A Conserved Glutamate Residue Exhibits Multifunctional Catalytic Roles in d-Fructose-1,6-bisphosphate Aldolases
Open Access
- 1 March 2002
- journal article
- Published by Elsevier
- Vol. 277 (11) , 9474-9483
- https://doi.org/10.1074/jbc.m107600200
Abstract
No abstract availableKeywords
This publication has 41 references indexed in Scilit:
- Crystal Structure of Fructose-1,6-bisphosphate Aldolase from the Human Malaria Parasite Plasmodium falciparum,Biochemistry, 1998
- Mechanism of the Reaction Catalyzed by Acetoacetate Decarboxylase. Importance of Lysine 116 in Determining the pKa of Active-Site Lysine 115Biochemistry, 1996
- The crystal structure of fructose‐1,6‐bisphosphate aldolase fromDrosophila melanogaster at 2.5A˚resolutionFEBS Letters, 1991
- Activity and specificity of human aldolasesJournal of Molecular Biology, 1991
- Molecular architecture of rabbit skeletal muscle aldolase at 2.7-A resolution.Proceedings of the National Academy of Sciences, 1987
- Complexes of muscle aldolase in equilibrium with fructose 1,6-bisphosphateBiochemistry, 1985
- Chemical trapping of complexes of dihydroxyacetone phosphate with muscle fructose-1,6-bisphosphate aldolaseBiochemistry, 1985
- Carbon-13 NMR evidence of carbinolamine formation at the active site of an imine-forming aldolaseJournal of the American Chemical Society, 1983
- The covalent binding of d-fructose 1,6-diphosphate to muscle aldolaseArchives of Biochemistry and Biophysics, 1972
- The mechanism of action of aldolases III. Schiff base formation with lysineBiochemical and Biophysical Research Communications, 1962