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In silico analysis of glycinamide ribonucleotide transformylase inhibition by PY873, PY899 and DIA

In humans, purine de novo synthesis pathway consists of multi-functional enzymes. Nucleotide metabolism enzymes are potential drug targets for treating cancer and autoimmune diseases. Glycinamide ribonucleotide transformylase (GART) is one of the most important trifunctional enzymes involved in puri...

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Autores principales: Batool, Sidra, Nawaz, Muhammad Sulaman, Mushtaq, Gohar, Parvaiz, Fahed, Kamal, Mohammad A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5562383/
https://www.ncbi.nlm.nih.gov/pubmed/28855807
http://dx.doi.org/10.1016/j.sjbs.2014.11.008
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author Batool, Sidra
Nawaz, Muhammad Sulaman
Mushtaq, Gohar
Parvaiz, Fahed
Kamal, Mohammad A.
author_facet Batool, Sidra
Nawaz, Muhammad Sulaman
Mushtaq, Gohar
Parvaiz, Fahed
Kamal, Mohammad A.
author_sort Batool, Sidra
collection PubMed
description In humans, purine de novo synthesis pathway consists of multi-functional enzymes. Nucleotide metabolism enzymes are potential drug targets for treating cancer and autoimmune diseases. Glycinamide ribonucleotide transformylase (GART) is one of the most important trifunctional enzymes involved in purine synthesis. Previous studies have demonstrated the role of folate inhibitors against tumor activity. In this present study, three components of GART enzyme were targeted as receptor dataset and in silico analysis was carried out with folate ligand dataset. To accomplish the task, Autodock 4.2 was used for determining the docking compatibilities of ligand and receptor dataset. Taken together, it has been suggested that folate ligands could be potentially used as inhibitors of GART.
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spelling pubmed-55623832017-08-30 In silico analysis of glycinamide ribonucleotide transformylase inhibition by PY873, PY899 and DIA Batool, Sidra Nawaz, Muhammad Sulaman Mushtaq, Gohar Parvaiz, Fahed Kamal, Mohammad A. Saudi J Biol Sci Original Article In humans, purine de novo synthesis pathway consists of multi-functional enzymes. Nucleotide metabolism enzymes are potential drug targets for treating cancer and autoimmune diseases. Glycinamide ribonucleotide transformylase (GART) is one of the most important trifunctional enzymes involved in purine synthesis. Previous studies have demonstrated the role of folate inhibitors against tumor activity. In this present study, three components of GART enzyme were targeted as receptor dataset and in silico analysis was carried out with folate ligand dataset. To accomplish the task, Autodock 4.2 was used for determining the docking compatibilities of ligand and receptor dataset. Taken together, it has been suggested that folate ligands could be potentially used as inhibitors of GART. Elsevier 2017-09 2014-11-22 /pmc/articles/PMC5562383/ /pubmed/28855807 http://dx.doi.org/10.1016/j.sjbs.2014.11.008 Text en © 2014 The Authors http://creativecommons.org/licenses/by-nc-nd/3.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/3.0/).
spellingShingle Original Article
Batool, Sidra
Nawaz, Muhammad Sulaman
Mushtaq, Gohar
Parvaiz, Fahed
Kamal, Mohammad A.
In silico analysis of glycinamide ribonucleotide transformylase inhibition by PY873, PY899 and DIA
title In silico analysis of glycinamide ribonucleotide transformylase inhibition by PY873, PY899 and DIA
title_full In silico analysis of glycinamide ribonucleotide transformylase inhibition by PY873, PY899 and DIA
title_fullStr In silico analysis of glycinamide ribonucleotide transformylase inhibition by PY873, PY899 and DIA
title_full_unstemmed In silico analysis of glycinamide ribonucleotide transformylase inhibition by PY873, PY899 and DIA
title_short In silico analysis of glycinamide ribonucleotide transformylase inhibition by PY873, PY899 and DIA
title_sort in silico analysis of glycinamide ribonucleotide transformylase inhibition by py873, py899 and dia
topic Original Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5562383/
https://www.ncbi.nlm.nih.gov/pubmed/28855807
http://dx.doi.org/10.1016/j.sjbs.2014.11.008
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