Nicking of the tryptophan synthase beta 2-subunit at Glu-296 prevents the conformational change undergone on binding the alpha-subunit.
Using a monoclonal antibody as conformational probe it has been shown that the weakly active nicked-beta 2 dimer of tryptophan synthase generated by proteolytic cleavage at Glu-296, does not undergo on association with alpha subunit a conformational change known to occur in intact beta 2 subunit. This alpha induced conformational change is also prevented in intact beta 2 by the coenzyme pyridoxal-5'-phosphate when the substrate L-serine is absent.
Linkens
H J
HJ
Unité de Biochimie Cellulaire, Institut Pasteur, Paris, France.
Djavadi-Ohaniance
L
L
Goldberg
M E
ME
D000911:Antibodies, Monoclonal; D010450:Endopeptidases / Q000494:pharmacology; D004926:Escherichia coli / Q000201:enzymology; D005971:Glutamates / Q000378:metabolism; D011487:Protein Conformation; D012694:Serine / Q000378:metabolism; D013329:Structure-Activity Relationship; D013379:Substrate Specificity; D014367:Tryptophan Synthase / Q000737:chemistry* / Q000378:metabolism
D000911:Antibodies, Monoclonal; D005971:Glutamates; D012694:Serine; D010450:Endopeptidases; D014367:Tryptophan Synthase