Efficient Catalytic Promiscuity for Chemically Distinct Reactions

被引：44

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

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2009年 / 48卷 / 20期

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

页码：3692 / 3694

页数：3

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