2.1.1.1: nicotinamide N-methyltransferase
This is an abbreviated version!
For detailed information about nicotinamide N-methyltransferase, go to the full flat file.
Reaction
Synonyms
ANMT-1, B0303.2, methyltransferase, nicotinamide, nicotinamide N-methyl transferase, nicotinamide N-methyltransferase, NNMT
ECTree
2.1.1.1 nicotinamide N-methyltransferaseAdvanced search results
results (
results (Crystallization
Crystallization on EC 2.1.1.1 - nicotinamide N-methyltransferase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
CRYSTALLIZATION (Commentary) 
ORGANISM
UNIPROT
LITERATURE
docking of inhibitors to the NNMT nicotinamide-binding site produces a robust correlation between ligand-enzyme interaction docking scores and experimentally calculated IC50 values
His-tagged K100A/E101A/E103A mutant, sitting drop vapor diffusion method, PEG3350
in complex with inhibitor (2S,5S)-2-amino-5-(((2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl)methyl)-7-(3-carbamoylphenyl)hept-6-ynoic acid. The alkynyl linker is able to span the methyl transfer tunnel of NNMT with ideal shape complementarity
in complex with inhibitor 5'-[[(3S)-3-amino-3-carboxypropyl][(3-carbamoylphenyl)methyl]amino]-5'-deoxyadenosine
in complex with inhibitors (S)-amino-4-((((2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl)methyl)(3-(3-carbamoylphenyl)propyl)amino)butanoic acid and (S)-2-amino-4-((((2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl)methyl)(3-(3-carbamoylphenyl)prop-2-yn-1-yl)amino)butanoic acid
in silico molecular docking. Substrate 4-phenylpyridine binds to the active site of NNMT in two non-redundant poses, one a substrate binding mode and the other an inhibitory mode
in complex with product, 1-methyl nicotinamide, and demethylated cofactor, S-adenosyl-homocysteine, to 1.88 A resolution. 1-methyl nicotinamide binds to the active site and it would be trapped in the active site due to the formation of the bridge between the pole and long C-terminal loop
in complex with product, 1-methyl nicotinamide, and demethylated cofactor, S-adenosyl-homocysteine, to 1.88 A resolution. 1-methyl nicotinamide binds to the active site and it would be trapped in the active site due to the formation of the bridge between the pole and long C-terminal loop
in complex with product, 1-methyl nicotinamide, and demethylated cofactor, S-adenosyl-homocysteine, to 1.88 A resolution. 1-methyl nicotinamide binds to the active site and it would be trapped in the active site due to the formation of the bridge between the pole and long C-terminal loop
