Diverse allosteric componentry and mechanisms control entry into aromatic metabolite biosynthesis.

Wanting Jiao, Eric Jm Lang, Yu Bai, Yifei Fan, Emily J Parker

Journal: Current opinion in structural biology 2021;65():159-167

PMID: 32739636

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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.

Address: Ferrier Research Institute, Victoria University of Wellington, Wellington, New Zealand; Maurice Wilkins Centre for Molecular Biodiscovery, Biomolecular Interaction Centre, University of Canterbury, Christchurch, New Zealand. Electronic address: [email protected].; Maurice Wilkins Centre for Molecular Biodiscovery, Biomolecular Interaction Centre, University of Canterbury, Christchurch, New Zealand.; Ferrier Research Institute, Victoria University of Wellington, Wellington, New Zealand; Maurice Wilkins Centre for Molecular Biodiscovery, Biomolecular Interaction Centre, University of Canterbury, Christchurch, New Zealand.; Ferrier Research Institute, Victoria University of Wellington, Wellington, New Zealand; Maurice Wilkins Centre for Molecular Biodiscovery, Biomolecular Interaction Centre, University of Canterbury, Christchurch, New Zealand. Electronic address: [email protected].

DOI: 10.1016/j.sbi.2020.06.015

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MeSH Terms: 3-Deoxy-7-Phosphoheptulonate Synthase, Allosteric Regulation, Bacteria, Bacterial Proteins, Plant Proteins, Plants