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Structure and mechanism of an unusual malonate decarboxylase and related racemases
K. Okrasa, C. Levy, N. Baudistel, D. Leys and J. Micklefield
Chemistry - A European Journal. 2008;6:6609-6613.
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Abstract
The first structure of an arylmalonate decarboxylase (AMDase; see picture), which reveals the mechanism by which this unusual cofactor-independent enzyme catalyses the decarboxylation of -arylmalonates, is presented. Notably, an active site dioxyanion hole motif is utilised to stabilise a putative high-energy enediolate intermediate. Other AMDases are also characterised, along with a Glu-racemase that also possesses a dioxyanion hole and promiscuous malonate decarboxylase activity.