CATALYTIC MECHANISM OF MANDELATE RACEMASE & OTHER MANDELATE ENZYMES

扁桃酸消旋酶的催化机理

• 批准号: 6308815
• 负责人: GEORGE L KENYON
• 金额: $ 0.99万
• 依托单位: UNIVERSITY OF CALIFORNIA, SAN FRANCISCO
• 依托单位国家: 美国
• 财政年份: 2000
• 资助国家: 美国
• 起止时间: 2000-03-01 至 2002-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6308815
• 关键词: biological products; biomedical resource; enzymes; spectrometry; structural biology

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.

扁桃酸消旋酶催化两者的相互转化 扁桃酸的对映异构体。 了解这一机制 酶可以进一步了解其他酶，介导 从碳中提取质子。 我们在合成对映体 α-苯基缩水甘油酸钾作为扁桃酸的亲和标记 消旋酶 我们也在合成 α-苯基缩水甘油酸酯和相应的二醇。 此外，我们计划 找出扁桃酸消旋酶的哪些残基被 α-苯基缩水甘油酸酯。 质谱法将用于鉴定 合成的化合物和精确定位的网站（S）的修改， α-苯基缩水甘油酸酯。 其他酶沿着扁桃酸代谢 将来可能会以类似的方式研究这一途径。 质量 光谱学将在未来的结构/功能中发挥关键作用 问题研究