Computational study on the role of residue Arg166 in alkaline phosphatases

Autores
Borosky, Gabriela Leonor
Año de publicación
2017
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Quantum chemical calculations were performed with the goal of achieving a better understanding of the influence of Arg166 on the catalytic activity of alkaline phosphatases. The present results indicate that the active site Arg166 residue contributes to catalysis by orienting the phosphate monoester substrate in a favorable position for the rate-limiting nucleophilic attack. The stabilizing hydrogen bond interactions of the guanidinium group with two nonbridging oxygens of the phosphate decrease the barrier for the phosphoryl transfer process by attainment of a tighter and preorganized transition state.
Fil: Borosky, Gabriela Leonor. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones en Físico-química de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Instituto de Investigaciones en Físico-química de Córdoba; Argentina
Materia
ENZYMATIC CATALYSIS
ONIOM CALCULATIONS
PHOSPHORYL TRANSFER
QUANTUM MECHANICS
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/64533
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/64533
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Computational study on the role of residue Arg166 in alkaline phosphatasesBorosky, Gabriela LeonorENZYMATIC CATALYSISONIOM CALCULATIONSPHOSPHORYL TRANSFERQUANTUM MECHANICShttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1Quantum chemical calculations were performed with the goal of achieving a better understanding of the influence of Arg166 on the catalytic activity of alkaline phosphatases. The present results indicate that the active site Arg166 residue contributes to catalysis by orienting the phosphate monoester substrate in a favorable position for the rate-limiting nucleophilic attack. The stabilizing hydrogen bond interactions of the guanidinium group with two nonbridging oxygens of the phosphate decrease the barrier for the phosphoryl transfer process by attainment of a tighter and preorganized transition state.Fil: Borosky, Gabriela Leonor. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones en Físico-química de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Instituto de Investigaciones en Físico-química de Córdoba; ArgentinaArkat USA2017-11info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/64533Borosky, Gabriela Leonor; Computational study on the role of residue Arg166 in alkaline phosphatases; Arkat USA; Arkivoc - Archive for Organic Chemistry; 2018; 2; 11-2017; 114-1211551-70041551-7012CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.24820/ark.5550190.p010.198info:eu-repo/semantics/altIdentifier/url/https://www.arkat-usa.org/arkivoc-journal/browse-arkivoc/ark.5550190.p010.198info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:08:31Zoai:ri.conicet.gov.ar:11336/64533instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 10:08:32.244CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Computational study on the role of residue Arg166 in alkaline phosphatases
title Computational study on the role of residue Arg166 in alkaline phosphatases
spellingShingle Computational study on the role of residue Arg166 in alkaline phosphatases
Borosky, Gabriela Leonor
ENZYMATIC CATALYSIS
ONIOM CALCULATIONS
PHOSPHORYL TRANSFER
QUANTUM MECHANICS
title_short Computational study on the role of residue Arg166 in alkaline phosphatases
title_full Computational study on the role of residue Arg166 in alkaline phosphatases
title_fullStr Computational study on the role of residue Arg166 in alkaline phosphatases
title_full_unstemmed Computational study on the role of residue Arg166 in alkaline phosphatases
title_sort Computational study on the role of residue Arg166 in alkaline phosphatases
dc.creator.none.fl_str_mv Borosky, Gabriela Leonor
author Borosky, Gabriela Leonor
author_facet Borosky, Gabriela Leonor
author_role author
dc.subject.none.fl_str_mv ENZYMATIC CATALYSIS
ONIOM CALCULATIONS
PHOSPHORYL TRANSFER
QUANTUM MECHANICS
topic ENZYMATIC CATALYSIS
ONIOM CALCULATIONS
PHOSPHORYL TRANSFER
QUANTUM MECHANICS
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Quantum chemical calculations were performed with the goal of achieving a better understanding of the influence of Arg166 on the catalytic activity of alkaline phosphatases. The present results indicate that the active site Arg166 residue contributes to catalysis by orienting the phosphate monoester substrate in a favorable position for the rate-limiting nucleophilic attack. The stabilizing hydrogen bond interactions of the guanidinium group with two nonbridging oxygens of the phosphate decrease the barrier for the phosphoryl transfer process by attainment of a tighter and preorganized transition state.
Fil: Borosky, Gabriela Leonor. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones en Físico-química de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Instituto de Investigaciones en Físico-química de Córdoba; Argentina
description Quantum chemical calculations were performed with the goal of achieving a better understanding of the influence of Arg166 on the catalytic activity of alkaline phosphatases. The present results indicate that the active site Arg166 residue contributes to catalysis by orienting the phosphate monoester substrate in a favorable position for the rate-limiting nucleophilic attack. The stabilizing hydrogen bond interactions of the guanidinium group with two nonbridging oxygens of the phosphate decrease the barrier for the phosphoryl transfer process by attainment of a tighter and preorganized transition state.
publishDate 2017
dc.date.none.fl_str_mv 2017-11
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/64533
Borosky, Gabriela Leonor; Computational study on the role of residue Arg166 in alkaline phosphatases; Arkat USA; Arkivoc - Archive for Organic Chemistry; 2018; 2; 11-2017; 114-121
1551-7004
1551-7012
CONICET Digital
CONICET
url http://hdl.handle.net/11336/64533
identifier_str_mv Borosky, Gabriela Leonor; Computational study on the role of residue Arg166 in alkaline phosphatases; Arkat USA; Arkivoc - Archive for Organic Chemistry; 2018; 2; 11-2017; 114-121
1551-7004
1551-7012
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.24820/ark.5550190.p010.198
info:eu-repo/semantics/altIdentifier/url/https://www.arkat-usa.org/arkivoc-journal/browse-arkivoc/ark.5550190.p010.198
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Arkat USA
publisher.none.fl_str_mv Arkat USA
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1844613954105507840
score 13.070432

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