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Vitamin K(2) in Electron Transport System: Are Enzymes Involved in Vitamin K(2) Biosynthesis Promising Drug Targets?

Aerobic and anaerobic respiratory systems allow cells to transport the electrons to terminal electron acceptors. The quinone (ubiquinone or menaquinone) pool is central to the electron transport chain. In the majority of Gram-positive bacteria, vitamin K(2) (menaquinone) is the sole quinone in the e...

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Detalles Bibliográficos
Autores principales: Kurosu, Michio, Begari, Eeshwaraiah
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Molecular Diversity Preservation International 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6257245/
https://www.ncbi.nlm.nih.gov/pubmed/20335999
http://dx.doi.org/10.3390/molecules15031531
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author Kurosu, Michio
Begari, Eeshwaraiah
author_facet Kurosu, Michio
Begari, Eeshwaraiah
author_sort Kurosu, Michio
collection PubMed
description Aerobic and anaerobic respiratory systems allow cells to transport the electrons to terminal electron acceptors. The quinone (ubiquinone or menaquinone) pool is central to the electron transport chain. In the majority of Gram-positive bacteria, vitamin K(2) (menaquinone) is the sole quinone in the electron transport chain, and thus, the bacterial enzymes catalyzing the synthesis of menaquinone are potential targets for the development of novel antibacterial drugs. This manuscript reviews the role of vitamin K in bacteria and humans, and especially emphasizes on recent aspects of menaquinones in bacterial electron transport chain and on discoveries of inhibitor molecules targeting bacterial electron transport systems for new antibacterial agents.
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spelling pubmed-62572452018-12-04 Vitamin K(2) in Electron Transport System: Are Enzymes Involved in Vitamin K(2) Biosynthesis Promising Drug Targets? Kurosu, Michio Begari, Eeshwaraiah Molecules Review Aerobic and anaerobic respiratory systems allow cells to transport the electrons to terminal electron acceptors. The quinone (ubiquinone or menaquinone) pool is central to the electron transport chain. In the majority of Gram-positive bacteria, vitamin K(2) (menaquinone) is the sole quinone in the electron transport chain, and thus, the bacterial enzymes catalyzing the synthesis of menaquinone are potential targets for the development of novel antibacterial drugs. This manuscript reviews the role of vitamin K in bacteria and humans, and especially emphasizes on recent aspects of menaquinones in bacterial electron transport chain and on discoveries of inhibitor molecules targeting bacterial electron transport systems for new antibacterial agents. Molecular Diversity Preservation International 2010-03-10 /pmc/articles/PMC6257245/ /pubmed/20335999 http://dx.doi.org/10.3390/molecules15031531 Text en © 2010 by the authors; http://creativecommons.org/licenses/by/3.0/ licensee Molecular Diversity Preservation International, Basel, Switzerland. This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Review
Kurosu, Michio
Begari, Eeshwaraiah
Vitamin K(2) in Electron Transport System: Are Enzymes Involved in Vitamin K(2) Biosynthesis Promising Drug Targets?
title Vitamin K(2) in Electron Transport System: Are Enzymes Involved in Vitamin K(2) Biosynthesis Promising Drug Targets?
title_full Vitamin K(2) in Electron Transport System: Are Enzymes Involved in Vitamin K(2) Biosynthesis Promising Drug Targets?
title_fullStr Vitamin K(2) in Electron Transport System: Are Enzymes Involved in Vitamin K(2) Biosynthesis Promising Drug Targets?
title_full_unstemmed Vitamin K(2) in Electron Transport System: Are Enzymes Involved in Vitamin K(2) Biosynthesis Promising Drug Targets?
title_short Vitamin K(2) in Electron Transport System: Are Enzymes Involved in Vitamin K(2) Biosynthesis Promising Drug Targets?
title_sort vitamin k(2) in electron transport system: are enzymes involved in vitamin k(2) biosynthesis promising drug targets?
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6257245/
https://www.ncbi.nlm.nih.gov/pubmed/20335999
http://dx.doi.org/10.3390/molecules15031531
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