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Journal Article
Tryptophan synthase: a mine for enzymologists
2009
Overview
Tryptophan synthase is a pyridoxal 5'-phosphate-dependent α₂β₂ complex catalyzing the last two steps of tryptophan biosynthesis in bacteria, plants and fungi. Structural, dynamic and functional studies, carried out over more than 40 years, have unveiled that: (1) α- and β-active sites are separated by about 20 Å and communicate via the selective stabilization of distinct conformational states, triggered by the chemical nature of individual catalytic intermediates and by allosteric ligands; (2) indole, formed at α-active site, is intramolecularly channeled to the β-active site; and (3) naturally occurring as well as genetically generated mutants have allowed to pinpoint functional and regulatory roles for several individual amino acids. These key features have made tryptophan synthase a text-book case for the understanding of the interplay between chemistry and conformational energy landscapes.
Publisher
Basel : SP Birkhäuser Verlag Basel,SP Birkhäuser Verlag Basel,Springer Nature B.V
