With the elucidation of myriad anabolic and catabolic enzyme-catalyzed cellular pathways
crisscrossing each other, an obvious question arose: how could these networks operate with …

Tryptophan synthase is a classic enzyme that channels a metabolic intermediate, indole.
The crystal structure of the tryptophan synthase α2β2 complex from Salmonella typhimurium …

Enzymes in heteromeric, allosterically regulated complexes catalyze a rich array of chemical
reactions. Separating the subunits of such complexes, however, often severely attenuates …

This chapter describes in detail the genes and proteins of Escherichia coli involved in the
biosynthesis and transport of the three aromatic amino acids tyrosine, phenylalanine, and …

Background: Feedback inhibition of biosynthetic threonine deaminase (TD) from Escherichia
coli provided one of the earliest examples of protein-based metabolic regulation. Isoleucine …

Crystal structures of wild-type tryptophan synthase α2β2 complexes from Salmonella
typhimurium were determined to investigate the mechanism of allosteric activation of the α …

Monovalent cations activate the pyridoxal phosphate-dependent reactions of tryptophan
synthase and affect intersubunit communication in the α2β2 complex. We report refined …

The natural history of genital Chlamydia trachomatis infections can vary widely; infections
can spontaneously resolve but can also last from months to years, potentially progressing to …

Three-dimensional structures are reported for a mutant (βK87T) tryptophan synthase α2β2
complex with either the substrate l-serine (βK87T-Ser) or product l-tryptophan (βK87T-Trp) at …

The ability of enzymes to catalyze specific reactions, while excluding others, is central to
cellular metabolism. Control of reaction specificity is of particular importance for enzymes …