Summary
Bacterial tryptophan synthase has been the subject of pioneering studies on the relationship between gene structure and protein structure. A system for oligonucleotide-directed site-specific mutagenesis of the trpA and trpB genes of Salmonella typhimurium has been developed to examine the role of specific amino acid residues in the two subunits. It has been found that changing arginine-179 of the a subunit to leucine does not inactivate the enzyme, but does cause marked alterations in the effects of ligands on site-site interactions. Our studies of structure and function in the tryptophan synthase complex will be greatly facilitated in the future by being able to correlate the effects of protein engineering with the known three-dimensional structure of the enzyme from S. typhimurium which is being solved by x-ray crystallography.
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© 1987 Birkhäuser Verlag Basel
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Miles, E.W., Kawasaki, H., Ahmed, S.A., Bauerle, R. (1987). Bacterial Tryptophan Synthase: A Multienzyme Complex Which Contains Pyridoxal Phosphate. In: Korpela, T.K., Christen, P. (eds) Biochemistry of Vitamin B6 . Birkhäuser Congress Reports. Birkhäuser, Basel. https://doi.org/10.1007/978-3-0348-9308-4_14
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