Journal Article10.1016/S0959-440X(03)00101-5
Optimising enzyme function by directed evolution.
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TL;DR: Recent advances in 'smart' library design and computational screening are now permitting much deeper searches of sequence space, which potentially increases the extent to which enzyme function can be modified.
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About: This article is published in Current Opinion in Structural Biology. The article was published on 01 Aug 2003.
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Citations
Semi-rational approaches to engineering enzyme activity: combining the benefits of directed evolution and rational design.
TL;DR: Efficient sampling of mutations likely to affect enzyme function has been conducted both experimentally and computationally, with remarkable improvements in substrate selectivity and specificity and in the de novo design of enzyme activities within scaffolds of known structure.
917
Biocatalysis for pharmaceutical intermediates: the future is now
David Pollard,John M. Woodley +1 more
TL;DR: This review describes how demands are being addressed to make biocatalysis successful, particularly by the use of micro-scale technology for high-speed catalyst screening and process development alongside discipline integration of biology and engineering with chemistry.
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Multi-Enzymatic Cascade Reactions: Overview and Perspectives
TL;DR: This review summarizes the developments in multi-enzymatic cascades employed for the asymmetric synthesis of chiral alcohols, amines and amino acids, as well as for CC bond formation.
489
Synthetic biology for the directed evolution of protein biocatalysts: navigating sequence space intelligently
TL;DR: Improving enzymes by directed evolution requires the navigation of very large search spaces; this work surveys how to do this intelligently.
389
High-throughput screens and selections of enzyme-encoding genes.
TL;DR: This work focuses on HTS approaches that enable selection from large libraries (>10(6) gene variants) with relatively humble means (i.e. non-robotic systems), and on in vitro compartmentalization in particular.
238
References
Rapid evolution of a protein in vitro by DNA shuffling.
TL;DR: It is reported here that selected mutants had a minimum inhibitory concentration of 640 μg ml-1, a 32,000-fold increase and 64-fold greater than any published TEM-1 derived enzyme.
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Expanding the Genetic Code of Escherichia coli
TL;DR: A unique transfer RNA/aminoacyl-tRNA synthetase pair has been generated that expands the number of genetically encoded amino acids in Escherichia coli and should provide a general method for increasing the genetic repertoire of living cells to include a variety of amino acids with novel structural, chemical, and physical properties not found in the common 20 amino acids.
Molecular evolution by staggered extension process (StEP) in vitro recombination
TL;DR: The staggered extension process (StEP) consists of priming the template sequence(s) followed by repeated cycles of denaturation and extremely abbreviated annealing/polymerase-catalyzed extension, which results in recombination of polynu-cleotide sequences.
984
A proficient enzyme
Anna Radzicka,Richard Wolfenden +1 more
TL;DR: Values of the known range of spontaneous rate constants for reactions that are also susceptible to catalysis by enzymes are extended to more than 14 orders of magnitude, in contrast to previous work.
887
Dispelling the myths--biocatalysis in industrial synthesis.
TL;DR: Expect many new industrial applications of biocatalysis to be realized, from single-step enzymatic conversions to customized multistep microbial synthesis by means of metabolic pathway engineering.
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