TRAINING IN DMX ELECTRONICS & NMR

酵母烯醇化酶-兔肌肉复合体的结构 丙酮酸激酶已被X射线分解到高分辨率 结晶学。这些结构揭示了 这两种酶的活性中心残基。定点突变 已经进行了研究，以澄清活性中心残基在 催化作用。被认为是酸/碱催化剂的残基 因为这些酶是酵母烯醇化酶的赖氨酸345和精氨酸 72或苏氨酸327为丙酮酸激酶。这两种酶都能催化 交替反应。这些化合物产物的核磁共振表征 我们将采取不同的反应，以帮助证实我们的 假设。反应立体专一性的核磁共振鉴定 在这些酶的催化下，也将使用突变体。

The structures of complexes of yeast enolase and rabbit muscle pyruvate kinase have been solved to high resolution by X-ray crystallography. These structures reveal the identities of active-site residues in these two enzymes. Site-directed mutagenesis has been performed to clarify the roles of the active-site residues in catalysis. Residues believed to function as the acid/base catalysts for these enzymes are lysine 345 for yeast enolase and either arginine 72 or threonine 327 for pyruvate kinase. Both enzymes catalyze alternate reactions. NMR characterization of the products of these alternate reactions will be carried to help corroborate our hypotheses. NMR identification of the stereospecificity of reactions catalyzed by these enzymes and mutants will also be employed.