The diversity of allosteric controls at the gateway to aromatic amino acid biosynthesis.

ABSTRACT: Present within bacteria, plants, and some lower eukaryotes 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase (DAHPS) catalyzes the first committed step in the synthesis of a number of metabolites, including the three aromatic amino acids phenylalanine, tyrosine, and tryptophan. Catalyzing the first reaction in an important biosynthetic pathway, DAHPS is situated at a critical regulatory checkpoint-at which pathway input can be efficiently modulated to respond to changes in the concentration of pathway outputs. Based on a phylogenetic classification scheme, DAHPSs have been divided into three major subtypes (Iα, Iβ, and II). These subtypes are subjected to an unusually diverse pattern of allosteric regulation, which can be used to further subdivide the enzymes. Crystal structures of most

SUBMITTER: Light SH 

PROVIDER: S-EPMC3610045 | biostudies-literature | 2013 Apr

REPOSITORIES: biostudies-literature