COMPUTATIONAL TOOLS FOR RATIONAL PROTEIN ENGINEERING OF ALDOLASES

被引:5
作者
Widmann, Michael [1 ]
Pleiss, Juergen [1 ]
Samland, Anne K. [2 ]
机构
[1] Univ Stuttgart, Inst Tech Biochem, D-70569 Stuttgart, Germany
[2] Univ Stuttgart, Inst Microbiol, Allmandring 31, D-70569 Stuttgart, Germany
来源
COMPUTATIONAL AND STRUCTURAL BIOTECHNOLOGY JOURNAL | 2012年 / 2卷 / 03期
关键词
protein engineering; substrate specificity; stereoselectivity; de novo design; transaldolase; biocatalysis;
D O I
10.5936/csbj.201209016
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
In this mini-review we describe the different strategies for rational protein engineering and summarize the computational tools available. Computational tools can either be used to design focused libraries, to predict sequence-function relationships or for structure-based molecular modelling. This also includes de novo design of enzymes. Examples for protein engineering of aldolases and transaldolases are given in the second part of the mini-review.
引用
收藏
页数:11
相关论文
共 105 条
  • [31] Rational engineering of enzyme stability
    Eijsink, VGH
    Bjork, A
    Gåseidnes, S
    Sirevåg, R
    Synstad, B
    van den Burg, B
    Vriend, G
    [J]. JOURNAL OF BIOTECHNOLOGY, 2004, 113 (1-3) : 105 - 120
  • [32] The Lipase Engineering Database: a navigation and analysis tool for protein families
    Fischer, M
    Pleiss, J
    [J]. NUCLEIC ACIDS RESEARCH, 2003, 31 (01) : 319 - 321
  • [33] DWARF - a data warehouse system for analyzing protein families
    Fischer, Markus
    Thai, Quan K.
    Grieb, Melanie
    Pleiss, Jurgen
    [J]. BMC BIOINFORMATICS, 2006, 7 (1)
  • [34] Influence of conservation on calculations of amino acid covariance in multiple sequence alignments
    Fodor, AA
    Aldrich, RW
    [J]. PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 2004, 56 (02) : 211 - 221
  • [35] Improving catalytic function by ProSAR-driven enzyme evolution
    Fox, Richard J.
    Davis, S. Christopher
    Mundorff, Emily C.
    Newman, Lisa M.
    Gavrilovic, Vesna
    Ma, Steven K.
    Chung, Loleta M.
    Ching, Charlene
    Tam, Sarena
    Muley, Sheela
    Grate, John
    Gruber, John
    Whitman, John C.
    Sheldon, Roger A.
    Huisman, Gjalt W.
    [J]. NATURE BIOTECHNOLOGY, 2007, 25 (03) : 338 - 344
  • [36] Redesign of the Phosphate Binding Site of L-Rhamnulose-1-Phosphate Aldolase towards a Dihydroxyacetone Dependent Aldolase
    Garrabou, Xavier
    Joglar, Jesus
    Parella, Teodor
    Crehuet, Ramon
    Bujons, Jordi
    Clapes, Pere
    [J]. ADVANCED SYNTHESIS & CATALYSIS, 2011, 353 (01) : 89 - 99
  • [37] Evolution of Stability in a Cold-Active Enzyme Elicits Specificity Relaxation and Highlights Substrate-Related Effects on Temperature Adaptation
    Gatti-Lafranconi, Pietro
    Natalello, Antonino
    Rehm, Sascha
    Doglia, Silvia Maria
    Pleiss, Juergen
    Lotti, Marina
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 2010, 395 (01) : 155 - 166
  • [38] Amino-acid interactions in psychrophiles, mesophiles, thermophiles, and hyperthermophiles: Insights from the quasi-chemical approximation
    Goldstein, Richard A.
    [J]. PROTEIN SCIENCE, 2007, 16 (09) : 1887 - 1895
  • [39] A structure-controlled investigation of lipase enantioselectivity by a path-planning approach
    Guieysse, David
    Cortes, Juan
    Puech-Guenot, Sophie
    Barbe, Sophie
    Lafaquiere, Vincent
    Monsan, Pierre
    Simeon, Thierry
    Andre, Isabelle
    Remaud-Simeon, Magali
    [J]. CHEMBIOCHEM, 2008, 9 (08) : 1308 - 1317
  • [40] Correlated mutations: Advances and limitations. A study on fusion proteins and on the cohesin-dockerin families
    Halperin, Inbal
    Wolfson, Haim
    Nussinov, Ruth
    [J]. PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 2006, 63 (04) : 832 - 845