Efficient Catalytic Promiscuity for Chemically Distinct Reactions

被引:43
作者
Babtie, Ann C. [1 ]
Bandyopadhyay, Subhajit [1 ]
Olguin, Luis F. [1 ]
Hollfelder, Florian [1 ]
机构
[1] Univ Cambridge, Dept Biochem, Cambridge CB2 1GA, England
基金
英国工程与自然科学研究理事会; 英国生物技术与生命科学研究理事会;
关键词
catalytic promiscuity; enzyme catalysis; hydrolases; phosphatases; sulfatases; COLI ALKALINE-PHOSPHATASE; PSEUDOMONAS-AERUGINOSA; TRANSITION-STATE; PHOSPHODIESTERASE ACTIVITY; ENZYME PROMISCUITY; SULFATASE ACTIVITY; HYDROLYSIS; EVOLUTION; ARYLSULFATASE; REACTIVITY;
D O I
10.1002/anie.200805843
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
High catalytic proficiencies observed for the native and promiscuous reaction of the Pseudomonas aeruginosa arylsulfatase (PAS; the picture shows transition states of the two substrates with corresponding binding constants Ktx) suggest that the trade-off between high activity and tight specificity can be substantially relaxed. © 2009 Wiley-VCH Verlag GmbH & Co. KGaA.
引用
收藏
页码:3692 / 3694
页数:3
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