Alteration of enzyme specificity and catalysis by protein engineering.
作者： Helen M. Wilks , J.John Holbrook
DOI: 10.1016/0958-1669(91)90081-F
关键词:
摘要: New substrate specificities can be introduced into existing enzymes for the purpose of making them more suitable chemoenzymic synthesis single compound drugs and other chiral compounds. The most productive route used in past year has involved utilization catalytic substrate-binding properties from homologous found nature, one example being broadening specificity yeast alcohol dehydrogenase. Other highlights include creation thermostable dehydrogenases that will interconvert NADPH NADH, design mutant with improved rates compared their wild-type counterparts.
elsevier.com
sci-hub.se 参考文章(14)
Anthony R. Clarke, Stephen Colebrook, Antonio Cortes, David C. Emery, David J. Halsall, Keith W. Hart, Richard M. Jackson, Helen M. Wilks, J. John Holbrook, Towards the construction of a universal NAD(P)(+)-dependent dehydrogenase: comparative and evolutionary considerations. Biochemical Society Transactions. ,vol. 19, pp. 576- 581 ,(1991) , 10.1042/BST0190576
F. Jacob, B. Joris, O. Dideberg, J. Dusart, J.-M. Ghuysen, J.-M. Frére, Engineering a novel β-Iactamase by a single point mutation Protein Engineering. ,vol. 4, pp. 79- 86 ,(1990) , 10.1093/PROTEIN/4.1.79
M MUTTER, Nature's rules and chemist's tools: a way for creating novel proteins Trends in Biochemical Sciences. ,vol. 13, pp. 260- 265 ,(1988) , 10.1016/0968-0004(88)90159-4
Pierre R. Bonneau, Thomas P. Graycar, David A. Estell, J. Bryan Jones, Alteration of the specificity of subtilisin BPN' by site-directed mutagenesis in its S1 and S1' binding sites Journal of the American Chemical Society. ,vol. 113, pp. 1026- 1030 ,(1991) , 10.1021/JA00003A043
E.H. Creaser, C. Murali, K.A. Britt, Protein engineering of alcohol dehydrogenases: effects of amino acid changes at positions 93 and 48 of yeast ADH1. Protein Engineering. ,vol. 3, pp. 523- 526 ,(1990) , 10.1093/PROTEIN/3.6.523
David A. Jewell, Chingkuang Tu, Shanthi R. Paranawithana, Susan M. Tanhauser, Philip V. LoGrasso, Philip J. Laipis, David N. Silverman, Enhancement of the catalytic properties of human carbonic anhydrase III by site-directed mutagenesis. Biochemistry. ,vol. 30, pp. 1484- 1490 ,(1991) , 10.1021/BI00220A006
H. Wilks, K. Hart, R Feeney, C. Dunn, H Muirhead, W. Chia, D. Barstow, T Atkinson, A. Clarke, J. Holbrook, A specific, highly active malate dehydrogenase by redesign of a lactate dehydrogenase framework. Science. ,vol. 242, pp. 1541- 1544 ,(1988) , 10.1126/SCIENCE.3201242
Chi Huey Wong, S. T. Chen, William J. Hennen, Jeffrey A. Bibbs, Y. F. Wang, Jennifer L. C. Liu, Michael W. Pantoliano, Marc Whitlow, Philip N. Bryan, Enzymes in organic synthesis: use of subtilisin and a highly stable mutant derived from multiple site-specific mutations Journal of the American Chemical Society. ,vol. 112, pp. 945- 953 ,(1990) , 10.1021/JA00159A006
Joseph P. Noel, Tiliang Deng, Kelly J. Hamilton, Ming Daw Tsai, Phospholipase A2 engineering. 3. Replacement of lysine-56 by neutral residues improves catalytic efficiency significantly, alters substrate specificity, and clarifies the mechanism of interfacial recognition Journal of the American Chemical Society. ,vol. 112, pp. 3704- 3706 ,(1990) , 10.1021/JA00165A090
Raymond Feeney, Anthony R. Clarke, J.John Holbrook, A single amino acid substitution in lactate dehydrogenase improves the catalytic efficiency with an alternative coenzyme Biochemical and Biophysical Research Communications. ,vol. 166, pp. 667- 672 ,(1990) , 10.1016/0006-291X(90)90861-G