Interaction of N-succinyl-diaminopimelate desuccinylase with flavonoids

DapE is an enzyme that belongs to the meso-diaminopimelate/Lysine pathway. It is recognized as an antimicrobial target, hence compounds that inhibit its catalytic activity are required. The principal features considered in the selection of potential inhibitors for this enzyme are compounds containin...

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Autores: Manuel Terrazas-Lopez, Naun Lobo, Emilio Alvarez_Parrilla, Laura A. de la Rosa, Alejandro Martinez_Martinez, Luis G. Aguirre-Reyes, Jorge L. Cuen-Andrade, Angel Díaz_Sanchez
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2020
País:México
Institución:Universidad Autónoma de Ciudad Juárez
Repositorio:Repositorio Institucional de la Universidad Autónoma de Ciudad Juárez
OAI Identifier:oai:uacj.mx:oai:cathi.uacj.mx:20.500.11961ir-15939
Acceso en línea:https://doi.org/10.1016/j.biochi.2020.08.016
Access Level:acceso abierto
Palabra clave:N-succinyl-diaminopimelate desuccinylase
M20 peptidases
Metal binding groups
Flavonoids
Molecular docking
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spelling Interaction of N-succinyl-diaminopimelate desuccinylase with flavonoidsManuel Terrazas-LopezNaun LoboEmilio Alvarez_ParrillaLaura A. de la RosaAlejandro Martinez_MartinezLuis G. Aguirre-ReyesJorge L. Cuen-AndradeAngel Díaz_SanchezN-succinyl-diaminopimelate desuccinylaseM20 peptidasesMetal binding groupsFlavonoidsMolecular dockinginfo:eu-repo/classification/cti/2DapE is an enzyme that belongs to the meso-diaminopimelate/Lysine pathway. It is recognized as an antimicrobial target, hence compounds that inhibit its catalytic activity are required. The principal features considered in the selection of potential inhibitors for this enzyme are compounds containing metal binding groups that could block access of the substrate to the Zinc metal centers and/or block the assembly of the oxyanion hole. We show the interaction of DapE from Enterococcus faecium, Staphylococcus aureus, Klebsiella aerogenes, Pseudomonas aeruginosa and Escherichia coli with flavonoids: quercetin, catechin, luteolin, rutin and hesperidin. Flavonoids contain several oxygen atoms distributed along their structure in a pattern that may be considered for the development of new antibiotics. Docking experiments suggest that these compounds containing metal binding groups that interact with metal centers of DapE and binding experiments indicate that glycoside flavonoids are preferred by DapE.Manuel Terrazas-LopezNaun Lobo GaloEmilio Alvarez-ParrillaLaura A. de la RosaAlejandro Martinez-MartinezLuis G. Aguirre-ReyesJorge L. Cuen-Andrade2020info:eu-repo/semantics/articleArtículoinfo:eu-repo/semantics/publishedVersionhttps://doi.org/10.1016/j.biochi.2020.08.016reponame:Repositorio Institucional de la Universidad Autónoma de Ciudad Juárezinstname:Universidad Autónoma de Ciudad Juárezinstacron:UACJEnglishinfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc/4.0oai:uacj.mx:oai:cathi.uacj.mx:20.500.11961ir-159392025-11-26T19:46:58Z
dc.title.none.fl_str_mv Interaction of N-succinyl-diaminopimelate desuccinylase with flavonoids
title Interaction of N-succinyl-diaminopimelate desuccinylase with flavonoids
spellingShingle Interaction of N-succinyl-diaminopimelate desuccinylase with flavonoids
Manuel Terrazas-Lopez
N-succinyl-diaminopimelate desuccinylase
M20 peptidases
Metal binding groups
Flavonoids
Molecular docking
info:eu-repo/classification/cti/2
title_short Interaction of N-succinyl-diaminopimelate desuccinylase with flavonoids
title_full Interaction of N-succinyl-diaminopimelate desuccinylase with flavonoids
title_fullStr Interaction of N-succinyl-diaminopimelate desuccinylase with flavonoids
title_full_unstemmed Interaction of N-succinyl-diaminopimelate desuccinylase with flavonoids
title_sort Interaction of N-succinyl-diaminopimelate desuccinylase with flavonoids
dc.creator.none.fl_str_mv Manuel Terrazas-Lopez
Naun Lobo
Emilio Alvarez_Parrilla
Laura A. de la Rosa
Alejandro Martinez_Martinez
Luis G. Aguirre-Reyes
Jorge L. Cuen-Andrade
Angel Díaz_Sanchez
author Manuel Terrazas-Lopez
author_facet Manuel Terrazas-Lopez
Naun Lobo
Emilio Alvarez_Parrilla
Laura A. de la Rosa
Alejandro Martinez_Martinez
Luis G. Aguirre-Reyes
Jorge L. Cuen-Andrade
Angel Díaz_Sanchez
author_role author
author2 Naun Lobo
Emilio Alvarez_Parrilla
Laura A. de la Rosa
Alejandro Martinez_Martinez
Luis G. Aguirre-Reyes
Jorge L. Cuen-Andrade
Angel Díaz_Sanchez
author2_role author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Manuel Terrazas-Lopez
Naun Lobo Galo
Emilio Alvarez-Parrilla
Laura A. de la Rosa
Alejandro Martinez-Martinez
Luis G. Aguirre-Reyes
Jorge L. Cuen-Andrade
dc.subject.none.fl_str_mv N-succinyl-diaminopimelate desuccinylase
M20 peptidases
Metal binding groups
Flavonoids
Molecular docking
info:eu-repo/classification/cti/2
topic N-succinyl-diaminopimelate desuccinylase
M20 peptidases
Metal binding groups
Flavonoids
Molecular docking
info:eu-repo/classification/cti/2
description DapE is an enzyme that belongs to the meso-diaminopimelate/Lysine pathway. It is recognized as an antimicrobial target, hence compounds that inhibit its catalytic activity are required. The principal features considered in the selection of potential inhibitors for this enzyme are compounds containing metal binding groups that could block access of the substrate to the Zinc metal centers and/or block the assembly of the oxyanion hole. We show the interaction of DapE from Enterococcus faecium, Staphylococcus aureus, Klebsiella aerogenes, Pseudomonas aeruginosa and Escherichia coli with flavonoids: quercetin, catechin, luteolin, rutin and hesperidin. Flavonoids contain several oxygen atoms distributed along their structure in a pattern that may be considered for the development of new antibiotics. Docking experiments suggest that these compounds containing metal binding groups that interact with metal centers of DapE and binding experiments indicate that glycoside flavonoids are preferred by DapE.
publishDate 2020
dc.date.none.fl_str_mv 2020
dc.type.none.fl_str_mv info:eu-repo/semantics/article
Artículo
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://doi.org/10.1016/j.biochi.2020.08.016
url https://doi.org/10.1016/j.biochi.2020.08.016
dc.language.none.fl_str_mv English
language_invalid_str_mv English
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc/4.0
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc/4.0
dc.source.none.fl_str_mv reponame:Repositorio Institucional de la Universidad Autónoma de Ciudad Juárez
instname:Universidad Autónoma de Ciudad Juárez
instacron:UACJ
instname_str Universidad Autónoma de Ciudad Juárez
instacron_str UACJ
institution UACJ
reponame_str Repositorio Institucional de la Universidad Autónoma de Ciudad Juárez
collection Repositorio Institucional de la Universidad Autónoma de Ciudad Juárez
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15.812429

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