Active Site
Two 6,7-dimethyl-8-ribityllumazine (Lumazine synthase) molecules are hydrogen bound to each monomer as the two domains are topologically similar. The active site is located in the interface of the substrates between monomer pairs and modeled structures of the active site dimer have been created. Only one of the active sites of the enzyme catalyze riboflavin formation at a time as the other two sites face outward and are exposed to solvent. The amino acid residues involved in hydrogen bonding to the ligand are pictured, participating residues may include Thr148, Met160, Ile162, Thr165, Val6, Tyr164, Ser146, and Gly96 at the C-terminal domain and Ser41, Thr50, Gly 62, Ala64, Ser64, Val103, Cys48, His102 at the N-terminal domain.
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Hydrogen bonding between substrate and enzyme at the C-terminal domain.
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Hydrogen bonding between substrate and enzyme at the N-terminal domain.
Read more about this topic: Riboflavin Synthase
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