Site-directed mutagenesis and proton NMR spectroscopy of an interdomain segment in the pyruvate dehydrogenase multienzyme complex of Escherichia coli

Biochemistry ◽  
1988 ◽  
Vol 27 (1) ◽  
pp. 289-296 ◽  
Author(s):  
Frieda L. Texter ◽  
Sheena E. Radford ◽  
Ernest D. Laue ◽  
Richard N. Perham ◽  
John S. Miles ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Nmr Spectroscopy ◽  
Pyruvate Dehydrogenase ◽  
Proton Nmr ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Multienzyme Complex ◽  
Proton Nmr Spectroscopy

scholarly journals Limited Proteolysis and Proton NMR Spectroscopy of Bacillus stearothermophilusPyruvate Dehydrogenase Multienzyme Complex

1982 ◽  
Vol 124 (1) ◽  
pp. 63-69 ◽  
Author(s):  
Harry W. DUCKWORTH ◽  
Rainer JAENICKE ◽  
Richard N. PERHAM ◽  
Andrew O. M. WILKIE ◽  
John T. FINCH ◽  
...  
Keyword(s):  
Nmr Spectroscopy ◽  
Limited Proteolysis ◽  
Proton Nmr ◽  
Multienzyme Complex ◽  
Proton Nmr Spectroscopy

Structural studies by proton-NMR spectroscopy of plant horseradish peroxidase C, the wild-type recombinant protein from Escherichia coli and two protein variants, Phe41 Val and Arg38 Lys

1992 ◽  
Vol 207 (2) ◽  
pp. 521-531 ◽  
Author(s):  
Nigel C. VEITCH ◽  
Robert J. P. WILLIAMS ◽  
Robert C. BRAY ◽  
Julian F. BURKE ◽  
Stephen A. SANDERS ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Nmr Spectroscopy ◽  
Horseradish Peroxidase ◽  
Recombinant Protein ◽  
Proton Nmr ◽  
Structural Studies ◽  
Proton Nmr Spectroscopy ◽  
Wild Type ◽  
Protein Variants

scholarly journals Overexpression, site-directed mutagenesis, and mechanism of Escherichia coli acid phosphatase

1992 ◽  
Vol 267 (32) ◽  
pp. 22830-22836 ◽  
Author(s):  
K Ostanin ◽  
E.H. Harms ◽  
P.E. Stevis ◽  
R Kuciel ◽  
M.M. Zhou ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Acid Phosphatase ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis

scholarly journals A genetically detoxified derivative of heat-labile Escherichia coli enterotoxin induces neutralizing antibodies against the A subunit.

1994 ◽  
Vol 180 (6) ◽  
pp. 2147-2153 ◽  
Author(s):  
M Pizza ◽  
M R Fontana ◽  
M M Giuliani ◽  
M Domenighini ◽  
C Magagnoli ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Cholera Toxin ◽  
Neutralizing Antibodies ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
E Coli ◽  
Heat Labile ◽  
A Subunit ◽  
Adp Ribosyltransferase ◽  
Derivatives Of

Escherichia coli enterotoxin (LT) and the homologous cholera toxin (CT) are A-B toxins that cause travelers' diarrhea and cholera, respectively. So far, experimental live and killed vaccines against these diseases have been developed using only the nontoxic B portion of these toxins. The enzymatically active A subunit has not been used because it is responsible for the toxicity and it is reported to induce a negligible titer of toxin neutralizing antibodies. We used site-directed mutagenesis to inactivate the ADP-ribosyltransferase activity of the A subunit and obtained nontoxic derivatives of LT that elicited a good titer of neutralizing antibodies recognizing the A subunit. These LT mutants and equivalent mutants of CT may be used to improve live and killed vaccines against cholera and enterotoxinogenic E. coli.

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