Modeling of the spatial structure of eukaryotic ornithine decarboxylases

摘要: We used sequence and structural comparisons to determine the fold for eukaryotic ornithine decarboxylase, which we found is related alanine racemase. These enzymes have no detectable identity with any protein of known structure, including three pyridoxal phosphate-utilizing enzymes. Our studies suggest that N-terminal domain decarboxylase folds into a beta/alpha-barrel. Through analysis barrel structures developed topographic model phosphate-binding predicts Schiff base lysine conserved glycine-rich both map C-termini beta-strands. Other residues in this are likely essential roles catalysis, substrate, cofactor binding were also identified, suggesting will be suitable guide mutagenic enzyme mechanism.