Directed evolution of biocatalysts

Current Opinion in Chemical Biology

Volumn 3, Issue 1, 1999, Pages 54-59

  Arnold, Frances H ^a   Volkov, Alexander A ^a  

^a California Institute of Technology   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYST; DNA RECOMBINATION; EMULSION; ENZYME SPECIFICITY; ENZYME STABILITY; EVOLUTION; GENE; REVIEW; THERMOSTABILITY;

EID: 0033023419     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1367-5931(99)80010-6     Document Type: Article

References (35)

1. Arnold FH Design by directed evolution. Accounts Chem Res. 31:1998;125-131. This is a short, readable account of directed enzyme evolution, as practiced in one laboratory.
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4. Yano T, Oue S, Kagamiyama H Directed evolution of an aspartate aminotransferase with new substrate specificities. Proc Natl Acad Sci USA. 95:1998;5511-5515. A nice example of the directed evolution of enzyme substrate specificity; a rational design approach to this had previously failed.
5. Liu DR, Magliery TJ, Pastrnak M, Schultz PG Engineering a tRNA and aminoacyl-tRNA synthetase for the site-specific incorporation of unnatural amino acids into proteins in vivo. Proc Natl Acad Sci USA. 94:1997;10092-10097.
6. Kumamaru T, Suenaga H, Mitsuoka M, Watanabe T, Furukawa K Enhanced degradation of polychlorinated biphenyls by directed evolution of biphenyl dioxygenase. Nat Biotechnol. 16:1998;663-666. Shuffling of two highly similiar biphenyl dioxygenase genes created variants with altered substrate specificities and a novel degradation activity.
7. Van Kampen MD, Dekker N, Egmond MR, Verheij HM Substrate specificity of Staphylococcus hyicus lipase and Staphylococcus aureus lipase as studied by in vivo chimeragenesis. Biochemistry. 37:1998;3459-3466.
8. Crameri A, Raillard SA, Bermudez E, Stemmer WP DNA shuffling of a family of genes from diverse species accelerates directed evolution. Nature. 391:1998;288-291. A novel approach to exploit the sequence diversity existing in families of homologous proteins for directed evolution. In vitro shuffling of four related cephalosporinase genes and selection for resistance to a drug is shown to generate a chimera with significantly higher activity towards that drug.
9. Reetz MT, Zonta A, Schimossek K, Liebeton K, Jaeger KE Creation of enantioselective biocatalysts for organic chemistry by in vitro evolution. Angew Chem Int Ed Engl. 36:1997;2830-2832. Lipase enantioselectivity was improved significantly during a few cycles of error-prone PCR and screening of the pure substrate enantiomers.
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11. Zhao H, Arnold FH Directed evolution converts subtilisin E into a functional equivalent of thermitase. Protein Eng. 12:1999;47-52. Several generations of PCR mutagenesis and staggered extention process recombination with screening created a highly stable, highly active subtilisin E variant. Eight amino acid substitutions create the variant, which is equivalent to the thermophilic homolog thermitase. The naturally occuring mesophilic and thermophilic enzymes differ at 157 amino acids.
12. Giver L, Gershenson A, Freskgard PO, Arnold FH Laboratory evolution of a thermostable enzyme. Proc Natl Acad Sci USA. 95:1998;12809-12813. Directed evolution was applied to simultaneously improve enzyme activity at low temperatures and improve thermostability, demonstrating that these two properties are not mutually exclusive.
13. Akanuma S, Yamagishi A, Tanaka N, Oshima T Serial increase in the thermal stability of 3-isopropylmalate dehydrogenase from Bacillus subtilis by experimental evolution. Protein Sci. 7:1998;698-705. Expression and selection in a thermophilic host was used to obtain a substantial increase in the thermostability of a mesophilic enzyme. This approach, while powerful, is not generally applicable to stabilization of a wide range of proteins.
14. Proba K, Worn A, Honegger A, Pluckthun A Antibody scFv fragments without disulfide bonds made by molecular evolution. J Mol Biol. 275:1998;245-253. Directed evolution was applied to protein folding and stability. Mutations were obtained that compensate for disulfide bonds and allow the protein to be expressed in E. coli.
15. Martineau P, Jones P, Winter G Expression of an antibody fragment at high levels in the bacterial cytoplasm. J Mol Biol. 280:1998;117-127. This paper describes a nice selection linking correct folding of an antibody fragment to cell survival, which yielded improved folding and expression of a disulfide-containing protein in the reducing environment of the cytoplasm of E. coli.
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23. Arnold FH When blind is better: protein design by evolution (Commentary). Nat Biotechnol. 16:1998;617-618.
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35. Stemmer, WPC: Methods for in vitro recombination. 25 February 1997; US5605793.