Title:

Glutathione Transferases and Serine Proteases: From Probing Mechanism of Enzyme Catalysis by Rational Protein Engineering to Evolutionary Design of Enzyme Function

Subtitle:

Glutathione Transferases and Serine Proteases: From Probing Mechanism of Enzyme Catalysis by Rational Protein Engineering to Evolutionary Design of Enzyme Function

Creator:

Sroga, Grażyna E.

Publisher:

Committee on Biotechnology PAS ; Institute of Bioorganic Chemistry PAS

Date issued/created:

2002

Subject and Keywords:

biotechnology

Abstract:

Research of the past decade has demonstrated that the use of enzymes andwhole-cell biocatalysts is environmentally friendly, economical and surprisingly,faces few barriers when applied in organic syntheses. In nature, enzymesevolved to function within a living system and may not exhibit features desirable for large-scale in vitro syntheses. Thus, protein engineering has the potential to dramatically enhance enzyme performance in a wide variety of unusual -but technologically important - environments. Site-directed, cassette-mutagenesis and construction of chimeric enzymes commonly used in rational protein engineering are important strategies which reveal the structure-functionrelationship of a given enzyme. Notably, construction of hybrid enzymes has become increasingly important in the rational design of novel biocatalysts withdesired properties and activities. However, “irrational” protein design based onrandom mutagenesis technologies or the combination with directed evolutionapproaches has truly revolutionized the generation offunctional biological molecules.

Relation:

Biotechnologia, vol.58, 3 (2002)-.

Volume:

58

Issue:

3

Start page:

53

End page:

60

Resource type:

Text

Detailed Resource Type:

Article

Format:

application/pdf

Resource Identifier:

0860-7796 ; IChB B-54

Source:

Library of Institute of Bioorganic Chemistry PAS

Language:

pol

Language of abstract:

eng

Temporal coverage:

1988-2010

Rights:

Creative Commons Attribution BY-SA 4.0 license

Terms of use:

Copyright-protected material. [CC BY-SA 4.0] May be used within the scope specified in Creative Commons Attribution BY-SA 4.0 license, full text available at:

Digitizing institution:

Institute of Bioorganic Chemistry of the Polish Academy of Science

Original in:

Institute of Bioorganic Chemistry of the Polish Academy of Science

Projects co-financed by:

Operational Program Digital Poland, 2014-2020, Measure 2.3: Digital accessibility and usefulness of public sector information; funds from the European Regional Development Fund and national co-financing from the state budget.

Access:

Open