@article{oai:tsukuba.repo.nii.ac.jp:00016720,
 author = {丹羽, 隆介 and Niwa, Ryusuke and Niimi, Teruyuki and Honda, Naoko and Yoshiyama, Michiyo and Itoyama, Kyo and Kataoka, Hiroshi and Shinoda, Tetsuro},
 issue = {7},
 journal = {Insect biochemistry and molecular biology},
 month = {Jul},
 note = {application/pdf, Juvenile hormone (JH) acid O-methyltransferase (JHAMT) is the enzyme that transfers a methyl group
from S-adenosyl-L-methionine (SAM) to the carboxyl group of JH acids to produce active JHs in the
corpora allata. While the JHAMT gene was originally identified and characterized in the silkworm
Bombyx mori, no orthologs from other insects have been studied until now. Here we report on the
functional characterization of the CG17330/DmJHAMT gene in the fruit fly Drosophila melanogaster.
Recombinant DmJHAMT protein expressed in Escherichia coli catalyzes the conversion of farnesoic acid
and JH III acid to their cognate methyl esters in the presence of SAM. DmJHAMT is predominantly
expressed in corpora allata, and its developmental expression profile correlates with changes in the JH
titer. While a transgenic RNA interference against DmJHAMT has no visible effect, overexpression of
DmJHAMT results in a pharate adult lethal phenotype, similar to that obtained with application of JH
analogs, suggesting that the temporal regulation of DmJHAMT is critical for Drosophila development.},
 pages = {714--720},
 title = {Juvenile hormone acid O-methyltransferase in Drosophila melanogaster},
 volume = {38},
 year = {2008}
}