Glycerol-3-Phosphate Dehydrogenase Isozymes: A computational approach to their metabolic roles in the flight muscles of triatoma infestans

Autores
Stroppa, Maria Mercedes; Cossy Isasi, Sadí
Año de publicación
2018
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
6 páginas
Fil: Stroppa, Maria Mercedes. Universidad Nacional de Córdoba. Facultad de Ciencias Médicas. Cátedra de Bioquímica y Biología Molecular; Argentina.
Fil: Cossy Isasi, Sadí. Universidad Nacional de Córdoba. Facultad de Ciencias Médicas. Cátedra de Bioquímica y Biología Molecular; Argentina.
Glycerol-3-phosphate dehydrogenase (GPDH) isoenzymes play different roles in Triatoma infestans flight metabolism and only differ in the C-terminal end. We studied with computational models their dynamics and interactions. Homology-modeling dynamics showed models close to minimal energy with amino acid distribution similar to crystallized structures. Radius of gyration decrease because the models presented well fitted folded structures with solvation free energy of non-polar groups increased with temperature. Heat maps suggested the need to form dimeric structures to preserve activity or that temperature could be an activity modulator. Modeled dimeric structures were similar to crystallized references and didn´t involve the C-terminals in their conformation. Docking studies of the C-terminals showed interaction between GPDH-1 and actin co-localized with glycolytic enzymes. GPDH-2 peptide could bind to model membranes and be substrate for lysine-acetyltransferases. Consequently, C-terminals could determine the sub-cellular localization and the metabolic functions in lipid biosynthesis or ATP generation.
info:eu-repo/semantics/publishedVersion
Fil: Stroppa, Maria Mercedes. Universidad Nacional de Córdoba. Facultad de Ciencias Médicas. Cátedra de Bioquímica y Biología Molecular; Argentina.
Fil: Cossy Isasi, Sadí. Universidad Nacional de Córdoba. Facultad de Ciencias Médicas. Cátedra de Bioquímica y Biología Molecular; Argentina.
Bioquímica y Biología Molecular (ídem 3.1.10)
Materia
Docking
Triatoma Infestans
Molecular Modeling and Dynamics
Localization
Gpdh Isoforms
Nivel de accesibilidad
acceso abierto
Condiciones de uso
Repositorio
Repositorio Digital Universitario (UNC)
Institución
Universidad Nacional de Córdoba
OAI Identificador
oai:rdu.unc.edu.ar:11086/555572
Acceder
id RDUUNC_126a2dc0a7a830e717efe1cd736342fc
oai_identifier_str oai:rdu.unc.edu.ar:11086/555572
network_acronym_str RDUUNC
repository_id_str 2572
network_name_str Repositorio Digital Universitario (UNC)
spelling Glycerol-3-Phosphate Dehydrogenase Isozymes: A computational approach to their metabolic roles in the flight muscles of triatoma infestansStroppa, Maria MercedesCossy Isasi, SadíDockingTriatoma InfestansMolecular Modeling and DynamicsLocalizationGpdh Isoforms6 páginasFil: Stroppa, Maria Mercedes. Universidad Nacional de Córdoba. Facultad de Ciencias Médicas. Cátedra de Bioquímica y Biología Molecular; Argentina.Fil: Cossy Isasi, Sadí. Universidad Nacional de Córdoba. Facultad de Ciencias Médicas. Cátedra de Bioquímica y Biología Molecular; Argentina.Glycerol-3-phosphate dehydrogenase (GPDH) isoenzymes play different roles in Triatoma infestans flight metabolism and only differ in the C-terminal end. We studied with computational models their dynamics and interactions. Homology-modeling dynamics showed models close to minimal energy with amino acid distribution similar to crystallized structures. Radius of gyration decrease because the models presented well fitted folded structures with solvation free energy of non-polar groups increased with temperature. Heat maps suggested the need to form dimeric structures to preserve activity or that temperature could be an activity modulator. Modeled dimeric structures were similar to crystallized references and didn´t involve the C-terminals in their conformation. Docking studies of the C-terminals showed interaction between GPDH-1 and actin co-localized with glycolytic enzymes. GPDH-2 peptide could bind to model membranes and be substrate for lysine-acetyltransferases. Consequently, C-terminals could determine the sub-cellular localization and the metabolic functions in lipid biosynthesis or ATP generation.info:eu-repo/semantics/publishedVersionFil: Stroppa, Maria Mercedes. Universidad Nacional de Córdoba. Facultad de Ciencias Médicas. Cátedra de Bioquímica y Biología Molecular; Argentina.Fil: Cossy Isasi, Sadí. Universidad Nacional de Córdoba. Facultad de Ciencias Médicas. Cátedra de Bioquímica y Biología Molecular; Argentina.Bioquímica y Biología Molecular (ídem 3.1.10)2018info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfCossy Isasi, Sadí; Stroppa, Maria Mercedes; Glycerol-3-Phosphate Dehydrogenase Isozymes: A computational approach to their metabolic roles in the flight muscles of triatoma infestans; International Organization Of Scientific Research; Journal of Pharmacy and Biological Sciences; 2-20182278-3008http://hdl.handle.net/11086/5555722319-767610.9790/3008-1301014550enginfo:eu-repo/semantics/openAccessreponame:Repositorio Digital Universitario (UNC)instname:Universidad Nacional de Córdobainstacron:UNC2025-10-16T09:31:31Zoai:rdu.unc.edu.ar:11086/555572Institucionalhttps://rdu.unc.edu.ar/Universidad públicaNo correspondehttp://rdu.unc.edu.ar/oai/snrdoca.unc@gmail.comArgentinaNo correspondeNo correspondeNo correspondeopendoar:25722025-10-16 09:31:31.464Repositorio Digital Universitario (UNC) - Universidad Nacional de Córdobafalse
dc.title.none.fl_str_mv Glycerol-3-Phosphate Dehydrogenase Isozymes: A computational approach to their metabolic roles in the flight muscles of triatoma infestans
title Glycerol-3-Phosphate Dehydrogenase Isozymes: A computational approach to their metabolic roles in the flight muscles of triatoma infestans
spellingShingle Glycerol-3-Phosphate Dehydrogenase Isozymes: A computational approach to their metabolic roles in the flight muscles of triatoma infestans
Stroppa, Maria Mercedes
Docking
Triatoma Infestans
Molecular Modeling and Dynamics
Localization
Gpdh Isoforms
title_short Glycerol-3-Phosphate Dehydrogenase Isozymes: A computational approach to their metabolic roles in the flight muscles of triatoma infestans
title_full Glycerol-3-Phosphate Dehydrogenase Isozymes: A computational approach to their metabolic roles in the flight muscles of triatoma infestans
title_fullStr Glycerol-3-Phosphate Dehydrogenase Isozymes: A computational approach to their metabolic roles in the flight muscles of triatoma infestans
title_full_unstemmed Glycerol-3-Phosphate Dehydrogenase Isozymes: A computational approach to their metabolic roles in the flight muscles of triatoma infestans
title_sort Glycerol-3-Phosphate Dehydrogenase Isozymes: A computational approach to their metabolic roles in the flight muscles of triatoma infestans
dc.creator.none.fl_str_mv Stroppa, Maria Mercedes
Cossy Isasi, Sadí
author Stroppa, Maria Mercedes
author_facet Stroppa, Maria Mercedes
Cossy Isasi, Sadí
author_role author
author2 Cossy Isasi, Sadí
author2_role author
dc.subject.none.fl_str_mv Docking
Triatoma Infestans
Molecular Modeling and Dynamics
Localization
Gpdh Isoforms
topic Docking
Triatoma Infestans
Molecular Modeling and Dynamics
Localization
Gpdh Isoforms
dc.description.none.fl_txt_mv 6 páginas
Fil: Stroppa, Maria Mercedes. Universidad Nacional de Córdoba. Facultad de Ciencias Médicas. Cátedra de Bioquímica y Biología Molecular; Argentina.
Fil: Cossy Isasi, Sadí. Universidad Nacional de Córdoba. Facultad de Ciencias Médicas. Cátedra de Bioquímica y Biología Molecular; Argentina.
Glycerol-3-phosphate dehydrogenase (GPDH) isoenzymes play different roles in Triatoma infestans flight metabolism and only differ in the C-terminal end. We studied with computational models their dynamics and interactions. Homology-modeling dynamics showed models close to minimal energy with amino acid distribution similar to crystallized structures. Radius of gyration decrease because the models presented well fitted folded structures with solvation free energy of non-polar groups increased with temperature. Heat maps suggested the need to form dimeric structures to preserve activity or that temperature could be an activity modulator. Modeled dimeric structures were similar to crystallized references and didn´t involve the C-terminals in their conformation. Docking studies of the C-terminals showed interaction between GPDH-1 and actin co-localized with glycolytic enzymes. GPDH-2 peptide could bind to model membranes and be substrate for lysine-acetyltransferases. Consequently, C-terminals could determine the sub-cellular localization and the metabolic functions in lipid biosynthesis or ATP generation.
info:eu-repo/semantics/publishedVersion
Fil: Stroppa, Maria Mercedes. Universidad Nacional de Córdoba. Facultad de Ciencias Médicas. Cátedra de Bioquímica y Biología Molecular; Argentina.
Fil: Cossy Isasi, Sadí. Universidad Nacional de Córdoba. Facultad de Ciencias Médicas. Cátedra de Bioquímica y Biología Molecular; Argentina.
Bioquímica y Biología Molecular (ídem 3.1.10)
description 6 páginas
publishDate 2018
dc.date.none.fl_str_mv 2018
dc.type.none.fl_str_mv info:eu-repo/semantics/publishedVersion
info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
status_str publishedVersion
format article
dc.identifier.none.fl_str_mv Cossy Isasi, Sadí; Stroppa, Maria Mercedes; Glycerol-3-Phosphate Dehydrogenase Isozymes: A computational approach to their metabolic roles in the flight muscles of triatoma infestans; International Organization Of Scientific Research; Journal of Pharmacy and Biological Sciences; 2-2018
2278-3008
http://hdl.handle.net/11086/555572
2319-7676
10.9790/3008-1301014550
identifier_str_mv Cossy Isasi, Sadí; Stroppa, Maria Mercedes; Glycerol-3-Phosphate Dehydrogenase Isozymes: A computational approach to their metabolic roles in the flight muscles of triatoma infestans; International Organization Of Scientific Research; Journal of Pharmacy and Biological Sciences; 2-2018
2278-3008
2319-7676
10.9790/3008-1301014550
url http://hdl.handle.net/11086/555572
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:Repositorio Digital Universitario (UNC)
instname:Universidad Nacional de Córdoba
instacron:UNC
reponame_str Repositorio Digital Universitario (UNC)
collection Repositorio Digital Universitario (UNC)
instname_str Universidad Nacional de Córdoba
instacron_str UNC
institution UNC
repository.name.fl_str_mv Repositorio Digital Universitario (UNC) - Universidad Nacional de Córdoba
repository.mail.fl_str_mv oca.unc@gmail.com
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score 12.712165

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