The objectives of the program include the synthesis of analogs of chorismate and prephenate and investigations of their activity as substrate inhibitors or suicide substrates for chorismate mutase or prephenate dehydrogenase. These target enzymes catalyze the biosynthesis of tyrosine and phenylalanine in bacteria, fungi, and higher plants. The long-range goal is the discovery of analogs that will be useful antibacterial agents and antifungal agents by selective blocking of target enzymes. Other objectives include the total synthesis of biosynthetic intermediates in chorismate pathway and the synthesis of substances that will be used for mechanistic investigations with chorismate mutase and prephenate dehydrogenase.
| Liu, J; Quinn, N; Berchtold, G A et al. (1990) Overexpression, purification, and characterization of isochorismate synthase (EntC), the first enzyme involved in the biosynthesis of enterobactin from chorismate. Biochemistry 29:1417-25 |
| Rusnak, F; Liu, J; Quinn, N et al. (1990) Subcloning of the enterobactin biosynthetic gene entB: expression, purification, characterization, and substrate specificity of isochorismatase. Biochemistry 29:1425-35 |
| Sakaitani, M; Rusnak, F; Quinn, N R et al. (1990) Mechanistic studies on trans-2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase (Ent A) in the biosynthesis of the iron chelator enterobactin. Biochemistry 29:6789-98 |
| Walsh, C T; Erion, M D; Walts, A E et al. (1987) Chorismate aminations: partial purification of Escherichia coli PABA synthase and mechanistic comparison with anthranilate synthase. Biochemistry 26:4734-45 |
