PLP undergoes conformational changes during the course of an enzymatic reaction

Structural snapshots of the L-serine dehydratase catalytic reactions of a PLP-dependent enzyme were determined by X-ray crystallography. PLP cofactor catalyzed a series of reactions with active conformational changes and its catalytic role was confirmed by high-level quantum-mechanical calculations.

Divalent metal ion-based catalytic mechanism of the Nudix hydrolase Orf153 (YmfB) from Escherichia coli

The structures of Escherichia coli YmfB on its own and in complex with three sulfates and two manganese ions, when compared with the structures of other Nudix hydrolases such as MutT, Ap₄Aase and DR1025, provide insight into the unique hydrolysis mechanism of YmfB.