Computational design gains momentum in enzyme catalysis engineering

被引:41
|
作者
Wijma, Hein J. [1 ]
Janssen, Dick B. [1 ]
机构
[1] Univ Groningen, Dept Biochem, Groningen Biomol Sci & Biotechnol Inst, NL-9747 AG Groningen, Netherlands
关键词
biocatalysis; computer-aided enzyme design; computer-aided protein design; enzymatic activity; insilico design; loop grafting; ranking; stability; substrate scope; substrate specificity; DEAD-END ELIMINATION; BACKBONE PROTEIN DESIGN; SIDE-CHAIN; DIRECTED EVOLUTION; LIGAND-BINDING; HUMAN BUTYRYLCHOLINESTERASE; REDESIGN; SPECIFICITY; VALIDATION; ALGORITHM;
D O I
10.1111/febs.12324
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
Computational protein design is becoming a powerful tool for tailoring enzymes for specific biotechnological applications. When applied to existing enzymes, computational re-design makes it possible to obtain orders of magnitude improvement in catalytic activity towards a new target substrate. Computational methods also allow the design of completely new active sites that catalyze reactions that are not known to occur in biological systems. If initial designs display modest catalytic activity, which is often the case, this may be improved by iterative cycles of computational design or by follow-up engineering through directed evolution. Compared to established protein engineering methods such as directed evolution and structure-based mutagenesis, computational design allows for much larger jumps in sequence space; for example, by introducing more than a dozen mutations in a single step or by introducing loops that provide new functional interactions. Recent advances in the computational design toolbox, which include new backbone re-design methods and the use of molecular dynamics simulations to better predict the catalytic activity of designed variants, will further enhance the use of computational tools in enzyme engineering.
引用
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页码:2948 / 2960
页数:13
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