EC Number |
Reference |
---|
4.2.1.24 | - |
210733 |
4.2.1.24 | crystal structure of enzyme complexed with 4-oxosebaic acid and of enzyme complexed with 4,7-dioxosebaic acid |
652256 |
4.2.1.24 | hanging drop method, enzyme complexed with the inhibitor laevulinic acid at 2.6 A resolution, unit cell parameters: a = 125.24 A, b = 125.24 A, c = 164.6 A and spec group P42(1)2 |
666028 |
4.2.1.24 | hanging drop vapor-diffusion method. Crystal structures of the active site of Pseudomonas aeruginosa PBGS with the various inhibitors 5-hydroxylevulinic acid, 5,5'-oxybis(4-oxopentanoic acid), 5,5'-iminobis(4-oxopentanoic acid), 5,5'-thiobis(4-oxopentanoic acid), 5,5'-sulfinylbis(4-oxopentanoic acid) or 5,5'-sulfonylbis(4-oxopentanoic acid) |
678204 |
4.2.1.24 | hanging drop vapour diffusion method, crystals of the enzyme complex with levulinic acid solved at 1.67 A resolution, crystals belong to space group P42(1)2 with cell dimensions of a = b = 129.8 A, c = 86.7 A |
664001 |
4.2.1.24 | hanging-drop vapour diffusion method, X-ray structure of the enzyme in which the catalytic site of the enzyme is complexed with a putative cyclic intermediate composed of both substrate moieties, solved at 0.16 nm resolution |
649757 |
4.2.1.24 | high-resolution structure of the enzyme cocrystallized with a noncovalently bound moiety of the product, porphobilinogen. The pyrrole side-chain amino group is datively bound to the active-site zinc ion and the porphobilinogen carboxylates interact with the enzyme via hydrogen bonds and salt bridges with invariant residues. Comparison of substrate and product complexes from humans, Escherichia coli and the hyperthermophile Pyrobaculum calidifontis |
746631 |
4.2.1.24 | porphobilinogen synthase is cocrystallized with the alaremycin |
701747 |
4.2.1.24 | sitting-drop vapour-diffusion method |
653303 |
4.2.1.24 | structure of the active-site variant D139N of the Mg2+-dependent enzyme in complex with the inhibitor 5-fluorolevulinic acid |
652890 |