Literature DB >> 2345059

Site-directed mutagenesis of ricin A chain Trp 211 to Phe.

J L Bradley1, P M McGuire.   

Abstract

Oligonucleotide-directed site-specific mutagenesis has been used to make a conservative change in the putative active site of the catalytic subunit of the toxin ricin. The substitution of phenylalanine for tryptophan at position 211 of the A chain reduces but does not abolish catalytic activity, as assayed by inhibition of cell-free protein synthesis.

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Year:  1990        PMID: 2345059     DOI: 10.1111/j.1399-3011.1990.tb00062.x

Source DB:  PubMed          Journal:  Int J Pept Protein Res        ISSN: 0367-8377


  4 in total

1.  Determination by systematic deletion of the amino acids essential for catalysis by ricin A chain.

Authors:  K N Morris; I G Wool
Journal:  Proc Natl Acad Sci U S A       Date:  1992-06-01       Impact factor: 11.205

2.  Analysis of the contribution of an amphiphilic alpha-helix to the structure and to the function of ricin A chain.

Authors:  K N Morris; I G Wool
Journal:  Proc Natl Acad Sci U S A       Date:  1994-08-02       Impact factor: 11.205

3.  The role of tyrosine-114 in the enzymatic activity of the Shiga-like toxin I A-chain.

Authors:  R L Deresiewicz; P R Austin; C J Hovde
Journal:  Mol Gen Genet       Date:  1993-11

4.  Simulation analysis of formycin 5'-monophosphate analog substrates in the ricin A-chain active site.

Authors:  M A Olson; J P Scovill; D C Hack
Journal:  J Comput Aided Mol Des       Date:  1995-06       Impact factor: 3.686

  4 in total

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