An unprecedented twist to ODCase catalytic activity |
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Authors: | Fujihashi Masahiro Bello Angelica M Poduch Ewa Wei Lianhu Annedi Subhash C Pai Emil F Kotra Lakshmi P |
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Affiliation: | Molecular Design and Information Technology Center, Leslie Dan Faculty of Pharmacy, Toronto, ON M5S 2S2 Canada. |
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Abstract: | Orotidine-5'-monophosphate decarboxylase (ODCase) has evolved to catalyze a decarboxylation reaction, most probably via a carbanion species at the C6 position of orotidine-5'-monophosphate. We reveal an unusual biochemical pathway of conversion of 6-cyano-uridine-5'-monophosphate by ODCase to barbiturate-5'-monophosphate via perhaps an electrophilic center at the C6 position, leading to inhibition. This potential of ODCase is very useful in the design of novel inhibitors. |
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