Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase
Diaminopimelate decarboxylase (DapDC, EC 4.1.1.20) participates in the last step of lysine biosynthesis. It converts meso-2,6-diaminoheptanedioate to L-lysine. It is a fold type III PLP-dependent enzyme that contains an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. DapDC exists as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Homodimer formation and the presence of the PLP cofactor are required for catalytic activity.
Comment:The active site is composed of residues from both subunits of the dimer. There are two active sites in the functional dimer. Only one subunit is shown in the structure 1KNW_A.
Structure:1KNW_A; Escherichia coli Diaminopimelate decarboxylase binds PLP and MES; defined at 4A contacts.
Structure:1TWI_AB; Methanocaldococcus jannaschii Diaminopimelate decarboxylase dimer binds two cofactors (PLP) and two substrates (L-lysine); defined at 4A contacts.
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