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基于结构的大肠杆菌 D-果糖-6-磷酸醛缩酶的重新设计：通过两点突变对受体底物具有显著的活性和选择性。

Structure-guided redesign of D-fructose-6-phosphate aldolase from E. coli: remarkable activity and selectivity towards acceptor substrates by two-point mutation.

机构信息

Instituto de Química Avanzada de Cataluña-CSIC, Jordi Girona 18-26, 08034 Barcelona, Spain.

出版信息

Chem Commun (Camb). 2011 May 28;47(20):5762-4. doi: 10.1039/c1cc11069a. Epub 2011 Apr 18.

DOI:10.1039/c1cc11069a
PMID:21499643
Abstract

Structure-guided re-design of the acceptor binding site of D-fructose-6-phosphate aldolase from E. coli leads to the construction of FSA A129S/A165G double mutant with an activity between 5- to >900-fold higher than that of wild-type towards N-Cbz-aminoaldehyde derivatives.

摘要

结构指导的大肠杆菌 D-果糖-6-磷酸醛缩酶受体结合部位的重新设计导致构建了 FSA A129S/A165G 双突变体，其对 N-Cbz-氨基醛衍生物的活性比野生型高 5 到 >900 倍。

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