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New Insight into the Transcarbamylase Family: TheStructure of Putrescine Transcarbamylase, a Key Catalystfor Fermentative Utilization of Agmatine

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New Insight into the Transcarbamylase Family: TheStructure of Putrescine Transcarbamylase, a Key Catalystfor Fermentative Utilization of Agmatine

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dc.contributor.author Polo, Luis Mariano es_ES
dc.contributor.author Gil Ortíz, Fernando es_ES
dc.contributor.author Cantin Sanz, Angel es_ES
dc.contributor.author Rubio, Vicente es_ES
dc.date.accessioned 2015-06-09T07:58:34Z
dc.date.available 2015-06-09T07:58:34Z
dc.date.issued 2012-02-20
dc.identifier.issn 1932-6203
dc.identifier.uri http://hdl.handle.net/10251/51405
dc.description.abstract Transcarbamylases reversibly transfer a carbamyl group from carbamylphosphate (CP) to an amine. Although aspartate transcarbamylase and ornithine transcarbamylase (OTC) are well characterized, little was known about putrescine transcarbamylase (PTC), the enzyme that generates CP for ATP production in the fermentative catabolism of agmatine. We demonstrate that PTC (from Enterococcus faecalis), in addition to using putrescine, can utilize L-ornithine as a poor substrate. Crystal structures at 2.5 A˚ and 2.0 A˚ resolutions of PTC bound to its respective bisubstrate analog inhibitors for putrescine and ornithine use, N-(phosphonoacetyl)-putrescine and d-N-(phosphonoacetyl)-L-ornithine, shed light on PTC preference for putrescine. Except for a highly prominent C-terminal helix that projects away and embraces an adjacent subunit, PTC closely resembles OTCs, suggesting recent divergence of the two enzymes. Since differences between the respective 230 and SMG loops of PTC and OTC appeared to account for the differential preference of these enzymes for putrescine and ornithine, we engineered the 230-loop of PTC to make it to resemble the SMG loop of OTCs, increasing the activity with ornithine and greatly decreasing the activity with putrescine. We also examined the role of the C-terminal helix that appears a constant and exclusive PTC trait. The enzyme lacking this helix remained active but the PTC trimer stability appeared decreased, since some of the enzyme eluted as monomers from a gel filtration column. In addition, truncated PTC tended to aggregate to hexamers, as shown both chromatographically and by X-ray crystallography. Therefore, the extra Cterminal helix plays a dual role: it stabilizes the PTC trimer and, by shielding helix 1 of an adjacent subunit, it prevents the supratrimeric oligomerizations of obscure significance observed with some OTCs. Guided by the structural data we identify signature traits that permit easy and unambiguous annotation of PTC sequences. es_ES
dc.description.sponsorship This work was supported by grants BFU2008-05021 of the Spanish Ministry for Science and Prometeo/2009/051 of the Valencian Government. The European Union and the European Molecular Biology Laboratory funded synchrotron visits. LMP was supported by a Consejo Superior de Investigaciones Cientificas-Banco de Santander fellowship and FGO by a JAE-DOC contract of the Consejo Superior de Investigaciones Cientificas. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript. en_EN
dc.language Inglés es_ES
dc.publisher Public Library of Science es_ES
dc.relation.ispartof PLoS ONE es_ES
dc.rights Reconocimiento (by) es_ES
dc.title New Insight into the Transcarbamylase Family: TheStructure of Putrescine Transcarbamylase, a Key Catalystfor Fermentative Utilization of Agmatine es_ES
dc.type Artículo es_ES
dc.identifier.doi 10.1371/journal.pone.0031528
dc.relation.projectID info:eu-repo/grantAgreement/MICINN//BFU2008-05021/ES/COMPLEJOS MACROMOLECULARES, PLURIEMPLEO E IMPLICACIONES EN ENFERMEDADES RARAS DE LOS MIEMBROS DE LA FAMILIA AMINOACIDO QUINASA/
dc.relation.projectID info:eu-repo/grantAgreement/GVA//PROMETEO09%2F2009%2F051/ES/Genes, proteínas y rutas de señalización en enfermedades raras (Biomeder)/
dc.rights.accessRights Abierto es_ES
dc.contributor.affiliation Universitat Politècnica de València. Instituto Universitario Mixto de Tecnología Química - Institut Universitari Mixt de Tecnologia Química es_ES
dc.description.bibliographicCitation Polo, LM.; Gil Ortíz, F.; Cantin Sanz, A.; Rubio, V. (2012). New Insight into the Transcarbamylase Family: TheStructure of Putrescine Transcarbamylase, a Key Catalystfor Fermentative Utilization of Agmatine. PLoS ONE. 7(2):31528-31543. https://doi.org/10.1371/journal.pone.0031528 es_ES
dc.description.accrualMethod S es_ES
dc.relation.publisherversion http://dx.doi.org/10.1371/journal.pone.0031528 es_ES
dc.description.upvformatpinicio 31528 es_ES
dc.description.upvformatpfin 31543 es_ES
dc.type.version info:eu-repo/semantics/publishedVersion es_ES
dc.description.volume 7 es_ES
dc.description.issue 2 es_ES
dc.relation.senia 239823
dc.identifier.pmid 22363663 en_EN
dc.identifier.pmcid PMC3282769 en_EN
dc.contributor.funder Ministerio de Ciencia e Innovación
dc.contributor.funder Generalitat Valenciana
dc.contributor.funder Banco Santander
dc.contributor.funder Consejo Superior de Investigaciones Científicas
dc.contributor.funder European Commission
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