Protein engineering of microbial enzymes

被引:96
作者
Boettcher, Dominique [1 ]
Bornscheuer, Uwe T. [1 ]
机构
[1] Ernst Moritz Arndt Univ Greifswald, Inst Biochem, Dept Biotechnol & Enzyme Catalysis, D-17487 Greifswald, Germany
关键词
ANTARCTICA LIPASE-B; AMINO ACID AMIDOHYDROLASE; DIRECTED EVOLUTION; TERTIARY ALCOHOLS; SUBSTRATE-SPECIFICITY; HYDROXYNITRILE LYASE; STRUCTURAL INTEGRITY; KINETIC RESOLUTION; ESCHERICHIA-COLI; ENANTIOSELECTIVITY;
D O I
10.1016/j.mib.2010.01.010
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Protein engineering has emerged as an important tool to overcome the limitations of natural enzymes as biocatalysts. Recent advances have mainly focused on applying directed evolution to enzymes, especially important for organic synthesis, such as monooxygenases, ketoreductases, lipases or aldolases in order to improve their activity, enantioselectivity, and stability. The combination of directed evolution and rational protein design using computational tools is becoming increasingly important in order to explore enzyme sequence-space and to create improved or novel enzymes. These developments should allow to further expand the application of microbial enzymes in industry.
引用
收藏
页码:274 / 282
页数:9
相关论文
共 79 条
[1]   The 'evolvability' of promiscuous protein functions [J].
Aharoni, A ;
Gaidukov, L ;
Khersonsky, O ;
Gould, SM ;
Roodveldt, C ;
Tawfik, DS .
NATURE GENETICS, 2005, 37 (01) :73-76
[2]   One biocatalyst - Many applications: The use of Candida antarctica B-lipase in organic synthesis [J].
Anderson, EM ;
Karin, M ;
Kirk, O .
BIOCATALYSIS AND BIOTRANSFORMATION, 1998, 16 (03) :181-204
[3]   Complete inversion of enantioselectivity towards acetylated tertiary alcohols by a double mutant of a Bacillus subtilis esterase [J].
Bartsch, Sebastian ;
Kourist, Robert ;
Bornscheuer, Uwe T. .
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 2008, 47 (08) :1508-1511
[4]   Directed evolution of aldolases for exploitation in synthetic organic chemistry [J].
Bolt, Amanda ;
Berry, Alan ;
Nelson, Adam .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 2008, 474 (02) :318-330
[5]   Catalytic promiscuity in biocatalysis: Using old enzymes to form new bonds and follow new pathways [J].
Bornscheuer, UT ;
Kazlauskas, RJ .
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 2004, 43 (45) :6032-6040
[6]   Carbon-carbon coupling in biotransformation [J].
Breuer, M ;
Hauer, B .
CURRENT OPINION IN BIOTECHNOLOGY, 2003, 14 (06) :570-576
[7]   Industrial methods for the production of optically active intermediates [J].
Breuer, M ;
Ditrich, K ;
Habicher, T ;
Hauer, B ;
Kesseler, M ;
Stürmer, R ;
Zelinski, T .
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 2004, 43 (07) :788-824
[8]   Substrate specificity of mutants of the hydroxynitrile lyase from Manihot esculenta [J].
Bühler, H ;
Effenberger, F ;
Förster, S ;
Roos, J ;
Wajant, H .
CHEMBIOCHEM, 2003, 4 (2-3) :211-216
[9]   Morphing Activity between Structurally Similar Enzymes: From Heme-Free Bromoperoxidase to Lipase [J].
Chen, Bo ;
Cai, Zhen ;
Wu, Wei ;
Huang, Yunlong ;
Pleiss, Juergen ;
Lin, Zhanglin .
BIOCHEMISTRY, 2009, 48 (48) :11496-11504
[10]   Redesigning the substrate specificity of ω-aminotransferase for the kinetic resolution of aliphatic chiral arnines [J].
Cho, Byung-Kwan ;
Park, Hyung-Yeon ;
Seo, Joo-Hyun ;
Kim, Juhan ;
Kang, Taek-Jin ;
Lee, Bon-Su ;
Kim, Byung-Gee .
BIOTECHNOLOGY AND BIOENGINEERING, 2008, 99 (02) :275-284