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Results 1 - 5 of 5
EC Number Cofactor Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.229FAD required for oxidative cleavage of carboxymethyl group from cmnm5U34, FAD-binding site structure, overview 735868, 735869
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.229S-adenosyl-L-methionine - 737223
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.229S-adenosyl-L-methionine binding site structure, overview 720990
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.229S-adenosyl-L-methionine dependent on, the N-terminal MnmC2 domain is composed of residues 1-245 and contains the SAM binding site. The binding pocket is composed of mostly hydrophobic residues, except for Glu101 and Asp178 735868, 735869
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.229S-adenosyl-S-carboxymethyl-L-homocysteine i.e. [(3S)-3-amino-3-carboxypropyl]{[(2S,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methyl}(carboxymethyl)sulfanium, the enzyme contains a cofactor, S-adenosyl-S-carboxymethyl-L-homocysteine (SCM-SAH), in which the donor methyl group is substituted by a carboxymethyl group. The carboxyl moiety forms a salt-bridge interaction with Arg199 that is conserved in a large group of CmoA-related proteins but is not conserved in other S-adenosyl-L-methionine-containing enzymes. The active site contains one molecule cofactor S-adenosyl-S-carboxymethyl-L-homocysteine per monomer, and not S-adenosyl-L-methionine 735357
Results 1 - 5 of 5