiological function
expression of enzyme NNMT in enzyme-deficient SH-SY5Y human neuroblastoma cells significantly increases the expression of all three sirtuins, class III DNA deacetylase enzymes known to regulate mitochondrial energy production and cell cycle. Sirtuin 3 is a key mediator of NNMT-induced complex I activity and ATP synthesis. Central role for enzyme NNMT in the regulation of energy homeostasis
Homo sapiens
General Information (protein specific)
EC Number
General Information
Commentary
Organism
2.1.1.1
additional information
in vitro overexpression of the enzyme has revealed many cytoprotective effects of NNMT, in particular increased complex I activity and ATP synthesis. siRNA-mediated silencing of sirtuin 3 expression decreases complex I activity in NNMT-expressing SH-SY5Y cells to that observed in wild-type SH-SY5Y, and significantly reduces cellular ATP content also
Homo sapiens
2.1.1.1
physiological function
expression of enzyme NNMT in enzyme-deficient SH-SY5Y human neuroblastoma cells significantly increases the expression of all three sirtuins, class III DNA deacetylase enzymes known to regulate mitochondrial energy production and cell cycle. Sirtuin 3 is a key mediator of NNMT-induced complex I activity and ATP synthesis. Central role for enzyme NNMT in the regulation of energy homeostasis
Homo sapiens