The diversity of allosteric controls at the gateway to aromatic amino acid biosynthesis. (8th March 2013)

• Record Type: Journal Article
• Authors: Light, Samuel H.; Anderson, Wayne F.
• Is Part Of: Protein science. Volume 22:Number 4(2013:Apr.)
• Page Start: 395
• Page End: 404
• Publication Date: 2013-03-08
• Subjects: Proteins -- Periodicals; 572.6
• DOI: 10.1002/pro.2233
• Languages: English
• ISSNs: 0961-8368

Abstract

<abstract abstract-type="main" xml:lang="en"> <title>Abstract</title> <p>Present within bacteria, plants, and some lower eukaryotes 3‐deoxy‐<sc>D</sc>‐<italic>arabino</italic>‐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 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.</p> </abstract>