Advances in menaquinone biosynthesis: sublocalisation and allosteric regulation.

Autor: Johnston JM; School of Physical and Chemical Sciences, Biomolecular Interaction Centre, and Maurice Wilkins Centre for MolecularBiodiscovery, University of Canterbury, Christchurch 8041, New Zealand. Electronic address: jodie.johnston@canterbury.ac.nz., Bulloch EM; Laboratory of Structural Biology, School of Biological Sciences and Maurice Wilkins Centre for MolecularBiodiscovery, University of Auckland, Private Bag 92019, Auckland, New Zealand.
Jazyk: angličtina
Zdroj: Current opinion in structural biology [Curr Opin Struct Biol] 2020 Dec; Vol. 65, pp. 33-41. Date of Electronic Publication: 2020 Jul 05.
DOI: 10.1016/j.sbi.2020.05.005
Abstrakt: Menaquinones (vitamin K2) are a family of redox-active small molecules with critical functions across all domains of life, including energy generation in bacteria and bone health in humans. The enzymes involved in menaquinone biosynthesis also have bioengineering applications and are potential antimicrobial drug targets. New insights into the essential roles of menaquinones, and their potential to cause redox-related toxicity, have highlighted the need for this pathway to be tightly controlled. Here, we provide an overview of our current understanding of the classical menaquinone biosynthesis pathway in bacteria. We also review recent discoveries on protein-level allostery and sublocalisation of membrane-bound enzymes that have provided insight into the regulation of flux through this biosynthetic pathway.
(Copyright © 2020 Elsevier Ltd. All rights reserved.)
Databáze: MEDLINE
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