Publications
Key publications | Publications by category | Publications by year
Publications by category
Journal articles
Matousková P, Luxová A, Matousková J, Jiros P, Svatos A, Valterová I, Pichová I (2008). A delta9 desaturase from Bombus lucorum males: investigation of the biosynthetic pathway of marking pheromones.
Chembiochem,
9(15), 2534-2541.
Abstract:
A delta9 desaturase from Bombus lucorum males: investigation of the biosynthetic pathway of marking pheromones.
The knowledge of the molecular basis of communication in bumblebee communities is limited. None of the enzymes that participate in pheromone production have been characterized. Here, we cloned the gene encoding the Delta(9) desaturase from cDNA prepared from the total RNA of the pheromone gland and fat bodies of Bombus lucorum male. Functional expression of BlucNPVE desaturase in Saccharomyces cerevisiae and GC-MS analyses revealed its preference for C(18) saturated fatty acids. This suggests that Delta(9) desaturase is involved in the desaturation of metabolic fatty acids stored in triacylglyceroles (TAGs), because oleic acid is the most abundant fatty acid bound in TAG in B. lucorum and it is present in low concentration in the pheromone blend. The incubation of pheromone precursors with a dissected labial gland as well as direct injection of labelled pheromone substrates into B. lucorum males revealed that esterification of pheromone products occurs in the labial gland. These results support both the biosynthesis of pheromones from common lipids and the de novo synthesis of unsaturated pheromones in the labial gland.
Abstract.
Author URL.
Matousková P, Pichová I, Svatos A (2007). Functional characterization of a desaturase from the tobacco hornworm moth (Manduca sexta) with bifunctional Z11- and 10,12-desaturase activity.
Insect Biochem Mol Biol,
37(6), 601-610.
Abstract:
Functional characterization of a desaturase from the tobacco hornworm moth (Manduca sexta) with bifunctional Z11- and 10,12-desaturase activity.
The pheromone blend produced by the tobacco hornworm moth (Manduca sexta) (L.) female is unusually complex and contains two conjugated dienals and trienals together with two monounsaturated alkenals. Here, we describe the identification and construction of two genes encoding MsexKPSE and MsexAPTQ desaturases from a cDNA library prepared from the total RNA of the M. sexta pheromone gland. The MsexKPSE desaturase shares a high degree of similarity with Delta(9)-desaturases from different moth species. The functional expression of MsexAPTQ desaturase in Saccharomyces cerevisiae followed by a detailed GC-MS analysis of fatty acid methyl esters (FAME) and their derivatized products and gas-phase Fourier transform infrared (FTIR) spectroscopy of the extracted FAME confirms that this enzyme is a bifunctional Z-Delta(11)-desaturase. MsexAPTQ desaturase catalyses the production of Z11-hexadecenoate (Z11-16) and Z10E12- and E10E12-hexadecadienoates (Z10E12-16) via 1,4-desaturation of the Z11-16 substrate. The stereochemistry of 1,4-desaturation and formation of isomers is discussed.
Abstract.
Author URL.
Publications by year
2008
Matousková P, Luxová A, Matousková J, Jiros P, Svatos A, Valterová I, Pichová I (2008). A delta9 desaturase from Bombus lucorum males: investigation of the biosynthetic pathway of marking pheromones.
Chembiochem,
9(15), 2534-2541.
Abstract:
A delta9 desaturase from Bombus lucorum males: investigation of the biosynthetic pathway of marking pheromones.
The knowledge of the molecular basis of communication in bumblebee communities is limited. None of the enzymes that participate in pheromone production have been characterized. Here, we cloned the gene encoding the Delta(9) desaturase from cDNA prepared from the total RNA of the pheromone gland and fat bodies of Bombus lucorum male. Functional expression of BlucNPVE desaturase in Saccharomyces cerevisiae and GC-MS analyses revealed its preference for C(18) saturated fatty acids. This suggests that Delta(9) desaturase is involved in the desaturation of metabolic fatty acids stored in triacylglyceroles (TAGs), because oleic acid is the most abundant fatty acid bound in TAG in B. lucorum and it is present in low concentration in the pheromone blend. The incubation of pheromone precursors with a dissected labial gland as well as direct injection of labelled pheromone substrates into B. lucorum males revealed that esterification of pheromone products occurs in the labial gland. These results support both the biosynthesis of pheromones from common lipids and the de novo synthesis of unsaturated pheromones in the labial gland.
Abstract.
Author URL.
2007
Matousková P, Pichová I, Svatos A (2007). Functional characterization of a desaturase from the tobacco hornworm moth (Manduca sexta) with bifunctional Z11- and 10,12-desaturase activity.
Insect Biochem Mol Biol,
37(6), 601-610.
Abstract:
Functional characterization of a desaturase from the tobacco hornworm moth (Manduca sexta) with bifunctional Z11- and 10,12-desaturase activity.
The pheromone blend produced by the tobacco hornworm moth (Manduca sexta) (L.) female is unusually complex and contains two conjugated dienals and trienals together with two monounsaturated alkenals. Here, we describe the identification and construction of two genes encoding MsexKPSE and MsexAPTQ desaturases from a cDNA library prepared from the total RNA of the M. sexta pheromone gland. The MsexKPSE desaturase shares a high degree of similarity with Delta(9)-desaturases from different moth species. The functional expression of MsexAPTQ desaturase in Saccharomyces cerevisiae followed by a detailed GC-MS analysis of fatty acid methyl esters (FAME) and their derivatized products and gas-phase Fourier transform infrared (FTIR) spectroscopy of the extracted FAME confirms that this enzyme is a bifunctional Z-Delta(11)-desaturase. MsexAPTQ desaturase catalyses the production of Z11-hexadecenoate (Z11-16) and Z10E12- and E10E12-hexadecadienoates (Z10E12-16) via 1,4-desaturation of the Z11-16 substrate. The stereochemistry of 1,4-desaturation and formation of isomers is discussed.
Abstract.
Author URL.
Refresh publications
