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File: /home/orthodiedw/nutridatabase/application/controllers/Articles.php
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File: /home/orthodiedw/nutridatabase/application/controllers/Articles.php
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File: /home/orthodiedw/nutridatabase/application/controllers/Articles.php
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Filename: drivers/Session_files_driver.php

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File: /home/orthodiedw/nutridatabase/application/controllers/Articles.php
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Filename: drivers/Session_files_driver.php

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File: /home/orthodiedw/nutridatabase/application/controllers/Articles.php
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File: /home/orthodiedw/nutridatabase/application/controllers/Articles.php
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File: /home/orthodiedw/nutridatabase/index.php
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Démêler le mécanisme d'inhibition de la l-gulonate-3-déshydrogénase par l'acide ascorbique: informations tirées de la modélisation moléculaire.

La l-Gulonate déshydrogénase (GuDH) est une enzyme cruciale de la voie du métabolisme du sucre non phosphorylée ou de la voie glucuronate-xylulose (GX). Certains composés naturels inhibent la GuDH. L'acide ascorbique est l'un de ces inhibiteurs de la GuDH. Cependant, le mécanisme exact par lequel l'acide ascorbique inhibe la GuDH est encore inconnu. Dans cette étude, nous essayons d'étudier l'inhibition de la GuDH en utilisant des approches informatiques en générant un modèle pour la GuDH de buffle. Nous avons utilisé ce modèle pour effectuer des amarrages à l’aveugle d’acide ascorbique à GuDH. Certaines conformations amarrées de l'acide ascorbique se lient près de Asp39 et présentent des collisions stériques avec la conformation de la structure cristalline du NADH. Pour évaluer la stabilité dynamique du complexe GuDH-acide ascorbique, nous avons effectué six simulations de dynamique moléculaire pour GuDH, trois sous forme libre et en complexe avec de l'acide ascorbique pendant 50 ns, pour obtenir 300 ns de trajectoires au total. Au cours des simulations, l’acide ascorbique a interagi avec plusieurs résidus à proximité de Asp39. Comme Asp39 est un résidu important pour la liaison et la spécificité du NADH, l’interaction de l’acide ascorbique près de Asp39 entrave la liaison du NADH et a une incidence sur le fonctionnement enzymatique de la GuDH. Dans cette étude, nous analysons ces interactions entre l’acide ascorbique et la GuDH. Notre analyse révèle de nouveaux détails sur le mécanisme d'inhibition de la GuDH par l'acide ascorbique.


Source: https://www.ncbi.nlm.nih.gov/pubmed/30316191


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