Prephenate dehydrogenase is involved in tyrosine biosynthesis. It catalyzes the reaction: prephenate + NAD+ = 4-hydroxyphenylpyruvate + CO2 + NADH. It uses NAD as a cofactor. Localized in the cytoplam; High confidence in function and specificity.

Chorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.

3-Phosphoshikimate 1-carboxyvinyltransferase; Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.

3-Dehydroquinate synthase; Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).

Anthranilate synthase component II (glutamine amidotransferase); The anthranilate synthase catalyzes the formation of anthranilate from chorismate and L-glutamine, the first step in the biosynthesis of tryptophan. The enzyme is a Tetramer of two components I and two components II. Associated with the component I, the component II of the anthranilate synthase provides the glutamine amidotransferase activity (GATase, 2.4.2.-) that catalyses the removal of the ammonia group from a glutamate molecule and its subsequent transfer to a specific substrate, thus creating a new carbon-nitrogen g [...]

Shikimate dehydrogenase catalyzes the fourth step of The shikimate pathway. In a NADP+-dependent reaction, AroE converts the shikimate to 3-dehydroshikimate. The N-terminal domain is the shikimate-binding domain and consists of a mainly parallel six-stranded beta-sheet and six alpha-helices. The C-terminal NADP-binding domain adopts a nearly canonical Rossmann fold; Localized in the cytoplasm; High confidence in function and specificity.

The anthranilate synthase catalyzes the formation of anthranilate from chorismate and L-glutamine, the first step in the biosynthesis of tryptophan. The enzyme is a Tetramer of two components I and two components II. The component I only catalyzes the formation of anthranilate using chorismate and ammonia rather than glutamine; The anthranilate synthase is regulated by feedback inhibition by tryptophan; Belongs to the anthranilate synthase component I family; Localized in the cytoplasm; High confidence in function and specificity.

3-Dehydroquinate synthase is involved in the biosynthesis of aromatic amino acids. It catalyzes the second step of the shikimate pathway, the formation of dehydroquinate and orthophosphate from 3-deoxy-D-arabino heptulosonic 7 phosphate. It forms a monomer and binds NAD and divalent metal cation as cofactors. Localized in the cytoplasm; High confidence in function and specificity.

The isochorismate synthase, called also isochorismate mutase catalyses the conversion of chorismate to isochorismate, the first step in the biosynthesis of both respiratory chain components: menaquinone (MK, vitamin K2) and phylloquinone (vitamin K1); Localized in the cytoplasm; High confidence in function and specificity.