Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2009-2-16
pubmed:abstractText
In insects, farnesyl pyrophosphate (FPP) is converted to juvenile hormone (JH) via a conserved pathway consisting of isoprenoid-derived metabolites. The first step of this pathway is presumed to be hydrolysis of FPP to farnesol in the ring gland. Based on alignment of putative phosphatases from Drosophila melanogaster with the phosphatase domain of soluble epoxide hydrolase, Phos2680 and Phos15739 with conserved phosphatase motifs were identified, cloned and purified. Both D. melanogaster phosphatases hydrolyzed para-nitrophenyl phosphate, however, Phos15739 also hydrolyzed FPP with a K(cat)/K(m) of 2.1x10(5)M(-1)s(-1). RT-PCR analysis revealed that Phos15739 was expressed in the ring gland and its expression was correlated with JHIII titer during development of D. melanogaster. N-acetyl-S-geranylgeranyl-l-cysteine was found to be a potent inhibitor of Phos15739 with an IC(50) value of 4.4muM. Thus, our data identify Phos15739 as a FPP phosphatase that likely catalyzes the hydrolysis of FPP to farnesol in D. melanogaster.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/19168029-10485878, http://linkedlifedata.com/resource/pubmed/commentcorrection/19168029-10706642, http://linkedlifedata.com/resource/pubmed/commentcorrection/19168029-10876106, http://linkedlifedata.com/resource/pubmed/commentcorrection/19168029-11342136, http://linkedlifedata.com/resource/pubmed/commentcorrection/19168029-11729082, http://linkedlifedata.com/resource/pubmed/commentcorrection/19168029-12574508, http://linkedlifedata.com/resource/pubmed/commentcorrection/19168029-12821501, http://linkedlifedata.com/resource/pubmed/commentcorrection/19168029-14530389, http://linkedlifedata.com/resource/pubmed/commentcorrection/19168029-14599489, http://linkedlifedata.com/resource/pubmed/commentcorrection/19168029-15024118, http://linkedlifedata.com/resource/pubmed/commentcorrection/19168029-15201301, http://linkedlifedata.com/resource/pubmed/commentcorrection/19168029-15242710, http://linkedlifedata.com/resource/pubmed/commentcorrection/19168029-15337123, http://linkedlifedata.com/resource/pubmed/commentcorrection/19168029-15355237, http://linkedlifedata.com/resource/pubmed/commentcorrection/19168029-16142916, http://linkedlifedata.com/resource/pubmed/commentcorrection/19168029-16414022, http://linkedlifedata.com/resource/pubmed/commentcorrection/19168029-16551550, http://linkedlifedata.com/resource/pubmed/commentcorrection/19168029-18775727, http://linkedlifedata.com/resource/pubmed/commentcorrection/19168029-2493154, http://linkedlifedata.com/resource/pubmed/commentcorrection/19168029-3106038
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1090-2104
pubmed:author
pubmed:issnType
Electronic
pubmed:day
27
pubmed:volume
380
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
188-92
pubmed:dateRevised
2011-3-29
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
An insect farnesyl phosphatase homologous to the N-terminal domain of soluble epoxide hydrolase.
pubmed:affiliation
Department of Molecular and Cell Biology, University of Connecticut, Storrs, CT 06269, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural