(Q30960950)

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Use of phage display and transition-state analogs to select enzyme variants with altered catalytic properties: glutathione transferase as an example

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scholarly article

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Europe PubMed Central

27 June 2017

Use of phage display and transition-state analogs to select enzyme variants with altered catalytic properties: glutathione transferase as an example (English)

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Europe PubMed Central

27 June 2017

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author name string

Widersten M

1

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Europe PubMed Central

27 June 2017

Hansson LO

2

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Europe PubMed Central

27 June 2017

Tronstad L

3

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27 June 2017

Mannervik B

4

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27 June 2017

language of work or name

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publication date

1 January 2000

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27 June 2017

Methods in Enzymology

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27 June 2017

328

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27 June 2017

389-404

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Europe PubMed Central

27 June 2017

Structure, catalytic mechanism, and evolution of the glutathione transferases

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Hormone phage: an enrichment method for variant proteins with altered binding properties

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A strategy for the isolation of catalytic activities from repertoires of enzymes displayed on phage 1 1Edited by J. Karn

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Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the Mu and Pi class enzymes

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The immunological evolution of catalysis

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Structural determinants in domain II of human glutathione transferase M2-2 govern the characteristic activities with aminochrome, 2-cyano-1,3-dimethyl-1-nitrosoguanidine, and 1,2-dichloro-4-nitrobenzene

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Glutathione transferases with novel active sites isolated by phage display from a library of random mutants

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Mechanism-based phage display selection of active-site mutants of human glutathione transferase A1-1 catalyzing SNAr reactions

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Contribution of tryptophan residues to the combining site of a monoclonal anti dinitrophenyl spin-label antibody

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Understanding enzyme superfamilies. Chemistry As the fundamental determinant in the evolution of new catalytic activities

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Rapid evolution of a protein in vitro by DNA shuffling

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An approach to optimizing the active site in a glutathione transferase by evolution in vitro

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Glutathione transferases--structure and catalytic activity

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Identifiers

10.1016/S0076-6879(00)28408-5

1 reference

Europe PubMed Central

27 June 2017

1 reference

Europe PubMed Central

27 June 2017

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