Fluorescent Mechanism-Based Probe for Aerobic Flavin-Dependent Enzyme Activity.

Fluorescent Mechanism-Based Probe for Aerobic Flavin-Dependent Enzyme Activity.
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DOI:
10.1002/cbic.201600275
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发表时间:
2016-09-02
期刊:
Chembiochem : a European journal of chemical biology
影响因子:
--
通讯作者:
Burkart MD
Burkart MD
中科院分区:
其他
文献类型:
--
作者:
McCulloch IP;La Clair JJ;Jaremko MJ;Burkart MD

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Diversity in non-ribosomal peptide and polyketide secondary metabolism is facilitated by interaction between biosynthetic domains with discrete monomer loading and their cognate tailoring enzymes, such as oxidation or halogenation enzymes. The cooperation between peptidyl carrier proteins and flavin-dependent enzymes offers a specialized strategy for monomer selectivity, which oxidizes small molecules from within a complex cellular milieu. In an effort to study this process, we have developed fluorescent probes to selectively label aerobic flavin-dependent enzymes. Here we report the preparation and implementation of these tools to label oxidase, monooxygenase and halogenase flavin-dependent enzymes. Domain specific probes offer a vital tool to identify and characterize biosynthetic enzymes. We now report on the development of tools to label oxidase, monooxygenase and halogenase flavin-dependent enzymes.
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