Hole in one! 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 α-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.
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Okrasa et al. (2008) studied this question.
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