The Molecular Anatomy of an Ancient Adaptive Event

American Scientist

Volumn 86, Issue 1, 1998, Pages 26-37

  Dean, Antony M ^a,b,c  

^a ROSALIND FRANKLIN UNIVERSITY OF MEDICINE AND SCIENCE   (United States)

^b WASHINGTON UNIVERSITY   (United States)

^c FUHS/CMS   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 0002682171     PISSN: 00030996     EISSN: None     Source Type: Trade Journal    
DOI: 10.1511/1998.1.26     Document Type: Article

References (10)

1. Chen, R, A. Greer and A. M. Dean. 1995. A highly active decarboxylating dehydrogenase with rationally inverted coenzyme specificity. Proceedings of the National Academy of Sciences 92:11666-11670.
2. Chen, R., A. Greer and A. M. Dean. 1966. Redesigning secondary structure to invert coenzyme specificity in isopropylmalate dehydrogenase. Proceedings of the National Academy of Sciences 93:12171-12176.
3. Dean, A. M., and G. B. Golding. 1997. Protein engineering reveals ancient adaptive replacements in isocitrate dehydrogenase. Proceedings of the National Academy of Sciences 94:3104-3109.
4. Golding, G. B. 1994. Non-Neutral Evolution: Theories and Molecular Data. New York: Chapman and Hall Inc.
5. + specificity-reversal murtant. Biochemistry 35:5670-5678.
6. Kimura, M. 1983. The Neutral Theory of Molecular Evolution. Cambridge, England: The Cambridge University Press.
7. Li, W.-H. 1997. Molecular Evolution. Sunderland, MA: Sinauer Associates, Inc.
8. Stoddard, B. L., A. M. Dean and P. A. Bash. 1996. Combining Laue diffraction and molecular dynamics to study enzyme intermediates: formation of a Michaelis complex. Nature Structural Biology 3:590-595.
9. Walsh, K., and D. E. Koshland, Jr. 1985. Branch point control by the phosphorylation state of isocitrate dehydrogenase. Journal of Biological Chemistry 260:8430-8437.
10. Wilks, H. M., K. W. Hart, R. Feeney, C. R. Dunn, H. Muirhead, W. N. Chia, D. A. Barstow, T. Atkinson, A. R. Clarke and J. J. Holbrook. 1988. A specific, highly active malate dehydrogenase by redesign of a lactate dehydrogenase framework. Science 242:1541-1544.