Literature DB >> 9667912

Improving hydrolases for organic synthesis.

R J Kazlauskas1, H K Weber.   

Abstract

Improving hydrolases by site-directed mutagenesis continues to be important, but an alternative method - directed evolution - also gains favor. Directed evolution combines random mutagenesis with screening or selection for the desired property. Directed evolution is especially useful for cases like solvent tolerance or thermostability where current theories are inadequate to predict which structural changes will give improvement. Researchers have also recently made significant progress on several practical problems: how to maintain the high activity of proteases and lipases in nonpolar organic solvents, how to resolve amines, and how to efficiently recycle the unwanted enantiomer in kinetic resolutions. Besides the lipases and proteases, researchers are also developing new hydrolases, notably dehalogenases and epoxide hydrolases.

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Year:  1998        PMID: 9667912     DOI: 10.1016/s1367-5931(98)80043-4

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


  3 in total

1.  Computational design of a lipase for catalysis of the Diels-Alder reaction.

Authors:  Mats Linder; Anders Hermansson; John Liebeschuetz; Tore Brinck
Journal:  J Mol Model       Date:  2010-06-24       Impact factor: 1.810

2.  Facile fabrication of a recyclable nanobiocatalyst: immobilization of Burkholderia cepacia lipase on carbon nanofibers for the kinetic resolution of a racemic atenolol intermediate.

Authors:  Surbhi Soni; Bharat Prasad Dwivedee; Uttam Chand Banerjee
Journal:  RSC Adv       Date:  2018-08-03       Impact factor: 4.036

3.  Modeling of solvent-dependent conformational transitions in Burkholderia cepacia lipase.

Authors:  Peter Trodler; Rolf D Schmid; Jürgen Pleiss
Journal:  BMC Struct Biol       Date:  2009-05-28
  3 in total

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