Livesay Dennis R, Jambeck Per, Rojnuckarin Atipat, Subramaniam Shankar
Department of Chemistry, University of Illinois, Urbana, Illinois 61820, USA.
Biochemistry. 2003 Apr 1;42(12):3464-73. doi: 10.1021/bi026918f.
Electrostatic interactions play a key role in enzyme catalytic function. At long range, electrostatics steer the incoming ligand/substrate to the active site, and at short distances, electrostatics provide the specific local interactions for catalysis. In cases in which electrostatics determine enzyme function, orthologs should share the electrostatic properties to maintain function. Often, electrostatic potential maps are employed to depict how conserved surface electrostatics preserve function. We expand on previous efforts to explain conservation of function, using novel electrostatic sequence and structure analyses of four enzyme families and one enzyme superfamily. We show that the spatial charge distribution is conserved within each family and superfamily. Conversely, phylogenetic analysis of key electrostatic residues provide the evolutionary origins of functionality.
静电相互作用在酶的催化功能中起着关键作用。在远距离时，静电作用将进入的配体/底物导向活性位点；在近距离时，静电作用为催化提供特定的局部相互作用。在静电作用决定酶功能的情况下，直系同源物应共享静电特性以维持功能。通常，静电势图被用于描绘保守的表面静电如何维持功能。我们通过对四个酶家族和一个酶超家族进行新颖的静电序列和结构分析，扩展了之前对功能保守性的解释。我们表明，每个家族和超家族内的空间电荷分布是保守的。相反，对关键静电残基的系统发育分析揭示了功能的进化起源。
