Tailoring new enzyme functions by rational redesign

被引:85
作者
Cedrone, F
Ménez, A
Quéméneur, E
机构
[1] Ctr Etud Saclay, CEA, Dept Ingn & Etud Prot, F-91191 Gif Sur Yvette, France
[2] CEA, Dept Ingn & Etud Prot, SBTN, DE Valrho, F-30207 Bagnols Sur Ceze, France
关键词
D O I
10.1016/S0959-440X(00)00106-8
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
Site-directed mutagenesis is still a very efficient strategy to elaborate improved enzymes. Recently, advances have been made in developing rational strategies aimed at reshaping enzyme specificities and mechanisms, and at engineering biocatalysts through molecular assembling. These knowledge-based studies greatly benefit from the most recent computational analyses of enzyme structures and functions. The combination of rational and combinatorial methods opens up new vistas in the design of stable and efficient enzymes.
引用
收藏
页码:405 / 410
页数:6
相关论文
共 59 条
[1]   RETRACTED: Directed evolution of new catalytic activity using the α/β-barrel scaffold (Retracted article. See vol 417, pg 468, 2002) [J].
Altamirano, MM ;
Blackburn, JM ;
Aguayo, C ;
Fersht, AR .
NATURE, 2000, 403 (6770) :617-622
[2]   Directed evolution of biocatalysts [J].
Arnold, FH ;
Volkov, AA .
CURRENT OPINION IN CHEMICAL BIOLOGY, 1999, 3 (01) :54-59
[3]   Understanding enzyme superfamilies - Chemistry as the fundamental determinant in the evolution of new catalytic activities [J].
Babbitt, PC ;
Gerlt, JA .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (49) :30591-30594
[4]   Hybrid enzymes [J].
Béguin, P .
CURRENT OPINION IN BIOTECHNOLOGY, 1999, 10 (04) :336-340
[5]   Catalytic activity of the N-terminal domain of Escherichia coli asparagine synthetase B can be reengineered by single-point mutation [J].
Boehlein, SK ;
RosaRodriguez, JG ;
Schuster, SM ;
Richards, NGJ .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1997, 119 (25) :5785-5791
[6]   The effects of an engineered cation site on the structure, activity, and EPR properties of cytochrome c peroxidase [J].
Bonagura, CA ;
Sundaramoorthy, M ;
Bhaskar, B ;
Poulos, TL .
BIOCHEMISTRY, 1999, 38 (17) :5538-5545
[7]   Conversion of an engineered potassium-binding site into a calcium-selective site in cytochrome c peroxidase [J].
Bonagura, CA ;
Bhaskar, B ;
Sundaramoorthy, M ;
Poulos, TL .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (53) :37827-37833
[8]   Catalytic plasticity of fatty acid modification enzymes underlying chemical diversity of plant lipids [J].
Broun, P ;
Shanklin, J ;
Whittle, E ;
Somerville, C .
SCIENCE, 1998, 282 (5392) :1315-1317
[9]   Redesign of soluble fatty acid desaturases from plants for altered substrate specificity and double bond position [J].
Cahoon, EB ;
Lindqvist, Y ;
Schneider, G ;
Shanklin, J .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1997, 94 (10) :4872-4877
[10]   Chimeric restriction enzymes: What is next? [J].
Chandrasegaran, S ;
Smith, J .
BIOLOGICAL CHEMISTRY, 1999, 380 (7-8) :841-848