000151339 001__ 151339
000151339 005__ 20250307114715.0
000151339 0247_ $$2doi$$a10.1021/acs.jcim.1c00394
000151339 0248_ $$2sideral$$a127128
000151339 037__ $$aART-2021-127128
000151339 041__ $$aeng
000151339 100__ $$aBoneta S.$$uUniversidad de Zaragoza
000151339 245__ $$aQM/MM Study of the Enzymatic Biodegradation Mechanism of Polyethylene Terephthalate
000151339 260__ $$c2021
000151339 5060_ $$aAccess copy available to the general public$$fUnrestricted
000151339 5203_ $$aThe environmental problems derived from the generalized plastic consumption and disposal could find a friendly solution in enzymatic biodegradation. Recently, two hydrolases from Ideonella sakaiensis 201-F6 and the metagenome-derived leaf-branch compost cutinase (LCC), more specially the improved ICCG variant, have revealed degradation activity toward poly ethylene terephthalate (PET). In the present study, the reaction mechanism of this polymer breakage is studied at an atomic level by multiscale QM/MM molecular dynamics simulations, using semiempirical and DFT Hamiltonians to describe the QM region. The obtained free energy surfaces confirmed a characteristic four-step path for both systems, with activation energies in agreement with the experimental observations. Structural analysis of the evolution of the active site along the reaction progress and the study of electrostatic effects generated by the proteins reveal the similarity in the behavior of the active site of these two enzymes. The origin of the apparent better performance of the LCC-ICCG protein over PETase must be due to its capabilities of working at higher temperature and its intrinsic relationship with the crystallinity grade of the polymer. Our results may be useful for the development of more efficient enzymes in the biodegradation of PET.
000151339 536__ $$9info:eu-repo/grantAgreement/ES/MICIU/PGC2018-094852-B-C21
000151339 540__ $$9info:eu-repo/semantics/openAccess$$aby$$uhttp://creativecommons.org/licenses/by/3.0/es/
000151339 590__ $$a6.162$$b2021
000151339 591__ $$aCHEMISTRY, MEDICINAL$$b9 / 63 = 0.143$$c2021$$dQ1$$eT1
000151339 591__ $$aCOMPUTER SCIENCE, INFORMATION SYSTEMS$$b29 / 163 = 0.178$$c2021$$dQ1$$eT1
000151339 591__ $$aCOMPUTER SCIENCE, INTERDISCIPLINARY APPLICATIONS$$b26 / 112 = 0.232$$c2021$$dQ1$$eT1
000151339 591__ $$aCHEMISTRY, MULTIDISCIPLINARY$$b51 / 179 = 0.285$$c2021$$dQ2$$eT1
000151339 592__ $$a1.223$$b2021
000151339 593__ $$aChemical Engineering (miscellaneous)$$c2021$$dQ1
000151339 593__ $$aLibrary and Information Sciences$$c2021$$dQ1
000151339 593__ $$aChemistry (miscellaneous)$$c2021$$dQ1
000151339 594__ $$a7.7$$b2021
000151339 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/publishedVersion
000151339 700__ $$aArafet K.
000151339 700__ $$aMoliner V.
000151339 7102_ $$11002$$2060$$aUniversidad de Zaragoza$$bDpto. Bioq.Biolog.Mol. Celular$$cÁrea Bioquímica y Biolog.Mole.
000151339 773__ $$g61, 6 (2021), 3041-3051$$pJ. Chem Inf. Model.$$tJournal of Chemical Information and Modeling$$x1549-9596
000151339 8564_ $$s4449559$$uhttps://zaguan.unizar.es/record/151339/files/texto_completo.pdf$$yVersión publicada
000151339 8564_ $$s3080846$$uhttps://zaguan.unizar.es/record/151339/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada
000151339 909CO $$ooai:zaguan.unizar.es:151339$$particulos$$pdriver
000151339 951__ $$a2025-03-07-09:32:35
000151339 980__ $$aARTICLE