Functional Analysis Of A Mosquito Short-Chain Dehydrogenase Cluster

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 xenobioti...

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Autores principales:	Defelipe, Lucas Alfredo, Turjanski, Adrián Gustavo
Publicado:	2013
Materias:	Aedes aegypti Alcohol Farnesol Juvenile hormone Mosquito Short-chain dehydrogenase insect protein oxidoreductase RNA Aedes amino acid sequence animal antibody specificity article biology chemistry enzyme specificity enzymology gene expression regulation metabolism molecular docking phylogeny polymerase chain reaction sequence alignment spectrophotometry Amino Acid Sequence Animals Computational Biology Gene Expression Regulation Insect Proteins Molecular Docking Simulation Organ Specificity Oxidoreductases Phylogeny Polymerase Chain Reaction Sequence Alignment Spectrophotometry Substrate Specificity Archaea Bacteria (microorganisms) Eukaryota Hexapoda
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_07394462_v82_n2_p96_Mayoral http://hdl.handle.net/20.500.12110/paper_07394462_v82_n2_p96_Mayoral
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_07394462_v82_n2_p96_Mayoral
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spelling	paper:paper_07394462_v82_n2_p96_Mayoral2023-06-08T15:44:24Z Functional Analysis Of A Mosquito Short-Chain Dehydrogenase Cluster Defelipe, Lucas Alfredo Turjanski, Adrián Gustavo Aedes aegypti Alcohol Farnesol Juvenile hormone Mosquito Short-chain dehydrogenase insect protein oxidoreductase RNA Aedes amino acid sequence animal antibody specificity article biology chemistry enzyme specificity enzymology gene expression regulation metabolism molecular docking phylogeny polymerase chain reaction sequence alignment spectrophotometry Aedes Amino Acid Sequence Animals Computational Biology Gene Expression Regulation Insect Proteins Molecular Docking Simulation Organ Specificity Oxidoreductases Phylogeny Polymerase Chain Reaction RNA Sequence Alignment Spectrophotometry Substrate Specificity Aedes aegypti Archaea Bacteria (microorganisms) Eukaryota Hexapoda 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. © 2012 Wiley Periodicals, Inc. Fil:Defelipe, L.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Turjanski, A.G. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2013 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_07394462_v82_n2_p96_Mayoral http://hdl.handle.net/20.500.12110/paper_07394462_v82_n2_p96_Mayoral
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	Aedes aegypti Alcohol Farnesol Juvenile hormone Mosquito Short-chain dehydrogenase insect protein oxidoreductase RNA Aedes amino acid sequence animal antibody specificity article biology chemistry enzyme specificity enzymology gene expression regulation metabolism molecular docking phylogeny polymerase chain reaction sequence alignment spectrophotometry Aedes Amino Acid Sequence Animals Computational Biology Gene Expression Regulation Insect Proteins Molecular Docking Simulation Organ Specificity Oxidoreductases Phylogeny Polymerase Chain Reaction RNA Sequence Alignment Spectrophotometry Substrate Specificity Aedes aegypti Archaea Bacteria (microorganisms) Eukaryota Hexapoda
spellingShingle	Aedes aegypti Alcohol Farnesol Juvenile hormone Mosquito Short-chain dehydrogenase insect protein oxidoreductase RNA Aedes amino acid sequence animal antibody specificity article biology chemistry enzyme specificity enzymology gene expression regulation metabolism molecular docking phylogeny polymerase chain reaction sequence alignment spectrophotometry Aedes Amino Acid Sequence Animals Computational Biology Gene Expression Regulation Insect Proteins Molecular Docking Simulation Organ Specificity Oxidoreductases Phylogeny Polymerase Chain Reaction RNA Sequence Alignment Spectrophotometry Substrate Specificity Aedes aegypti Archaea Bacteria (microorganisms) Eukaryota Hexapoda Defelipe, Lucas Alfredo Turjanski, Adrián Gustavo Functional Analysis Of A Mosquito Short-Chain Dehydrogenase Cluster
topic_facet	Aedes aegypti Alcohol Farnesol Juvenile hormone Mosquito Short-chain dehydrogenase insect protein oxidoreductase RNA Aedes amino acid sequence animal antibody specificity article biology chemistry enzyme specificity enzymology gene expression regulation metabolism molecular docking phylogeny polymerase chain reaction sequence alignment spectrophotometry Aedes Amino Acid Sequence Animals Computational Biology Gene Expression Regulation Insect Proteins Molecular Docking Simulation Organ Specificity Oxidoreductases Phylogeny Polymerase Chain Reaction RNA Sequence Alignment Spectrophotometry Substrate Specificity Aedes aegypti Archaea Bacteria (microorganisms) Eukaryota Hexapoda
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. © 2012 Wiley Periodicals, Inc.
author	Defelipe, Lucas Alfredo Turjanski, Adrián Gustavo
author_facet	Defelipe, Lucas Alfredo Turjanski, Adrián Gustavo
author_sort	Defelipe, Lucas Alfredo
title	Functional Analysis Of A Mosquito Short-Chain Dehydrogenase Cluster
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
publishDate	2013
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_07394462_v82_n2_p96_Mayoral http://hdl.handle.net/20.500.12110/paper_07394462_v82_n2_p96_Mayoral
work_keys_str_mv	AT defelipelucasalfredo functionalanalysisofamosquitoshortchaindehydrogenasecluster AT turjanskiadriangustavo functionalanalysisofamosquitoshortchaindehydrogenasecluster
_version_	1768543138607005696

Functional Analysis Of A Mosquito Short-Chain Dehydrogenase Cluster

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