Functional Analysis of a Mosquito Short-Chain Dehydrogenase Cluster

Mayoral J.G., Leonard K.T., Nouzova M., Noriega F.G., Defelipe L.A. and Turjanski A.G. (2013) Functional Analysis of a Mosquito Short-Chain Dehydrogenase Cluster. Archives of Insect Biochemistry and Physiology, 82 2: 96-115. doi:10.1002/arch.21078

Author Mayoral J.G.
Leonard K.T.
Nouzova M.
Noriega F.G.
Defelipe L.A.
Turjanski A.G.
Title Functional Analysis of a Mosquito Short-Chain Dehydrogenase Cluster
Journal name Archives of Insect Biochemistry and Physiology   Check publisher's open access policy
ISSN 0739-4462
Publication date 2013-02-01
Year available 2012
Sub-type Article (original research)
DOI 10.1002/arch.21078
Open Access Status Not Open Access
Volume 82
Issue 2
Start page 96
End page 115
Total pages 20
Place of publication Hoboken, United States
Publisher John Wiley & Sons
Subject 1109 Neurosciences
1314 Physiology
1303 Specialist Studies in Education
Abstract 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.
Keyword Aedes aegypti
Juvenile hormone
Short-chain dehydrogenase
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2014 Collection
School of Biological Sciences Publications
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 6 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 6 times in Scopus Article | Citations
Google Scholar Search Google Scholar
Created: Thu, 28 Nov 2013, 21:19:42 EST by System User on behalf of School of Biological Sciences