Crystallization (Comment) | Organism |
---|---|
sitting-drop vapor diffusion method, crystal structures of the enzyme from the hyperthermophilic bacterium Aquifex aeolicus in complex with different inhibitor compounds. The structures are refined at resolutions of 1.72 A (enzyme-7-dioxo-5H-8-ribitylaminolumazine complex), 1.85 A (enzyme-3-(7-hydroxy-8-ribityllumazine-6-yl)propionic acid complex), 2.05 A (enzyme-5-nitroso-6-ribityl-amino-2,4(1H,3H)pyrimidinedione complex) and 2.2 A (enzyme-5-(6-D-ribitylamino-2,4(1H,3H)pyrimidinedione-5-yl)-1-pentyl-phosphonic acid complex), respectively. Structural comparisons of the native enzyme and the inhibitor complexes as well as the kinetic data of single site mutants of lumazine synthase from Bacillus subtilis show that several highly conserved residues at the active site, namely Phe22, His88, Arg127, Lys135 and Glu138 are most likely involved in catalysis. A structural model of the catalytic process, which illustrates binding of substrates, enantiomer specificity, proton abstraction/donation, phosphate elimination, formation of the Schiff base and cyclization is proposed | Aquifex aeolicus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
3-(7-hydroxy-8-ribityllumazine-6-yl)propionic acid | - |
Aquifex aeolicus | |
5-(6-D-ribitylamino-2,4(1H,3H)pyrimidinedione-5-yl)-1-pentyl-phosphonic acid | - |
Aquifex aeolicus | |
5-nitroso-6-ribityl-amino-2,4(1H,3H)pyrimidinedione | - |
Aquifex aeolicus | |
6,7-dioxo-5H-8-ribitylaminolumazine | - |
Aquifex aeolicus |
Organism | UniProt | Comment | Textmining |
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Aquifex aeolicus | - |
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