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Nucleobase deaminases: a potential enzyme system for new therapies

Nucleobase deaminases are essential enzymes that are involved in the catabolic pathway and stringently regulate the concentration of the nucleobase derivative pool, which is paramount for nucleotide recycling. This review presents an overview of the structure, function and mechanism of CDA deaminase...

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Detalles Bibliográficos
Autores principales: Gaded, Vandana, Anand, Ruchi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Royal Society of Chemistry 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9081823/
https://www.ncbi.nlm.nih.gov/pubmed/35540270
http://dx.doi.org/10.1039/c8ra04112a
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author Gaded, Vandana
Anand, Ruchi
author_facet Gaded, Vandana
Anand, Ruchi
author_sort Gaded, Vandana
collection PubMed
description Nucleobase deaminases are essential enzymes that are involved in the catabolic pathway and stringently regulate the concentration of the nucleobase derivative pool, which is paramount for nucleotide recycling. This review presents an overview of the structure, function and mechanism of CDA deaminases and their potential as enzyme systems for the development of new antimicrobial therapies. The evolutionary divergence of human nucleobase deaminases with respect to bacterial enzymes has been used as a central theme towards the development of strategies for potential drug targets. Especially, differences in their tertiary fold, active site architectures and mechanisms of regulation have been highlighted in this study. Overall, deaminases present a unique opportunity as drug targets because of their functional plasticity and fidelity.
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spelling pubmed-90818232022-05-09 Nucleobase deaminases: a potential enzyme system for new therapies Gaded, Vandana Anand, Ruchi RSC Adv Chemistry Nucleobase deaminases are essential enzymes that are involved in the catabolic pathway and stringently regulate the concentration of the nucleobase derivative pool, which is paramount for nucleotide recycling. This review presents an overview of the structure, function and mechanism of CDA deaminases and their potential as enzyme systems for the development of new antimicrobial therapies. The evolutionary divergence of human nucleobase deaminases with respect to bacterial enzymes has been used as a central theme towards the development of strategies for potential drug targets. Especially, differences in their tertiary fold, active site architectures and mechanisms of regulation have been highlighted in this study. Overall, deaminases present a unique opportunity as drug targets because of their functional plasticity and fidelity. The Royal Society of Chemistry 2018-06-28 /pmc/articles/PMC9081823/ /pubmed/35540270 http://dx.doi.org/10.1039/c8ra04112a Text en This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by-nc/3.0/
spellingShingle Chemistry
Gaded, Vandana
Anand, Ruchi
Nucleobase deaminases: a potential enzyme system for new therapies
title Nucleobase deaminases: a potential enzyme system for new therapies
title_full Nucleobase deaminases: a potential enzyme system for new therapies
title_fullStr Nucleobase deaminases: a potential enzyme system for new therapies
title_full_unstemmed Nucleobase deaminases: a potential enzyme system for new therapies
title_short Nucleobase deaminases: a potential enzyme system for new therapies
title_sort nucleobase deaminases: a potential enzyme system for new therapies
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9081823/
https://www.ncbi.nlm.nih.gov/pubmed/35540270
http://dx.doi.org/10.1039/c8ra04112a
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