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[40] Fructose-bisphosphate aldolase from Helix pomatia
1982Publisher Summary This chapter describes the purification and properties of the enzyme, fructose-bisphosphate aldolase, from the commercially available snail Helix pomatia . Snail aldolase activity is measured at 25 ° C as described for ascarid aldolase and aldolase concentration is measured assuming the same extinction coefficient as for rabbit ...
Marian Kochman +2 more
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Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1990
The combination of binding and kinetic approaches is suggested to study (i) the mechanism of substrate-modulated dynamic enzyme associations; (ii) the specificity of enzyme interactions. The effect of complex formation between aldolase and glyceraldehyde-3-phosphate dehydrogenase (D-glyceraldehyde-3-phosphate:NAD+ oxidoreductase (phosphorylating), EC 1.
J, Neuzil +3 more
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The combination of binding and kinetic approaches is suggested to study (i) the mechanism of substrate-modulated dynamic enzyme associations; (ii) the specificity of enzyme interactions. The effect of complex formation between aldolase and glyceraldehyde-3-phosphate dehydrogenase (D-glyceraldehyde-3-phosphate:NAD+ oxidoreductase (phosphorylating), EC 1.
J, Neuzil +3 more
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[39] Fructose-bisphosphate aldolase from Ascaris suum
1982Publisher Summary This chapter describes an assay method and the purification procedure for fructose-bisphosphate aldolase from Ascaris suum . The assay is based on the oxidation of NADH by dihydroxyacetone phosphate (DHAP) in a coupled system containing triosephosphate isomerase and α-glycerophosphate dehydrogenase.
Marian Kochman, Danuta Kwiatkowska
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Biochemistry, 2009
Fructose-1,6-bisphosphate muscle aldolase is an essential glycolytic enzyme that catalyzes reversible carbon-carbon bond formation by cleaving fructose 1,6-bisphosphate to yield dihydroxyacetone phosphate (DHAP) and d-glyceraldehyde phosphate. To elucidate the mechanistic role of conserved amino acid Asp-33, Asn-33 and Ser-33 mutants were examined by ...
Miguel, St-Jean +2 more
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Fructose-1,6-bisphosphate muscle aldolase is an essential glycolytic enzyme that catalyzes reversible carbon-carbon bond formation by cleaving fructose 1,6-bisphosphate to yield dihydroxyacetone phosphate (DHAP) and d-glyceraldehyde phosphate. To elucidate the mechanistic role of conserved amino acid Asp-33, Asn-33 and Ser-33 mutants were examined by ...
Miguel, St-Jean +2 more
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Plant Molecular Biology, 2004
Fructose-bisphosphate aldolase is a glycolytic enzyme whose activity increases in rice roots treated with gibberellin (GA). To investigate the relationship between aldolase and root growth, GA-induced root aldolase was characterized. GA3 promoted an increase in aldolase accumulation when 0.1 microM GA3 was added exogenously to rice roots.
Hirosato, Konishi +3 more
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Fructose-bisphosphate aldolase is a glycolytic enzyme whose activity increases in rice roots treated with gibberellin (GA). To investigate the relationship between aldolase and root growth, GA-induced root aldolase was characterized. GA3 promoted an increase in aldolase accumulation when 0.1 microM GA3 was added exogenously to rice roots.
Hirosato, Konishi +3 more
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Molecular and Biochemical Parasitology, 1991
Chemical modifications of Class I aldolases from Trypanosoma brucei, rabbit muscle and Staphylococcus aureus with carboxypeptidase A, glyceraldehyde 3-phosphate and cysteine-specific reagents revealed the following differences between the three homologous enzymes. Aldolase from S. aureus was not affected by any of these reagents.
M, Callens, F R, Opperdoes
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Chemical modifications of Class I aldolases from Trypanosoma brucei, rabbit muscle and Staphylococcus aureus with carboxypeptidase A, glyceraldehyde 3-phosphate and cysteine-specific reagents revealed the following differences between the three homologous enzymes. Aldolase from S. aureus was not affected by any of these reagents.
M, Callens, F R, Opperdoes
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Molecular and Biochemical Parasitology, 1991
The kinetic properties of aldolase from Trypanosoma brucei were studied in comparison with aldolase from rabbit muscle and Staphylococcus aureus. The 3 enzymes displayed a similar broad pH optimum for the cleavage of fructose 1,6-bisphosphate (Fru(1,6)P2) and a similar narrow pH optimum for the cleavage of fructose 1-phosphate (Fru-1-P). However, small
M, Callens, D A, Kuntz, F R, Opperdoes
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The kinetic properties of aldolase from Trypanosoma brucei were studied in comparison with aldolase from rabbit muscle and Staphylococcus aureus. The 3 enzymes displayed a similar broad pH optimum for the cleavage of fructose 1,6-bisphosphate (Fru(1,6)P2) and a similar narrow pH optimum for the cleavage of fructose 1-phosphate (Fru-1-P). However, small
M, Callens, D A, Kuntz, F R, Opperdoes
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Journal of Molecular Recognition, 2008
AbstractThe present work describes the selective covalent modification of fructose bisphosphate aldolase in crude extracts of chicken breast muscle by fluorescein 5′‐isothiocyanate (5′‐FITC) at pH 7.0 and 35°C. The modification was observed after 1 min while no other major soluble protein was labeled even after 30 min. We calculated that ca.
Andrew G, Gehring +2 more
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AbstractThe present work describes the selective covalent modification of fructose bisphosphate aldolase in crude extracts of chicken breast muscle by fluorescein 5′‐isothiocyanate (5′‐FITC) at pH 7.0 and 35°C. The modification was observed after 1 min while no other major soluble protein was labeled even after 30 min. We calculated that ca.
Andrew G, Gehring +2 more
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Digestive Diseases and Sciences, 2019
Hypoxia is an important factor in malignant tumors, and glycolysis is a major metabolic contributor in their development. Glycolytic enzymes have gained increasing attention as potential therapeutic targets because they are associated with cancer-specific metabolism.
Xin, Li +9 more
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Hypoxia is an important factor in malignant tumors, and glycolysis is a major metabolic contributor in their development. Glycolytic enzymes have gained increasing attention as potential therapeutic targets because they are associated with cancer-specific metabolism.
Xin, Li +9 more
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Fructose-bisphosphate aldolase from rabbit muscle
Biochimica et Biophysica Acta (BBA) - Enzymology, 1974Enrico Grazi, Giorgio Trombetta
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