6533b7ddfe1ef96bd1275557
RESEARCH PRODUCT
A molecular dynamics study on the role of the protonation state in the biosynthesis of R-PAC by AHAS
Omar AlvaradoOmar AlvaradoRafael Garcia-meseguerRafael García-meseguerJ. Javier Ruiz-perníaIñaki TuñónEduardo J. Delgadosubject
Acetohydroxy Acid SynthaseStereochemistryGeneral Physics and AstronomyProtonation02 engineering and technology010402 general chemistry021001 nanoscience & nanotechnologyRing (chemistry)01 natural sciences0104 chemical sciencesCatalysisIonchemistry.chemical_compoundMolecular dynamicsBiosynthesischemistryAtomPhysical and Theoretical Chemistry0210 nano-technologydescription
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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2019-02-01 | Chemical Physics Letters |