Diverse allosteric componentry and mechanisms control entry into aromatic metabolite biosynthesis
Related Experiment Video
Updated: Dec 13, 2025

A Customizable Approach for the Enzymatic Production and Purification of Diterpenoid Natural Products
Published on: October 4, 2019
Wanting Jiao1, Eric Jm Lang2, Yu Bai1
1Ferrier Research Institute, Victoria University of Wellington, Wellington, New Zealand; Maurice Wilkins Centre for Molecular Biodiscovery, Biomolecular Interaction Centre, University of Canterbury, Christchurch, New Zealand.
Abstract:
Allosteric regulation of the enzyme 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase (DAH7PS) controls the entry into aromatic amino acid biosynthesis in plants and microorganisms. DAH7PS has acquired a diverse range of allosteric machinery to enable this functionality. This review provides an overview of the current knowledge of the structural basis of allostery in this enzyme family and the evolutionary relationships between the different solutions to allosteric control of aromatic metabolite biosynthesis.
More Related Videos
09:27Functional Complementation Analysis FCA: A Laboratory Exercise Designed and Implemented to Supplement the Teaching of Biochemical Pathways
Published on: June 24, 2016
08:56Transient Expression in Nicotiana Benthamiana Leaves for Triterpene Production at a Preparative Scale
Published on: August 16, 2018
Related Concept Videos
Amino Acid Biosynthetic Pathways
Regulation of Metabolism
Allosteric Proteins-ATCase
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
Allosteric Regulation
Ligand Binding and Linkage
Biosynthesis in Bacteria