PMID:10425687
| Citation |
Shumilin, IA, Kretsinger, RH and Bauerle, RH (1999) Crystal structure of phenylalanine-regulated 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Escherichia coli. Structure 7:865-75 |
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| 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. |
| Links | |
| Keywords |
3-Deoxy-7-Phosphoheptulonate Synthase/antagonists & inhibitors; 3-Deoxy-7-Phosphoheptulonate Synthase/chemistry; 3-Deoxy-7-Phosphoheptulonate Synthase/metabolism; Amino Acid Sequence; Binding Sites; Catalysis; Crystallography, X-Ray; Escherichia coli/enzymology; Models, Molecular; Molecular Sequence Data; Phenylalanine/metabolism; Protein Conformation; Sequence Homology, Amino Acid |
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