Department of Chemistry, University at Buffalo, SUNY, Buffalo, NY 14260-3000, USA.
Biochemistry. 2013 Jan 22;52(3):537-46. doi: 10.1021/bi301650d. Epub 2013 Jan 11.
The syntheses of two novel truncated analogs of the natural substrate orotidine 5'-monophosphate (OMP) for orotidine 5'-monophosphate decarboxylase (OMPDC) with enhanced reactivity toward decarboxylation are reported: 1-(β-d-erythrofuranosyl)-5-fluoroorotic acid (FEO) and 5'-deoxy-5-fluoroorotidine (5'-dFO). A comparison of the second-order rate constants for the OMPDC-catalyzed decarboxylations of FEO (10 M⁻¹ s⁻¹) and 1-(β-d-erythrofuranosyl)orotic acid (EO, 0.026 M⁻¹ s⁻¹) shows that the vinyl carbanion-like transition state is stabilized by 3.5 kcal/mol by interactions with the 5-F substituent of FEO. The OMPDC-catalyzed decarboxylations of FEO and EO are both activated by exogenous phosphite dianion (HPO₃²⁻), but the 5-F substituent results in only a 0.8 kcal stabilization of the transition state for the phosphite-activated reaction of FEO. This provides strong evidence that the phosphite-activated OMPDC-catalyzed reaction of FEO is not limited by the chemical step of decarboxylation of the enzyme-bound substrate. Evidence is presented that there is a change in the rate-limiting step from the chemical step of decarboxylation for the phosphite-activated reaction of EO, to closure of the phosphate gripper loop and an enzyme conformational change at the ternary E•FEO•HPO₃²⁻ complex for the reaction of FEO. The 4'-CH₃ and 4'-CH₂OH groups of 5'-dFO and orotidine, respectively, result in identical destabilizations of the transition state for the unactivated decarboxylation of 2.9 kcal/mol. By contrast, the 4'-CH₃ group of 5'-dFO and the 4'-CH₂OH group of orotidine result in very different 4.7 and 8.3 kcal/mol destabilizations of the transition state for the phosphite-activated decarboxylation. Here, the destabilizing effect of the 4'-CH₃ substituent at 5'-dFO is masked by the rate-limiting conformational change that depresses the third-order rate constant for the phosphite-activated reaction of the parent substrate FEO.
报告了两种新型截短类似物的合成,它们是天然底物乳清酸 5'-单磷酸(OMP)的 OMP 脱羧酶(OMPDC)的类似物,具有增强的脱羧反应性:1-(β-d-呋喃核糖基)-5-氟乳清酸(FEO)和 5'-脱氧-5-氟乳苷(5'-dFO)。OMPDC 催化的 FEO(10 M⁻¹ s⁻¹)和 1-(β-d-呋喃核糖基)乳清酸(EO,0.026 M⁻¹ s⁻¹)脱羧反应的二级速率常数的比较表明,乙烯碳负离子样过渡态通过与 FEO 的 5-F 取代基相互作用稳定了 3.5 kcal/mol。FEO 的 OMPDC 催化脱羧和 EO 的 OMPDC 催化脱羧均受外源亚磷酸二阴离子(HPO₃²⁻)激活,但 5-F 取代基仅使 FEO 的亚磷酸激活反应的过渡态稳定 0.8 kcal。这提供了强有力的证据表明,FEO 的亚磷酸激活的 OMPDC 催化反应不受酶结合底物脱羧的化学步骤的限制。有证据表明,对于 EO 的亚磷酸激活反应,从脱羧的化学步骤到磷酸夹夹环的闭合和三元 E•FEO•HPO₃²⁻复合物的酶构象变化,限速步骤发生了变化。5'-dFO 的 4'-CH₃ 和 OMP 的 4'-CH₂OH 基团分别使未激活的 2 脱羧的过渡态稳定化 2.9 kcal/mol。相比之下,5'-dFO 的 4'-CH₃ 基团和 OMP 的 4'-CH₂OH 基团使亚磷酸激活脱羧的过渡态分别稳定化 4.7 和 8.3 kcal/mol。在这里,5'-dFO 的 4'-CH₃ 取代基的去稳定化效应被限速构象变化所掩盖,该构象变化抑制了亲本底物 FEO 的亚磷酸激活反应的三阶速率常数。