Functional Analysis Of A Mosquito Short-Chain Dehydrogenase Cluster

Autores
Mayoral, Jaime G.; Leonard, Kate T.; Nouzova, Marcela; Noriega, Fernando G.; Defelipe, Lucas Alfredo; Turjanski, Adrian
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The short-chain dehydrogenases (SDR) constitute one of the oldest and largest families of enzymes with over 46,000 members in sequence databases. About 25% of all known dehydrogenases belong to the SDR family. SDR enzymes have critical roles in lipid, amino acid, carbohydrate, hormone, and xenobiotic metabolism as well as in redox sensor mechanisms. This family is present in archaea, bacteria, and eukaryota, emphasizing their versatility and fundamental importance for metabolic processes. We identified a cluster of eight SDRs in the mosquito Aedes aegypti (AaSDRs). Members of the cluster differ in tissue specificity and developmental expression. Heterologous expression produced recombinant proteins that had diverse substrate specificities, but distinct from the conventional insect alcohol (ethanol) dehydrogenases. They are all NADP+-dependent and they have S-enantioselectivity and preference for secondary alcohols with 8-15 carbons. Homology modeling was used to build the structure of AaSDR1 and two additional cluster members. The computational study helped explain the selectivity toward the (10S)-isomers as well as the reduced activity of AaSDR4 and AaSDR9 for longer isoprenoid substrates. Similar clusters of SDRs are present in other species of insects, suggesting similar selection mechanisms causing duplication and diversification of this family of enzymes.
Fil: Mayoral, Jaime G.. Florida International University; Estados Unidos
Fil: Leonard, Kate T.. Florida International University; Estados Unidos
Fil: Nouzova, Marcela. Florida International University; Estados Unidos
Fil: Noriega, Fernando G.. Florida International University; Estados Unidos
Fil: Defelipe, Lucas Alfredo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina
Fil: Turjanski, Adrian. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina
Materia
Aedes Aegypti
Alcohol
Farnesol
Juvenile Hormone
Mosquito
Short-Chain Dehydrogenase
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:11336/83666
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/83666
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Functional Analysis Of A Mosquito Short-Chain Dehydrogenase ClusterMayoral, Jaime G.Leonard, Kate T.Nouzova, MarcelaNoriega, Fernando G.Defelipe, Lucas AlfredoTurjanski, AdrianAedes AegyptiAlcoholFarnesolJuvenile HormoneMosquitoShort-Chain Dehydrogenasehttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The short-chain dehydrogenases (SDR) constitute one of the oldest and largest families of enzymes with over 46,000 members in sequence databases. About 25% of all known dehydrogenases belong to the SDR family. SDR enzymes have critical roles in lipid, amino acid, carbohydrate, hormone, and xenobiotic metabolism as well as in redox sensor mechanisms. This family is present in archaea, bacteria, and eukaryota, emphasizing their versatility and fundamental importance for metabolic processes. We identified a cluster of eight SDRs in the mosquito Aedes aegypti (AaSDRs). Members of the cluster differ in tissue specificity and developmental expression. Heterologous expression produced recombinant proteins that had diverse substrate specificities, but distinct from the conventional insect alcohol (ethanol) dehydrogenases. They are all NADP+-dependent and they have S-enantioselectivity and preference for secondary alcohols with 8-15 carbons. Homology modeling was used to build the structure of AaSDR1 and two additional cluster members. The computational study helped explain the selectivity toward the (10S)-isomers as well as the reduced activity of AaSDR4 and AaSDR9 for longer isoprenoid substrates. Similar clusters of SDRs are present in other species of insects, suggesting similar selection mechanisms causing duplication and diversification of this family of enzymes.Fil: Mayoral, Jaime G.. Florida International University; Estados UnidosFil: Leonard, Kate T.. Florida International University; Estados UnidosFil: Nouzova, Marcela. Florida International University; Estados UnidosFil: Noriega, Fernando G.. Florida International University; Estados UnidosFil: Defelipe, Lucas Alfredo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; ArgentinaFil: Turjanski, Adrian. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; ArgentinaWiley-liss, Div John Wiley & Sons Inc2013-02info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/83666Mayoral, Jaime G.; Leonard, Kate T.; Nouzova, Marcela; Noriega, Fernando G.; Defelipe, Lucas Alfredo; et al.; Functional Analysis Of A Mosquito Short-Chain Dehydrogenase Cluster; Wiley-liss, Div John Wiley & Sons Inc; Archives Of Insect Biochemistry And Physiology; 82; 2; 2-2013; 96-1150739-4462CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1002/arch.21078info:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/abs/10.1002/arch.21078info:eu-repo/semantics/altIdentifier/url/https://pubmed.ncbi.nlm.nih.gov/23238893/info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:50:03Zoai:ri.conicet.gov.ar:11336/83666instacron: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 09:50:04.188CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Functional Analysis Of A Mosquito Short-Chain Dehydrogenase Cluster
title Functional Analysis Of A Mosquito Short-Chain Dehydrogenase Cluster
spellingShingle Functional Analysis Of A Mosquito Short-Chain Dehydrogenase Cluster
Mayoral, Jaime G.
Aedes Aegypti
Alcohol
Farnesol
Juvenile Hormone
Mosquito
Short-Chain Dehydrogenase
title_short Functional Analysis Of A Mosquito Short-Chain Dehydrogenase Cluster
title_full Functional Analysis Of A Mosquito Short-Chain Dehydrogenase Cluster
title_fullStr Functional Analysis Of A Mosquito Short-Chain Dehydrogenase Cluster
title_full_unstemmed Functional Analysis Of A Mosquito Short-Chain Dehydrogenase Cluster
title_sort Functional Analysis Of A Mosquito Short-Chain Dehydrogenase Cluster
dc.creator.none.fl_str_mv Mayoral, Jaime G.
Leonard, Kate T.
Nouzova, Marcela
Noriega, Fernando G.
Defelipe, Lucas Alfredo
Turjanski, Adrian
author Mayoral, Jaime G.
author_facet Mayoral, Jaime G.
Leonard, Kate T.
Nouzova, Marcela
Noriega, Fernando G.
Defelipe, Lucas Alfredo
Turjanski, Adrian
author_role author
author2 Leonard, Kate T.
Nouzova, Marcela
Noriega, Fernando G.
Defelipe, Lucas Alfredo
Turjanski, Adrian
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Aedes Aegypti
Alcohol
Farnesol
Juvenile Hormone
Mosquito
Short-Chain Dehydrogenase
topic Aedes Aegypti
Alcohol
Farnesol
Juvenile Hormone
Mosquito
Short-Chain Dehydrogenase
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The short-chain dehydrogenases (SDR) constitute one of the oldest and largest families of enzymes with over 46,000 members in sequence databases. About 25% of all known dehydrogenases belong to the SDR family. SDR enzymes have critical roles in lipid, amino acid, carbohydrate, hormone, and xenobiotic metabolism as well as in redox sensor mechanisms. This family is present in archaea, bacteria, and eukaryota, emphasizing their versatility and fundamental importance for metabolic processes. We identified a cluster of eight SDRs in the mosquito Aedes aegypti (AaSDRs). Members of the cluster differ in tissue specificity and developmental expression. Heterologous expression produced recombinant proteins that had diverse substrate specificities, but distinct from the conventional insect alcohol (ethanol) dehydrogenases. They are all NADP+-dependent and they have S-enantioselectivity and preference for secondary alcohols with 8-15 carbons. Homology modeling was used to build the structure of AaSDR1 and two additional cluster members. The computational study helped explain the selectivity toward the (10S)-isomers as well as the reduced activity of AaSDR4 and AaSDR9 for longer isoprenoid substrates. Similar clusters of SDRs are present in other species of insects, suggesting similar selection mechanisms causing duplication and diversification of this family of enzymes.
Fil: Mayoral, Jaime G.. Florida International University; Estados Unidos
Fil: Leonard, Kate T.. Florida International University; Estados Unidos
Fil: Nouzova, Marcela. Florida International University; Estados Unidos
Fil: Noriega, Fernando G.. Florida International University; Estados Unidos
Fil: Defelipe, Lucas Alfredo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina
Fil: Turjanski, Adrian. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina
description The short-chain dehydrogenases (SDR) constitute one of the oldest and largest families of enzymes with over 46,000 members in sequence databases. About 25% of all known dehydrogenases belong to the SDR family. SDR enzymes have critical roles in lipid, amino acid, carbohydrate, hormone, and xenobiotic metabolism as well as in redox sensor mechanisms. This family is present in archaea, bacteria, and eukaryota, emphasizing their versatility and fundamental importance for metabolic processes. We identified a cluster of eight SDRs in the mosquito Aedes aegypti (AaSDRs). Members of the cluster differ in tissue specificity and developmental expression. Heterologous expression produced recombinant proteins that had diverse substrate specificities, but distinct from the conventional insect alcohol (ethanol) dehydrogenases. They are all NADP+-dependent and they have S-enantioselectivity and preference for secondary alcohols with 8-15 carbons. Homology modeling was used to build the structure of AaSDR1 and two additional cluster members. The computational study helped explain the selectivity toward the (10S)-isomers as well as the reduced activity of AaSDR4 and AaSDR9 for longer isoprenoid substrates. Similar clusters of SDRs are present in other species of insects, suggesting similar selection mechanisms causing duplication and diversification of this family of enzymes.
publishDate 2013
dc.date.none.fl_str_mv 2013-02
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/11336/83666
Mayoral, Jaime G.; Leonard, Kate T.; Nouzova, Marcela; Noriega, Fernando G.; Defelipe, Lucas Alfredo; et al.; Functional Analysis Of A Mosquito Short-Chain Dehydrogenase Cluster; Wiley-liss, Div John Wiley & Sons Inc; Archives Of Insect Biochemistry And Physiology; 82; 2; 2-2013; 96-115
0739-4462
CONICET Digital
CONICET
url http://hdl.handle.net/11336/83666
identifier_str_mv Mayoral, Jaime G.; Leonard, Kate T.; Nouzova, Marcela; Noriega, Fernando G.; Defelipe, Lucas Alfredo; et al.; Functional Analysis Of A Mosquito Short-Chain Dehydrogenase Cluster; Wiley-liss, Div John Wiley & Sons Inc; Archives Of Insect Biochemistry And Physiology; 82; 2; 2-2013; 96-115
0739-4462
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1002/arch.21078
info:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/abs/10.1002/arch.21078
info:eu-repo/semantics/altIdentifier/url/https://pubmed.ncbi.nlm.nih.gov/23238893/
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
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Wiley-liss, Div John Wiley & Sons Inc
publisher.none.fl_str_mv Wiley-liss, Div John Wiley & Sons Inc
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
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score 13.070432

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