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Evolution of active site architecture in the OMPDC suprafamily Efforts in the design and evolution of 3-keto-L-gulonate 6-phosphate decarboxylase



Evolution of active site architecture in the OMPDC suprafamily Efforts in the design and evolution of 3-keto-L-gulonate 6-phosphate decarboxylase



FASEB Journal 17(4-5): Abstract No 625 2



The orotidine 5'-monophosphate decarboxylase (OMPDC) suprafamily is a group of homologous enzymes that bears testament to the opportunistic nature of enzyme evolution. Members of this suprafamily catalyze unrelated reactions in different metabolic contexts, utilizing a common constellation of active site residues to effect mechanistically distinct reactions in diverse functional contexts. OMPDC is the paradigm member that catalyzes the decarboxylation of OMP to UMP in the de novo pyrimidine biosynthetic pathway; hexulose 6-phosphate synthase (HPS) catalyzes the aldol-condensation reaction between D-ribulose 5-phosphate and formaldehyde in methylotrophs; and 3-keto-L-gulonate 6-phosphate decarboxylase (KGPDC) catalyzes the decarboxylation of 3-keto-L-gulonate 6-phosphate to L-xylulose 5-phosphate in the catabolic pathway of L-ascorbate. Using the scaffold of KGPDC, insights obtained from structural, mechanistic and stereochemical studies on KGPDC form the basis for rational design and directed evolution of enzymes in the OMPDC suprafamily. This research was supported by NIH GM-52594.

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