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通过活性位点重新设计优化一种小漆酶。

Optimization of a small laccase by active-site redesign.

机构信息

Department of Protein Diversity, Novozymes A/S, Krogshoejvej 36, 2880 Bagsvaerd, Denmark.

出版信息

Chembiochem. 2013 Jul 8;14(10):1209-11. doi: 10.1002/cbic.201300256. Epub 2013 Jun 14.

DOI:10.1002/cbic.201300256
PMID:23775916
Abstract

Small but faster: A small laccase from Streptomyces coelicolor (SLAC) has been engineered by structure-based design and site-directed mutagenesis to improve the activity on commercially relevant substrates. The variants generated showed up to 40-fold increased efficiency on 2,6-dimethoxyphenol and the ability to use mediators with considerably higher redox potentials (methylsyringate and TEMPO).

摘要

体积小但速度快

通过基于结构的设计和定点突变工程改造，来自链霉菌（Streptomyces coelicolor）的小型漆酶（SLAC）提高了对商业相关底物的活性。所产生的变体在 2,6-二甲氧基苯酚上的效率提高了多达 40 倍，并且能够使用具有更高氧化还原电位的介体（甲基丁香酚和 TEMPO）。

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