Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase
This subfamily is composed mainly of eukaryotic ornithine decarboxylases (ODC, EC 4.1.1.17) and ODC-like enzymes from prokaryotes represented by Vibrio vulnificus LysineOrnithine decarboxylase. These are fold type III PLP-dependent enzymes that differ from most bacterial ODCs which are fold type I PLP-dependent enzymes. ODC participates in the formation of putrescine by catalyzing the decarboxylation of ornithine, the first step in polyamine biosynthesis. Members of this subfamily contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. They exist 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. Also members of this subfamily are proteins with homology to ODC but do not possess any catalytic activity, the Antizyme inhibitor (AZI) and ODC-paralogue (ODC-p). AZI binds to the regulatory protein Antizyme with a higher affinity than ODC and prevents ODC degradation. ODC-p is a novel ODC-like protein, present only in mammals, that is specifically exressed in the brain and testes. ODC-p may function as a tissue-specific antizyme inhibitory protein.
Comment:The active site is composed of residues from both subunits of the dimer. There are two active sites in the functional dimer.
Structure:1F3T_AB; Trypanosoma Brucei Ornithine decarboxylase dimer binds two cofactor-substrate (PLP-putrescine) complexes; defined at 4A contacts. - View structure with Cn3D
Structure:2PLJ_AB; Vibrio vulnificus LysineOrnithine decarboxylase dimer binds two PLP-putrescine complexes; defined at 4A contacts. - View structure with Cn3D
Jiyao W et al.(2023). "The conserved domain database in 2023.",