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Crystal structure of the pyridoxal‐5′‐phosphate‐dependent serine dehydratase from human liver

L‐serine dehydratase (SDH), a member of the β‐family of pyridoxal phosphate‐dependent (PLP) enzymes, catalyzes the deamination of L‐serine and L‐threonine to yield pyruvate or 2‐oxobutyrate. The crystal structure of L‐serine dehydratase from human liver (hSDH) has been solved at 2.5 Å‐resolution by molecular replacement. The structure is a homodimer and reveals a fold typical for β‐family PLP‐dependent enzymes. Each monomer serves as an active unit and is subdivided into two distinct domains: a small domain and a PLP‐binding domain that covalently anchors the cofactor. Both domains show the typical open α/β architecture of PLP enzymes. Comparison with the rSDH‐(PLP‐OMS) holo‐enzyme reveals a large structural difference in active sites caused by the artifical O‐methylserine. Furthermore, the activity of hSDH‐PLP was assayed and it proved to show catalytic activity. That suggests that the structure of hSDH‐PLP is the first structure of the active natural holo‐SDH.