Dreyer M K, Schulz G E
Institut für Organische Chemie und Biochemie, Albert-Ludwigs-Universität, Freiburg im Breisgau, Germany.
J Mol Biol. 1996 Jun 14;259(3):458-66. doi: 10.1006/jmbi.1996.0332.
The structure of L-fuculose-1-phosphate aldolase in a cubic crystal form has been determined with and without the inhibitor phosphoglycolohydroxamate at 2.4 and 2.7 angstrom (1 angstrom = 0.1 nm) resolution, respectively. This inhibitor mimics the enediolate transition state of the substrate moiety dihydroxyacetone phosphate. The structures showed that dihydroxyacetone phosphate ligates the zinc ion of this metal-dependent class II aldolase with its hydroxyl and keto oxygen atoms, shifting Glu73 away from the zinc coordination sphere to a non-polar environment. At this position Glu73 accepts a proton in the initial reaction step, producing the enediolate which is then stabilized by the zinc ion. The other substrate moiety L-lactaldehyde was modeled, because no binding structure is yet available.
已分别在2.4埃和2.7埃（1埃 = 0.1纳米）分辨率下测定了立方晶型的L-岩藻糖-1-磷酸醛缩酶在有和没有抑制剂磷酸甘氨羟肟酸情况下的结构。该抑制剂模拟底物部分磷酸二羟丙酮的烯二醇中间体过渡态。结构显示，磷酸二羟丙酮通过其羟基和酮基氧原子与这种金属依赖性II类醛缩酶的锌离子结合，使Glu73从锌配位球移至非极性环境。在这个位置，Glu73在初始反应步骤中接受一个质子，生成烯二醇中间体，然后由锌离子使其稳定。对另一个底物部分L-乳醛进行了建模，因为尚无结合结构。
