Literature DB >> 6375667

Affinity engineering of maltoporin: variants with enhanced affinity for particular ligands.

A Clune, K S Lee, T Ferenci.   

Abstract

Affinity-chromatographic selection on immobilized starch was used to selectively enhance the affinity of the maltodextrin-specific pore protein ( maltoporin , LamB protein, or lambda receptor protein) in the outer membrane of E. coli. Selection strategies were established for rare bacteria in large populations producing maltoporin variants with enhanced affinities for both starch and maltose, for starch but not maltose and for maltose but not starch. Three classes of lamB mutants with up to eight-fold increase in affinity for particular ligands were isolated. These mutants provide a unique range of modifications in the specificity of a transport protein.

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Year:  1984        PMID: 6375667     DOI: 10.1016/0006-291x(84)90684-3

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  5 in total

1.  Site-directed mutagenesis of tyrosine 118 within the central constriction site of the LamB (Maltoporin) channel of Escherichia coli. I. Effect on ion transport.

Authors:  Frank Orlik; Christian Andersen; Roland Benz
Journal:  Biophys J       Date:  2002-05       Impact factor: 4.033

2.  Protein engineering and site-directed mutagenesis. Patents and literature.

Authors:  R J Linhardt
Journal:  Appl Biochem Biotechnol       Date:  1986-08       Impact factor: 2.926

3.  Site-directed mutagenesis of tyrosine 118 within the central constriction site of the LamB (maltoporin) channel of Escherichia coli. II. Effect on maltose and maltooligosaccharide binding kinetics.

Authors:  Frank Orlik; Christian Andersen; Roland Benz
Journal:  Biophys J       Date:  2002-07       Impact factor: 4.033

4.  Genetic analysis of sequences in maltoporin that contribute to binding domains and pore structure.

Authors:  H G Heine; G Francis; K S Lee; T Ferenci
Journal:  J Bacteriol       Date:  1988-04       Impact factor: 3.490

5.  Channel architecture in maltoporin: dominance studies with lamB mutations influencing maltodextrin binding provide evidence for independent selectivity filters in each subunit.

Authors:  T Ferenci; K S Lee
Journal:  J Bacteriol       Date:  1989-02       Impact factor: 3.490

  5 in total

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