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dc.contributor.authorAcebrón, Iván-
dc.contributor.authorMahasenan, K.V.-
dc.contributor.authorDe Benedetti, S.-
dc.contributor.authorLee, M.-
dc.contributor.authorArtola-Recolons, Cecilia-
dc.contributor.authorHesek, D.-
dc.contributor.authorWang, H.-
dc.contributor.authorHermoso, Juan A.-
dc.contributor.authorMobashery, S.-
dc.date.accessioned2018-05-25T10:08:24Z-
dc.date.available2018-05-25T10:08:24Z-
dc.date.issued2017-
dc.identifierdoi: 10.1021/jacs.7b01626-
dc.identifierissn: 1520-5126-
dc.identifier.citationJournal of the American Chemical Society 139: 6795- 6798 (2017)-
dc.identifier.urihttp://hdl.handle.net/10261/165119-
dc.description.abstractThe N-acetylglucosaminidase NagZ of Pseudomonas aeruginosa catalyzes the first cytoplasmic step in recycling of muropeptides, cell-wall-derived natural products. This reaction regulates gene expression for the β-lactam resistance enzyme, β-lactamase. The enzyme catalyzes hydrolysis of N-acetyl-β-d-glucosamine-(1→4)-1,6-anhydro-N-acetyl-β-d-muramyl-peptide (1) to N-acetyl-β-d-glucosamine (2) and 1,6-anhydro-N-acetyl-β-d-muramyl-peptide (3). The structural and functional aspects of catalysis by NagZ were investigated by a total of seven X-ray structures, three computational models based on the X-ray structures, molecular-dynamics simulations and mutagenesis. The structural insights came from the unbound state and complexes of NagZ with the substrate, products and a mimetic of the transient oxocarbenium species, which were prepared by synthesis. The mechanism involves a histidine as acid/base catalyst, which is unique for glycosidases. The turnover process utilizes covalent modification of D244, requiring two transition-state species and is regulated by coordination with a zinc ion. The analysis provides a seamless continuum for the catalytic cycle, incorporating large motions by four loops that surround the active site.-
dc.publisherAmerican Chemical Society-
dc.relationMINECO/ICTI2013-2016/BFU2014-59389-P-
dc.rightsclosedAccess-
dc.titleCatalytic Cycle of the N-Acetylglucosaminidase NagZ from Pseudomonas aeruginosa-
dc.typeartículo-
dc.date.updated2018-05-25T10:08:25Z-
dc.description.versionPeer Reviewed-
dc.language.rfc3066eng-
dc.contributor.funderMinisterio de Economía y Competitividad (España)-
dc.relation.csic-
dc.identifier.funderhttp://dx.doi.org/10.13039/501100003329es_ES
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