Cloning and structural characterization of the 6-phosphogluconate dehydrogenase locus of the medfly Ceratitis capitata and the olive fruit fly Bactrocera oleae

dc.contributor.author	Goulielmos, GN	en
dc.contributor.author	Cosmidis, N	en
dc.contributor.author	Eliopoulos, E	en
dc.contributor.author	Loukas, M	en
dc.contributor.author	Zouros, E	en
dc.date.accessioned	2014-06-06T06:47:02Z
dc.date.available	2014-06-06T06:47:02Z
dc.date.issued	2006	en
dc.identifier.issn	0006291X	en
dc.identifier.uri	http://dx.doi.org/10.1016/j.bbrc.2005.12.222	en
dc.identifier.uri	http://62.217.125.90/xmlui/handle/123456789/3347
dc.subject	6-Phosphate dehydrogenase	en
dc.subject	Functional constraints	en
dc.subject	Insects	en
dc.subject	Structure	en
dc.subject	Tephritidae	en
dc.subject.other	phosphogluconate dehydrogenase	en
dc.subject.other	amino acid sequence	en
dc.subject.other	antigenicity	en
dc.subject.other	article	en
dc.subject.other	controlled study	en
dc.subject.other	dimerization	en
dc.subject.other	enzyme analysis	en
dc.subject.other	enzyme binding	en
dc.subject.other	enzyme structure	en
dc.subject.other	gene sequence	en
dc.subject.other	Mediterranean fruit fly	en
dc.subject.other	molecular cloning	en
dc.subject.other	molecular model	en
dc.subject.other	nonhuman	en
dc.subject.other	nucleotide sequence	en
dc.subject.other	priority journal	en
dc.subject.other	sequence homology	en
dc.subject.other	Amino Acid Sequence	en
dc.subject.other	Animals	en
dc.subject.other	Cloning, Molecular	en
dc.subject.other	Conserved Sequence	en
dc.subject.other	Genome, Insect	en
dc.subject.other	Humans	en
dc.subject.other	Models, Molecular	en
dc.subject.other	Molecular Sequence Data	en
dc.subject.other	Olea	en
dc.subject.other	Phosphogluconate Dehydrogenase	en
dc.subject.other	Protein Structure, Quaternary	en
dc.subject.other	Sequence Alignment	en
dc.subject.other	Sequence Homology, Amino Acid	en
dc.subject.other	Tephritidae	en
dc.subject.other	Bactrocera oleae	en
dc.subject.other	Ceratitis capitata	en
dc.subject.other	Hexapoda	en
dc.subject.other	Ovis aries	en
dc.subject.other	Tephritidae	en
dc.title	Cloning and structural characterization of the 6-phosphogluconate dehydrogenase locus of the medfly Ceratitis capitata and the olive fruit fly Bactrocera oleae	en
heal.type	journalArticle	en
heal.identifier.primary	10.1016/j.bbrc.2005.12.222	en
heal.publicationDate	2006	en
heal.abstract	The pentose phosphate cycle is considered as a major source of NADPH and pentose needed for nucleic acid biosynthesis. 6-Phosphogluconate dehydrogenase (6PGD), an enzyme participating in this cycle, catalyzes the oxidative decarboxylation of 6PGD to ribulose 5-phosphate with the subsequent release of CO2 and the reduction of NADP. We have determined the genomic sequences of 6PGD of two species of Tephritidae, the medfly Ceratitis capitata and olive fruit fly Bactrocera oleae, and constructed a three-dimensional model of 6PGD of C. capitata based on the homologous known sheep structure. In a comparative study of 6PGD sequences from seven species, all the conserved and variable sites of the enzyme were analyzed and the regions of functional importance were localized, an attempt promoted also by the direct involvement of the enzyme in various human diseases. The enzymes between the two species of Tephritidae have a very high homology and further examination of the variable positions with respect to the highly conserved binding site residues enabled their grouping in three distinct categories, with possible association to dimer formation, functional specificity, and antigenicity. Moreover, placement of sequence differences on the 3-D model suggests probable sites accommodating variations appearing at the allozymic variants of both species. © 2006 Elsevier Inc. All rights reserved.	en
heal.journalName	Biochemical and Biophysical Research Communications	en
dc.identifier.issue	3	en
dc.identifier.volume	341	en
dc.identifier.doi	10.1016/j.bbrc.2005.12.222	en
dc.identifier.spage	721	en
dc.identifier.epage	727	en