De Raffele Daria, Martí Sergio, Moliner Vicent
Departament de Química Física i Analítica, Universitat Jaume I, Castellón 12071, Spain.
Chem Commun (Camb). 2021 May 27;57(43):5306-5309. doi: 10.1039/d1cc01081f.
The retro-aldolase mechanism of methodol catalysed by the catalytic antibody 33F12 is described based on the exploration of the free energy landscape obtained with QM/MM methods. The amino acids involved in the reaction have been identified, as well as their specific role played in the active site and in the flexibility of the loops. Finally, the comparison with a de novo enzyme RA95.5-8F provides a deeper understanding of catalytic differences between such different protein scaffolds.
基于采用量子力学/分子力学（QM/MM）方法获得的自由能面探索，描述了催化抗体33F12催化甲磺酸甲酯的逆羟醛缩合机制。已确定了反应中涉及的氨基酸，以及它们在活性位点和环的柔韧性中所起的特定作用。最后，与从头设计的酶RA95.5-8F进行比较，能更深入地了解此类不同蛋白质支架之间的催化差异。
