STRUCTURE STABILITY IN THE ENOLASE SUPERFAMILY CATALYTIC MODULE

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 在烯醇化酶超家族中，一组保守的活性位点残基（“催化模块”）在自然界中反复用于许多不同酶的进化中，用于进行涉及化学多样性底物组的独特整体反应。虽然活性位点残基的这些高能构象经常通过静电或空间排斥使酶的全局稳定性不稳定，但几项研究的结果表明，这种相互作用是酶催化的基本要素，这表明了功能的稳定性权衡。邻琥珀酰苯甲酸合酶（OSBS）突变体的结构解决方案和改进表明，在催化模块（E190）中最保守的残基是最不稳定的，确认存在的稳定性功能权衡。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. In the enolase superfamily, a set of conserved active site residues (the "catalytic module") has repeatedly been used in nature in the evolution of many different enzymes for the performance of unique overall reactions involving a chemically diverse set of substrates. While these high-energy conformations of active site residues often destabilize the global stability of the enzyme through electrostatic or steric repulsion, results from several investigations have shown that this interplay is an essential element of enzyme catalysis, suggesting a stability trade-off for functionality. Structure solution and refinement of the o-succinylbenzoate synthase (OSBS) mutants show that the most conserved residues in the catalytic module (E190) is the most destabilizing, confirming the existence of the stability-functionality trade-off.