A molecular dynamics study on the role of the protonation state in the biosynthesis of R-PAC by AHAS

Omar Alvarado, Rafael García-Meseguer, José Javier Ruiz-Pernía, Iñaki Tuñon, Eduardo J. Delgado*

*Corresponding author for this work

Research output: Contribution to journalArticle (Academic Journal)peer-review

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Abstract

The effect of the protonation state of the hydroxyl-ethylthiamin diphosphate intermediate, HEThDP, on the enzyme-substrate interactions and their consequences on the biosynthesis of R-phenylacetylcarbinol, R-PAC, by the acetohydroxy acid synthase, AHAS, is addressed by molecular dynamics simulations. It is found that the form of HEThDP, which favors the formation of R-PAC, is that having the 4-aminopyrimidine ring with the N1′ atom protonated and the N4′ atom as aminopyrimidinium ion. Under this form both active sites of AHAS have the ability to perform the catalysis, unlike that observed for the other possible protonation states of N1′ and N4′ atoms.

Original languageEnglish
Pages (from-to)247-251
Number of pages5
JournalChemical Physics Letters
Volume716
Early online date31 Dec 2018
DOIs
Publication statusPublished - Feb 2019

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