Chorismate biosynthesis (Saccharomyces cerevisiae)

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Chorismate, an intermediate in the synthesis of the aromatic amino acids and the vitamins, p-aminobenzoate and p-hydroxybenzoate, is synthesized by the shikimate pathway. The shikimate pathway has been found to be common to all eukaryotes and prokaryotes studied thus far (as reported in (CITS:[1943992])). In Saccharomyces cerevisiae the initial step is catalyzed by two deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) synthase isoenzymes, one of which (ARO3) is feedback inhibited by phenylalanine, and the other (ARO4) by tyrosine (CITS:[1943992]). Both DAHP isoenzymes are derepressed by amino acid starvation (general control of amino acid biosynthesis) (CITS:[2906401]). The 5 subsequent reactions are catalyzed by the pentafunctional arom enzyme, Aro1p (CITS:[1943992][2825635]). Aro1p is a mosaic of five monofunctional domains, each of which corresponds to one of five separate monofunctional E. coli enzymes (CITS:[1943992][2825635]). The last step of chorismate biosynthesis, before the pathway branches to synthesize different terminal products, is catalyzed by Aro2p (CITS:[Jones][1943992]).

SOURCE: SGD pathways, http://pathway.yeastgenome.org/server.html

Based on http://pathway.yeastgenome.org/biocyc/