3-Dehydroquinate synthase (DHQS)

3-Dehydroquinate synthase is a monomeric enzyme (about 37–39 kDa) that catalyzes the second step in the shikimate pathway—a biosynthetic route essential for the production of aromatic amino acids such as phenylalanine, tyrosine, and tryptophan—in bacteria, plants, fungi, and some protists, but absent in animals and humans. It converts 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to 3-dehydroquinate through a complex mechanism involving oxidation, phosphate elimination, carbonyl reduction, ring opening, and aldol condensation. The essential nature of the shikimate pathway in many pathogens, and its absence in mammals, makes 3-dehydroquinate synthase an attractive and highly selective target for antimicrobial, antifungal, anti-parasitic, and herbicidal development. In some fungi and protists, this enzyme forms part of a larger multifunctional protein complex known as the AROM complex. Enzyme activity requires cofactors such as NAD+, and may depend on divalent metal ions (notably Co2+, Zn2+, Mn2+, or Cd2+ in some species)[1][5][6][8][9]. **Note:** No approved drugs currently target this enzyme in clinical practice, but research is ongoing in the context of new antimicrobial and herbicidal agents. No human biomarker or safety concern exists given humans lack the shikimate pathway[1][6].

Other names

Dehydroquinate synthaseDHQSAROM protein (as part of the AROM complex in some eukaryotes)

Inhibition of the enzyme to block the shikimate pathway, thereby preventing biosynthesis of aromatic amino acids and leading to growth inhibition or death of bacteria, fungi, or plants[1][4][6].