Literature DB >> 11738181

Enzyme design by chemical modification of protein scaffolds.

C M Tann1, D Qi, M D Distefano.   

Abstract

Covalent modification methods allow an almost unlimited range of functionality to be introduced into proteins. In concert with genetic techniques, chemical strategies have had significant impact in the field of enzyme design. Major recent developments include introducing catalytic activity into inactive proteins, modifying the selectivity and/or reactivity of existing enzymes and designing novel enzyme-based biosensors. New chemical methods promise to further increase the range of functionality that can be incorporated into proteins. These results suggest that semi-synthetic methods will play a key role in the development of future biocatalysts.

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Year:  2001        PMID: 11738181     DOI: 10.1016/s1367-5931(01)00268-x

Source DB:  PubMed          Journal:  Curr Opin Chem Biol        ISSN: 1367-5931            Impact factor:   8.822


  5 in total

1.  Artificial metalloenzymes based on biotin-avidin technology for the enantioselective reduction of ketones by transfer hydrogenation.

Authors:  Christophe Letondor; Nicolas Humbert; Thomas R Ward
Journal:  Proc Natl Acad Sci U S A       Date:  2005-03-16       Impact factor: 11.205

2.  Covalent Anchor Positions Play an Important Role in Tuning Catalytic Properties of a Rationally Designed MnSalen-containing Metalloenzyme.

Authors:  Dewain K Garner; Lei Liang; David A Barrios; Jun-Long Zhang; Yi Lu
Journal:  ACS Catal       Date:  2011-09-02       Impact factor: 13.084

3.  Design of a zinc-finger hydrolase with a synthetic αββ protein.

Authors:  Kinshuk Raj Srivastava; Susheel Durani
Journal:  PLoS One       Date:  2014-05-09       Impact factor: 3.240

4.  Orthogonal site-specific protein modification by engineering reversible thiol protection mechanisms.

Authors:  J Jefferson Smith; David W Conrad; Matthew J Cuneo; Homme W Hellinga
Journal:  Protein Sci       Date:  2004-12-02       Impact factor: 6.725

5.  The NMR structure of a stable and compact all-beta-sheet variant of intestinal fatty acid-binding protein.

Authors:  Benhur Ogbay; Gregory T Dekoster; David P Cistola
Journal:  Protein Sci       Date:  2004-05       Impact factor: 6.725

  5 in total

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