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

Samuel H. Light, Wayne F. Anderson*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

40 Scopus citations


Present within bacteria, plants, and some lower eukaryotes 3-deoxy-D-arabinoheptulosonate 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 of the regulatory subclasses have been determined. When viewed collectively, these structures illustrate how distinct mechanisms of allostery are applied to a common catalytic scaffold. Here, we review structural revelations regarding DAHPS regulation and make the case that the functional difference between the three major DAHPS subtypes relates to basic distinctions in quaternary structure and mechanism of allostery.

Original languageEnglish (US)
Pages (from-to)395-404
Number of pages10
JournalProtein Science
Issue number4
StatePublished - Apr 2013


  • 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase
  • Allostery
  • Chorismate mutase
  • Feedback regulation
  • Inhibition
  • Phenylalanine
  • Shikimate pathway
  • Tryptophan
  • Tyrosine

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology


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