Mostrar el registro sencillo del ítem
dc.contributor.author
Correia, Hugo D.
dc.contributor.author
Marangon, Jacopo
dc.contributor.author
Brondino, Carlos Dante
![Se ha confirmado la validez de este valor de autoridad por un usuario](/themes/CONICETDigital/images/authority_control/invisible.gif)
dc.contributor.author
Moura, Jose J. G.
dc.contributor.author
Romão, Maria J.
dc.contributor.author
González, Pablo Javier
![Se ha confirmado la validez de este valor de autoridad por un usuario](/themes/CONICETDigital/images/authority_control/invisible.gif)
dc.contributor.author
Santos Silva, Teresa
![Se ha confirmado la validez de este valor de autoridad por un usuario](/themes/CONICETDigital/images/authority_control/invisible.gif)
dc.date.available
2018-04-09T18:10:50Z
dc.date.issued
2015-03
dc.identifier.citation
Correia, Hugo D.; Marangon, Jacopo; Brondino, Carlos Dante; Moura, Jose J. G.; Romão, Maria J.; et al.; Aromatic aldehydes at the active site of aldehyde oxidoreductase from Desulfovibrio gigas: reactivity and molecular details of the enzyme–substrate and enzyme–product interaction; Springer; Journal of Biological Inorganic Chemistry; 20; 2; 3-2015; 219-229
dc.identifier.issn
0949-8257
dc.identifier.uri
http://hdl.handle.net/11336/41360
dc.description.abstract
Desulfovibrio gigas aldehyde oxidoreductase (DgAOR) is a mononuclear molybdenum-containing enzyme from the xanthine oxidase (XO) family, a group of enzymes capable of catalyzing the oxidative hydroxylation of aldehydes and heterocyclic compounds. The kinetic studies reported in this work showed that DgAOR catalyzes the oxidative hydroxylation of aromatic aldehydes, but not heterocyclic compounds. NMR spectroscopy studies using 13C-labeled benzaldehyde confirmed that DgAOR catalyzes the conversion of aldehydes to the respective carboxylic acids. Steady-state kinetics in solution showed that high concentrations of the aromatic aldehydes produce substrate inhibition and in the case of 3-phenyl propionaldehyde a suicide substrate behavior. Hydroxyl-substituted aromatic aldehydes present none of these behaviors but the kinetic parameters are largely affected by the position of the OH group. High-resolution crystallographic structures obtained from single crystals of active-DgAOR soaked with benzaldehyde showed that the side chains of Phe425 and Tyr535 are important for the stabilization of the substrate in the active site. On the other hand, the X-ray data of DgAOR soaked with trans-cinnamaldehyde showed a cinnamic acid molecule in the substrate channel. The X-ray data of DgAOR soaked with 3-phenyl propionaldehyde showed clearly how high substrate concentrations inactivate the enzyme by binding covalently at the surface of the enzyme and blocking the substrate channel. The different reactivity of DgAOR versus aldehyde oxidase and XO towards aromatic aldehydes and N-heterocyclic compounds is explained on the basis of the present kinetic and structural data.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Springer
![Se ha confirmado la validez de este valor de autoridad por un usuario](/themes/CONICETDigital/images/authority_control/invisible.gif)
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Aldehyde Oxidoreductase
dc.subject
Molybdenum
dc.subject
X-Ray Crystallography
dc.subject
Enzyme Kinetics
dc.subject
Suicide Substrate
dc.subject.classification
Otras Ciencias Biológicas
![Se ha confirmado la validez de este valor de autoridad por un usuario](/themes/CONICETDigital/images/authority_control/invisible.gif)
dc.subject.classification
Ciencias Biológicas
![Se ha confirmado la validez de este valor de autoridad por un usuario](/themes/CONICETDigital/images/authority_control/invisible.gif)
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
![Se ha confirmado la validez de este valor de autoridad por un usuario](/themes/CONICETDigital/images/authority_control/invisible.gif)
dc.title
Aromatic aldehydes at the active site of aldehyde oxidoreductase from Desulfovibrio gigas: reactivity and molecular details of the enzyme–substrate and enzyme–product interaction
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-03-26T18:15:19Z
dc.journal.volume
20
dc.journal.number
2
dc.journal.pagination
219-229
dc.journal.pais
Alemania
![Se ha confirmado la validez de este valor de autoridad por un usuario](/themes/CONICETDigital/images/authority_control/invisible.gif)
dc.journal.ciudad
Berlin
dc.description.fil
Fil: Correia, Hugo D.. Universidade Nova de Lisboa; Portugal
dc.description.fil
Fil: Marangon, Jacopo. Universidade Nova de Lisboa; Portugal
dc.description.fil
Fil: Brondino, Carlos Dante. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Física; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina
dc.description.fil
Fil: Moura, Jose J. G.. Universidade Nova de Lisboa; Portugal
dc.description.fil
Fil: Romão, Maria J.. Universidade Nova de Lisboa; Portugal
dc.description.fil
Fil: González, Pablo Javier. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Física; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina
dc.description.fil
Fil: Santos Silva, Teresa. Universidade Nova de Lisboa; Portugal
dc.journal.title
Journal of Biological Inorganic Chemistry
![Se ha confirmado la validez de este valor de autoridad por un usuario](/themes/CONICETDigital/images/authority_control/invisible.gif)
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://link.springer.com/article/10.1007%2Fs00775-014-1196-4
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1007/s00775-014-1196-4
Archivos asociados