Engineering aldolases as biocatalysts.
Engineering aldolases as biocatalysts.
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DOI：
10.1016/j.cbpa.2013.12.010
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发表时间：
2014-04
影响因子：
7.8
通讯作者：
Berry, Alan
中科院分区：
文献类型：
--
作者：
Windle, Claire L.;Mueller, Marion;Nelson, Adam;Berry, Alan
醛缩酶是一种很有吸引力的生物催化剂。醛缩酶的稳定性、立体选择性和底物特异性已被改变。具有所需活性的醛缩酶已经使用多种方法产生。结合计算与其他方法产生高效的设计师醛缩酶。由于其形成碳-碳键的能力，醛缩酶被视为生产生物学上重要化合物的有吸引力的途径。然而，对于许多工业反应，没有天然存在的酶，因此许多不同的工程方法已被用于解决这个问题。工程方法已被用于改变醛缩酶的稳定性、底物特异性和立体特异性，以产生用于生物催化过程的优异的酶。最近，对醛缩酶机制的更深入理解使得合理的工程方法和醛缩酶的计算设计都取得了许多成功。合理的工程方法已经快速有效地产生了所需的酶，而计算设计与实验室方法的结合已经产生了活性接近天然酶的酶。
Aldolase enzymes are attractive candidates as biocatalysts. Stability, stereoselectivity and substrate specificity of aldolases have been altered. Aldolases with desirable activities have been produced using a variety of methods. Combining computational with other methods produces efficient designer aldolases. Aldolases are seen as an attractive route to the production of biologically important compounds due to their ability to form carbon–carbon bonds. However, for many industrial reactions there are no naturally occurring enzymes, and so many different engineering approaches have been used to address this problem. Engineering methods have been used to alter the stability, substrate specificity and stereospecificity of aldolases to produce excellent enzymes for biocatalytic processes. Recently greater understanding of the aldolase mechanism has allowed many successes with both rational engineering approaches and computational design of aldolases. Rational engineering approaches have produced desired enzymes quickly and efficiently while combination of computational design with laboratory methods has created enzymes with activity approaching that of natural enzymes.
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