Minimalist active-site redesign: teaching old enzymes new tricks.

Minimalist active-site redesign: teaching old enzymes new tricks. Research Abstract Details 

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Minimalist active-site redesign: teaching old enzymes new tricks. Abstract Text:

Miguel D Toscano,Kenneth J Woycechowsky,Donald Hilvert,

Although nature evolves its catalysts over millions of years, enzyme engineers try to do it a bit faster. Enzyme active sites provide highly optimized microenvironments for the catalysis of biologically useful chemical transformations. Consequently, changes at these centers can have large effects on enzyme activity. The prediction and control of these effects provides a promising way to access new functions. The development of methods and strategies to explore the untapped catalytic potential of natural enzyme scaffolds has been pushed by the increasing demand for industrial biocatalysts. This Review describes the use of minimal modifications at enzyme active sites to expand their catalytic repertoires, including targeted mutagenesis and the addition of new reactive functionalities. Often, a novel activity can be obtained with only a single point mutation. The many successful examples of active-site engineering through minimal mutations give useful insights into enzyme evolution and open new avenues in biocatalyst research.

Minimalist active-site redesign: teaching old enzymes new tricks. Publishing Authors By Initials

MD Toscano,KJ Woycechowsky,D Hilvert,

For similar enzymes and coenzymes: enzymes: hydrolases: peptide hydrolases: endopeptidases: serine endopeptidases: subtilisins research abstracts see: enzymes and coenzymes: enzymes: hydrolases: peptide hydrolases: endopeptidases: serine endopeptidases: subtilisins research

PUBMED ID PMID:

MEDLINE DATE:

Minimalist active-site redesign: teaching old enzymes new tricks. Journal Published:

PUBLICATION TYPE: Review

Journal: Angewandte Chemie (International ed. in English)

VOLUME: 46

Page Numbers: 3212-36

Journal Abbreviation:

ISSN: 1433-7851

DAY: 3

MONTH: 12

YEAR: 2007

Minimalist active-site redesign: teaching old enzymes new tricks. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 370543

Minimalist active-site redesign: teaching old enzymes new tricks. Keywords Mesh Terms:

KEYWORDS: Subtilisins

MESH TERMS: metabolism

Chemical & Substance for Abstract: Minimalist active-site redesign: teaching old enzymes new tricks. Information

Substance Name: selenosubtilisin

Registry Number: EC 3.4.21.-

Grant and Affiliation Information for Minimalist active-site redesign: teaching old enzymes new tricks.

AFFILIATION: Laboratory of Organic Chemistry, ETH Zürich, Hönggerberg, Switzerland.

Country: Germany

AGENCY: United States NIGMS

GRANT: F32 GM 71126-02

ACRONYM: GM

MEDLINETA: Angew Chem Int Ed Engl

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