Substitution of glutamic acid 109 by aspartic acid alters the substrate specificity and catalytic activity of the .beta.-subunit in the tryptophan synthase bienzyme complex from Salmonella typhimurium
1992
In an effort to understand the catalytic mechanism of the tryptophan synthase β-subunit from Salmonella typhimurium, possible functional active site residues have been identified (on the basis of the 3-D crystal structure of the bienzyme complex) and targeted for analysis utilizing site-directed mutagenesis. The chromophoric properties of the pyridoxal 5'-phosphate cofactor provide a particularly convenient and sensitive spectral probe to directly investigate changes in catalytic events which occur upon modification of the β-subunit
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