Investigation of the reaction mechanism of orotidine monophosphate decarboxylase using the distortion of the substrate

Orotidine 5'-单磷酸脱羧酶（ODCase）将Orotidine 5'-单磷酸（OMP）脱羧为尿苷5'-单磷酸（UMP）的速度提高了17个量级。我们已经确定了几种配体类似物的晶体结构，并对酶的短寿命中间体进行了计算机模拟。结果表明，ODCase同时利用基态不稳定和过渡态稳定催化脱羧反应。

Orotidine 5'-monophosphate decarboxylase(ODCase) accelerates the decarboxylation of orotidine 5'-monophosphate(OMP) to uridine 5'-monophosphate(UMP) by 17 orders of magnitude. We have determined several crystal structures with ligand analogues and performed computer simulations of the enzyme's short-lived intermediates. The results show that ODCase catalyzes the decarboxylation reaction utilizing both ground state destabilization and transition state stabilization.