References
- Albery W.J., Knowles J.R. (1976). Evolution of enzyme function and the development of catalytic efficiency. Biochemistry, 15: 5631–5640.
- Carrillo N., Ceccarelli E.A. (2003). Open questions in ferredoxin-NADP+ reductase catalytic mechanism. European Journal of Biochemistry, 270: 1900–1915.
- Ceccarelli E.A., Carrillo N., Roveri O.A. (2008). Efficiency function for comparing catalytic competence. Trends in Biotechnology, 26: 117–118.
- Cornish-Bowden A. (2002). Fundamentals of Enzyme Kinetics. Portland Press: London.
- Edwards A.W. (2000). The genetical theory of natural selection. Genetics, 154: 1419–1426.
- Eisenthal R., Danson M.J., Hough D.W. (2007). Catalytic efficiency and kcat/KM: a useful comparator? Trends in Biotechnology, 25: 247–249.
- Fersht A. (1999). Structure and Mechanism in Protein Science. A Guide to Enzyme Catalysis and Protein Folding. W.H. Freeman and Co.
- Fox R.J., Clay M.D. (2009). Catalytic effectiveness, a measure of enzyme proficiency for industrial applications. Trends in Biotechnology, 27: 137–140.
- Fox R.J., Huisman G.W. (2008). Enzyme optimization: moving from blind evolution to statistical exploration of sequence-function space. Trends in Biotechnology, 26: 132–138.
- Giver L., Arnold F.H. (1998). Combinatorial protein design by in vitro recombination. Current Opinion in Chemical Biology, 2: 335–338.
- Koshland D.E. (2002). The application and usefulness of the ratio kcat/KM. Bioorganic Chemistry, 30: 211–213.
- Park H.S., Nam S.H., Lee J.K., Yoon C.N., Mannervik B., Benkovic S.J., et al. (2006). Design and evolution of new catalytic activity with an existing protein scaffold. Science, 311: 535–538.
- Piubelli L., Aliverti A., Arakaki A.K., Carrillo N., Ceccarelli E.A., Karplus P.A., et al. (2000). Competition between C-terminal tyrosine and nicotinamide modulates pyridine nucleotide affinity and specificity in plant ferredoxin-NADP(+) reductase. Journal of Biological Chemistry, 275: 10472–10476.
- Pollard D.J., Woodley J.M. (2007). Biocatalysis for pharmaceutical intermediates: the future is now. Trends in Biotechnology, 25: 66–73.
- Robertson M.P., Scott W.G. (2007). Biochemistry: designer enzymes. Nature, 448: 757–758.
- Rubin-Pitel S.B., Zhao H. (2006). Recent advances in biocatalysis by directed enzyme evolution. Combinatorial Chemistry & High Throughput Screening, 9: 247–257.
- Schoemaker H.E., Mink D., Wubbolts M.G. (2003). Dispelling the myths-biocatalysis in industrial synthesis. Science, 299: 1694–1697.
- Stemmer W.P. (1994). Rapid evolution of a protein in vitro by DNA shuffling. Nature, 370: 389–391.
- Stutzman-Engwall K., Conlon S., Fedechko R., Mcarthur H., Pekrun K., Jenne S., et al. (2005). Semi-synthetic DNA shuffling of aveC leads to improved industrial scale production of doramectin by Streptomyces avermitilis. Metabolic Engineering, 7: 27–37.
- Thayer A.M. (2006). Custom Chemicals. Chemical and Engineering News, 84: 1724.
- Wong T.S., Roccatano D., Schwaneberg U. (2007). Steering directed protein evolution: strategies to manage combinatorial complexity of mutant libraries. Environmental Microbiology, 9: 2645–2659.
- Yuan L., Kurek I., English J., Keenan R. (2005). Laboratory-directed protein evolution. Microbiology and Molecular Biology Reviews, 69: 373–392.