CATALYTIC MECHANISM OF MANDELATE RACEMASE & OTHER MANDELATE ENZYMES

芒果酸外消旋酶催化这两者的相互转化 芒地酸的对映体。了解这一现象的机制 酶可能会加深对其他酶的理解 从碳中提取质子。我们正在合成对映体 α-苯基缩水甘油酸钾作为扁桃酸酯亲和标记物的研究 消旋酶。我们还在合成这些化合物的甲酯 A-苯基缩水甘油酸酯和相应的二元醇。此外，我们计划 找出芒果酸外消旋酶的哪些残基被修饰 A-苯基缩水甘油酸酯。将使用质谱学来鉴定 人工合成化合物并精确定位修饰部位(S) A-苯基缩水甘油酸酯。扁桃体代谢的其他酶 这条途径未来可能会以类似的方式进行研究。质量 光谱学将在未来的结构/功能中发挥关键作用 学习。

Mandelate racemase catalyzes the interconversion of the two enantiomers of mendelic acid. Understanding the mechanism of this enzyme may further the understanding of other enzymes that mediate proton abstraction from carbon. We are synthesizing the enantiomers of potassium a-phenylglycidate as an affinity label for Mandelate racemase. We are also synthesizing the methyl esters of the a-phenylglycidate and the corresponding diol. Further, we plan to find out which residues of Mandelate racemase are modified by a-phenylglycidate. Mass spectrometry will be used to identify the synthesized compounds and pinpoint the site(s) of modification by a-phenylglycidate. Other enzymes along the mandelate metabolic pathway may in the future be studied in similar fashion. Mass spectrometry will play a key role for future structure/function studies.