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10.1016/j.bbagen.2019.03.017
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Campo DC | Valor | Lengua/Idioma |
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dc.contributor.author | Gallego Jara, Julia | - |
dc.contributor.author | Lozano Terol, Gema | - |
dc.contributor.author | Écija Conesa, Ana | - |
dc.contributor.author | Zambelli, Barbara | - |
dc.contributor.author | Cánovas Díaz, Manuel | - |
dc.contributor.author | de Diego Puente, Teresa | - |
dc.contributor.other | Department of Biochemistry and Molecular Biology and Immunology (B), Faculty of Chemistry, University of Murcia | es |
dc.date.accessioned | 2021-11-03T17:19:34Z | - |
dc.date.available | 2021-11-03T17:19:34Z | - |
dc.date.issued | 2019 | - |
dc.identifier.citation | BBA - General Subjects | es |
dc.identifier.issn | 0304-4165 | - |
dc.identifier.uri | http://hdl.handle.net/10201/113648 | - |
dc.description.abstract | Background The superfamily of adenylating enzymes is a large family of enzymes broadly distributed from bacteria to humans. Acetyl-CoA synthetase (Acs), member of this family, is a metabolic enzyme with an essential role in Escherichia coli (E. coli) acetate metabolism, whose catalytic activity is regulated by acetylation/deacetylation in vivo. Methods In this study, the kinetics and thermodynamic parameters of deacetylated and acetylated E. coli Acs were studied for the adenylating step. Moreover, the role of the T264, K270, D500 and K609 residues in catalysis and ATP-binding was also determined by Isothermal titration calorimetry. Results The results showed that native Acs enzyme binds ATP in an endothermic way. The dissociation constant has been determined and ATP-binding showed no significant differences between acetylated and deacetylated enzyme, although kcat was much higher for the deacetylated enzyme. However, K609 lysine mutation resulted in an increase in ATP-Acs-affinity and in a total loss of enzymatic activity, while T264 and D500 mutant proteins showed a total loss of ATP-binding ability and a decrease in catalytic activity. K609 site-specified acetylation induced a change in Acs conformation which resulted in an exothermic and more energetic ATP-binding. Conclusions The differences in ATP-binding could explain the broadly conserved inactivation of Acs when K609 is acetylated. General Significance The results presented in this study demonstrate the importance of the selected residues in Acs ATP-binding and represent an advance in our understanding of the adenylation step of the superfamily of adenylating enzymes and of their acetylation/deacetylation regulation. | es |
dc.format | application/pdf | es |
dc.format.extent | 28 | es |
dc.language | eng | es |
dc.publisher | Elsevier | es |
dc.relation | Nombre del proyecto: Biología de Sistemas y sintética de la acetilación-desacetilación del proteoma de E. coli. Código: BIO2014-54411-C2-1-R. Agencia/entidad financiadora: Ministerio de Economía y Competitividad. Ámbito Nacional. Proyectos de I+D+I, del programa estatal de investigación, desarrollo e innovación orientada a los retos de la sociedad. Convocatoria 2014. Nombre del proyecto: Biotecnología de Sistemas para la mejora de bioprocesos relacionados con el metabolismo central de E. coli: integracion de la regulación transcripcional y post-traduccional en la produccion de terpenos. Código: 19236/PI/14. Agencia/entidad financiadora: Fundación Séneca. Ayudas a la realización de proyectos para el desarrollo de investigación científica y técnica por grupos competitivos. Ámbito regional. Convocatoria 2014. | es |
dc.rights | info:eu-repo/semantics/openAccess | es |
dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 Internacional | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | * |
dc.subject | Escherichia col | es |
dc.subject | Acetyl-CoA synthetase | es |
dc.subject | ITC | es |
dc.subject | ATP | es |
dc.subject | lysine acetylation | es |
dc.subject.other | - Biología::577 - Bioquímica. Biología molecular. Biofísica | es |
dc.title | Characterization of acetyl-CoA synthetase kinetics and ATP-binding | es |
dc.type | info:eu-repo/semantics/article | es |
dc.relation.publisherversion | https://www.sciencedirect.com/science/article/pii/S030441651930073X | es |
dc.identifier.doi | 10.1016/j.bbagen.2019.03.017 | - |
Aparece en las colecciones: | Artículos: Bioquímica y Biología Molecular "B" e Inmunología |
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