Regular ArticleCaenorhabditis elegansHas Two Isozymic Forms, CE-1 and CE-2, of Fructose-1,6-bisphosphate Aldolase Which Are Encoded by Different Genes☆,☆☆
References (55)
- et al.
Biochem. Biophys. Res. Commun.
(1985) - et al.
Biochimie
(1987) - et al.
Biochem. Biophys. Res. Commun.
(1991) - et al.
J. Biol. Chem.
(1984) - et al.
J. Biol. Chem.
(1990) - et al.
J. Biol. Chem.
(1985) - et al.
Biochim. Biophys. Acta
(1994) - et al.
Biochim. Biophys. Acta
(1995) - et al.
Arch. Biochem. Biophys.
(1994) - et al.
Mol. Biochem. Parasitol.
(1990)
Insect. Biochem. Mol. Biol.
Anal. Biochem.
Biochem. Biophys. Res. Commun.
J. Mol. Biol.
Methods Enzymol.
Anal. Biochem.
Biochim. Biophys. Acta
Methods Enzymol.
GATA
J. Biol. Chem.
J. Biol. Chem.
The Enzymes
Fed. Proc.
Proc. Natl. Acad. Sci. USA
Gene
Biochem. Int.
J. Biochem.
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Characterization and localization of Opisthorchis viverrini fructose-1,6-bisphosphate aldolase
2017, Parasitology InternationalCitation Excerpt :Aldolase C is expressed in neural tissue and exhibits intermediate properties to those of aldolase A and B [12]. In parasites, several FBPA isozymes were identified [13,14] and detected in components of excretory-secretory (ES) products [15,16]. Nonetheless, many parasite FBPAs showed multifunctional roles in both glycolysis and host invasion [17,18].
Recent Advances in Elucidating Nematode Moulting - Prospects of Using Oesophagostomum dentatum as a Model
2016, Advances in ParasitologyCitation Excerpt :In addition to its function as an enzyme in fatty acid metabolism, PCC might interact with selected gene products, similar to its homologue in C. elegans for which modulating roles of mlt-10, a key regulator of moulting, have been proposed (Frand et al., 2005). FBA, another enzyme of carbohydrate metabolism involved in glycolysis by catalyzing the conversion of fructose-1,6-bisphosphate to glyceraldehyde-3-phosphate and dihydroxyacetone phosphate (Inoue et al., 1997), was inferred to function during moulting in O. dentatum. This enzyme has been reported in various nematode species (Craig et al., 2006; Inoue et al., 1997; McCarthy et al., 2002; Moreno and Geary, 2008; Yan et al., 2013) and might serve in providing energy during moulting.
Proteomics-based identification and analysis proteins associated with spirotetramat tolerance in Aphis gossypii Glover
2015, Pesticide Biochemistry and PhysiologyCitation Excerpt :These upregulated proteins include putative fructose 1,6-bisphosphate aldolase (spot 5), fructose-bisphosphate aldolase-like isoform (spot 10), ATP synthase E chain (spot 19), and UDP-glucose 6-dehydrogenase (spot 28). The fructose 1,6-bisphosphate aldolase (FBA) plays a central role in glycolysis and is important for production of the energy [23], by catalyzing the reversible aldol condensation of dihydroxyacetonephosphate and glyceraldehydes 3-phosphate in the glycolysis [24]. The DDT resistant Drosophila melanogaster relies primarily on biochemical pathway-glycolysis to produce reduced NADP and increase DDT detoxification [25].
Molecular and biochemical characterizations of three fructose-1,6- bisphosphate aldolases from Clonorchis sinensis
2014, Molecular and Biochemical ParasitologyCitation Excerpt :Kinetic parameters of rCsFbAs were compared with those of Class I FbA isozymes from other species (Table 1). FbA is a well-known glycometabolism enzyme in almost all organisms, and FbA isozymes with distinct properties have been described in some invertebrates, such as Caenorhabditis elegans [27], Echinococcus granulosus [28] and Drosophila melanogaster [29]. In the present study, we screened out three distinct FbA genes encoding FbA isozymes from C. sinensis.
Fructose-bisphosphate aldolase and enolase from Echinococcus granulosus: Genes, expression patterns and protein interactions of two potential moonlighting proteins
2012, GeneCitation Excerpt :In D. melanogaster there are three isozymic forms of aldolase which are generated from a single gene by alternative splicing (Kai et al., 1992). C. elegans and Clonorchis sinensis present two and three isozymes, respectively (Cho et al., 2006; Inoue et al., 1997), and similarly to vertebrates, each of these isozymes is encoded by different genes. Enolase primary function is the catalysis of the reversible transformation between 2-phospho-glyceric acid and phosphoenolpyruvic acid.
Molecular evolution of amphioxus fructose-1,6 bisphosphate aldolase
1997, Archives of Biochemistry and Biophysics
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The sequences reported in this paper have been submitted to the DDBJ/EMBL/GenBank data bases (Accession Nos. D83738 for the Ce-1 aldolase and D83739 for the Ce-2 aldolase).
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P. D. Boyer, Ed.
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