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Evolution of active site architecture in the orotidine 5-monophosphate decarboxylase suprafamily Mechanistic insights for 3-keto-L-gulonate 6-phosphate decarboxylase



Evolution of active site architecture in the orotidine 5-monophosphate decarboxylase suprafamily Mechanistic insights for 3-keto-L-gulonate 6-phosphate decarboxylase



FASEB Journal 16(5): A904



The orotidine 5'-monophosphate decarboxylase (OMPDC) suprafamily is the first identified example where active site architecture is the dominant strategy for divergent evolution of enzyme function. 3-keto-L-gulonate 6-phosphate decarboxylase (KGPDC) is a member of the OMPDC suprafamily that catalyzes a magnesium ion-dependent decarboxylation reaction in the catabolic pathway that enables the utilization of L-ascorbate (Ula) by E. coli K-12. Using stereochemical studies and x-ray crystallography of wild-type and site-directed mutants of UlaD (encoding KGPDC in the Ula operon in locus AE000491 of E. coli K-12), we provide a mechanistic viewpoint of the KGPDC reaction that illustrates Nature's opportunistic strategy in using conserved active site residues to catalyze mechanistically distinct reactions in different metabolic pathways.

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Accession: 034891712

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