Crystal structure of phenylalanine-regulated 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Escherichia coli.
Shumilin, I.A., Kretsinger, R.H., Bauerle, R.H.(1999) Structure 7: 865-875
- PubMed: 10425687 
- DOI: https://doi.org/10.1016/s0969-2126(99)80109-9
- Primary Citation of Related Structures:  
1QR7 - PubMed Abstract: 
In microorganisms and plants the first step in the common pathway leading to the biosynthesis of aromatic compounds is the stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP). This reaction is catalyzed by DAHP synthase (DAHPS), a metal-activated enzyme, which in microorganisms is the target for negative-feedback regulation by pathway intermediates or by end products. In Escherichia coli there are three DAHPS isoforms, each specifically inhibited by one of the three aromatic amino acids.
Organizational Affiliation: 
Department of Biology, University of Virginia, Charlottesville 22903, USA.