Control over Enzymatic Activity by DNA-Directed Split Enzyme Reassembly

被引：16

作者：

Oltra, Nuria Sancho ^{[1
]}

Bos, Jeffrey ^{[1
]}

Roelfes, Gerard ^{[1
]}

机构：

[1] Univ Groningen, Stratingh Inst Chem, NL-9747 AG Groningen, Netherlands

来源：

CHEMBIOCHEM | 2010年 / 11卷 / 16期

关键词：

allosterism; DNA; enzyme catalysis; protein-DNA conjugates; split enzymes; PROTEIN-PROTEIN INTERACTIONS; DIHYDROFOLATE-REDUCTASE; FRAGMENT COMPLEMENTATION; ALLOSTERIC REGULATION; SIGNAL AMPLIFICATION; FLUORESCENT PROTEIN; IN-VIVO; SENSORS; CATALYSIS; DNAZYME;

D O I：

10.1002/cbic.201000517

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A novel and versatile approach toward DNA-controlled enzymatic activity is presented. The approach was based on the DNA-conjugated split enzyme, murine dihydrofolate reductase (mDHFR), which can be reassembled into a catalytically active conformation by hybridization of the protein fragment conjugated oligonucleotides with a DNA template strand. Copyright © 2010 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

引用

页码：2255 / 2258

页数：4

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