The shikimate dehydrogenase family: Functional diversity within a conserved structural and mechanistic framework

• The shikimate dehydrogenase (SDH) family consists of at least five different enzyme classes.
• SDH family proteins have diverse roles in the secondary metabolism of plants and microbes.
• The biochemical and structural properties of the members of the SDH family are described here.

Shikimate dehydrogenase (SDH) catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes. The indispensible nature of this enzyme makes it a potential target for herbicides and antimicrobials. SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences, making the family a particularly interesting system for studying modes of substrate recognition used by enzymes. Here, we review our current understanding of the biochemical and structural properties of each of the five previously identified SDH family functional classes.