On the substrate specificity of fructose 1,6-diphosphate aldolase (E.C.4.1.2.13) from rabbit muscle: A critical revision
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference8 articles.
1. Substrates of D-fructose 1,6-diphosphate aldolase in solution
2. Magnetic resonance studies of the anomeric distribution and manganese binding properties of fructose phosphates
3. Tautomeric composition of D-fructose phosphates in solution by fourier transform carbon-13 nuclear magnetic resonance
4. Dihydroxyacetone phosphate. Its structure and reactivity with α-glycerophosphate dehydrogenase, aldolase and triose phosphate isomerase and some possible metabolic implications
5. Anomeric specificity of fructosediphosphate aldolase E.C.4.1.2.13 from rabbit muscle
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1. Presteady-State Kinetic Evidence for a Ring-Opening Activity in Fructose-1,6-(bis)phosphate Aldolase;Journal of the American Chemical Society;2004-02-26
2. C-C Bond Formation;Tetrahedron Organic Chemistry Series;1994
3. Theoretical study in vacuo of the first step of the reversible aldol cleavage catalyzed by aldolase from rabbit muscle;Journal of Molecular Structure: THEOCHEM;1993-11
4. Complexes of muscle aldolase in equilibrium with fructose 1,6-bisphosphate;Biochemistry;1985-07-01
5. Fructose bisphosphate aldolase from rabbit muscle. A new, acid-labile intermediate of the aldolase reaction and the partition of the enzyme among the catalytic intermediates at equilibrium;Archives of Biochemistry and Biophysics;1980-03
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