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Proton exchange of the pro-S hydrogen at C-1 in dihydroxyacetone phosphate, D-fructose 1,6-bisphosphate and D-fructose 1-phosphate catalysed by rabbit-muscle aldolase. 1976

G Lowe, and R F Pratt

UI MeSH Term Description Entries
D007700 Kinetics The rate dynamics in chemical or physical systems.
D008968 Molecular Conformation The characteristic three-dimensional shape of a molecule. Molecular Configuration,3D Molecular Structure,Configuration, Molecular,Molecular Structure, Three Dimensional,Three Dimensional Molecular Structure,3D Molecular Structures,Configurations, Molecular,Conformation, Molecular,Conformations, Molecular,Molecular Configurations,Molecular Conformations,Molecular Structure, 3D,Molecular Structures, 3D,Structure, 3D Molecular,Structures, 3D Molecular
D009132 Muscles Contractile tissue that produces movement in animals. Muscle Tissue,Muscle,Muscle Tissues,Tissue, Muscle,Tissues, Muscle
D009682 Magnetic Resonance Spectroscopy Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING). In Vivo NMR Spectroscopy,MR Spectroscopy,Magnetic Resonance,NMR Spectroscopy,NMR Spectroscopy, In Vivo,Nuclear Magnetic Resonance,Spectroscopy, Magnetic Resonance,Spectroscopy, NMR,Spectroscopy, Nuclear Magnetic Resonance,Magnetic Resonance Spectroscopies,Magnetic Resonance, Nuclear,NMR Spectroscopies,Resonance Spectroscopy, Magnetic,Resonance, Magnetic,Resonance, Nuclear Magnetic,Spectroscopies, NMR,Spectroscopy, MR
D011485 Protein Binding The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. Plasma Protein Binding Capacity,Binding, Protein
D011487 Protein Conformation The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). Conformation, Protein,Conformations, Protein,Protein Conformations
D011817 Rabbits A burrowing plant-eating mammal with hind limbs that are longer than its fore limbs. It belongs to the family Leporidae of the order Lagomorpha, and in contrast to hares, possesses 22 instead of 24 pairs of chromosomes. Belgian Hare,New Zealand Rabbit,New Zealand Rabbits,New Zealand White Rabbit,Rabbit,Rabbit, Domestic,Chinchilla Rabbits,NZW Rabbits,New Zealand White Rabbits,Oryctolagus cuniculus,Chinchilla Rabbit,Domestic Rabbit,Domestic Rabbits,Hare, Belgian,NZW Rabbit,Rabbit, Chinchilla,Rabbit, NZW,Rabbit, New Zealand,Rabbits, Chinchilla,Rabbits, Domestic,Rabbits, NZW,Rabbits, New Zealand,Zealand Rabbit, New,Zealand Rabbits, New,cuniculus, Oryctolagus
D004099 Dihydroxyacetone Phosphate An important intermediate in lipid biosynthesis and in glycolysis. Dihydroxyacetone 3-Phosphate,3-Phosphate, Dihydroxyacetone,Dihydroxyacetone 3 Phosphate,Phosphate, Dihydroxyacetone
D005634 Fructose-Bisphosphate Aldolase An enzyme of the lyase class that catalyzes the cleavage of fructose 1,6-biphosphate to form dihydroxyacetone phosphate and glyceraldehyde 3-phosphate. The enzyme also acts on (3S,4R)-ketose 1-phosphates. The yeast and bacterial enzymes are zinc proteins. (Enzyme Nomenclature, 1992) E.C. 4.1.2.13. Aldolase,Fructosediphosphate Aldolase,Aldolase A,Aldolase B,Aldolase C,Fructose 1,6-Bisphosphate Aldolase,Fructose 1,6-Bisphosphate Aldolase, Class II,Fructose 1-Phosphate Aldolase,Fructose Biphosphate Aldolase,Fructosemonophosphate Aldolase,1,6-Bisphosphate Aldolase, Fructose,Aldolase, Fructose 1,6-Bisphosphate,Aldolase, Fructose 1-Phosphate,Aldolase, Fructose Biphosphate,Aldolase, Fructose-Bisphosphate,Aldolase, Fructosediphosphate,Aldolase, Fructosemonophosphate,Fructose 1 Phosphate Aldolase,Fructose 1,6 Bisphosphate Aldolase,Fructose Bisphosphate Aldolase
D005636 Fructosephosphates

Related Publications

G Lowe, and R F Pratt
The proton exchange of the pro-S hydrogen atom at C-1 in dihydroxyacetone phosphate and D-fructose 1,6-bisphosphate catalysed by class-I and class-II aldolases.
June 1978, The Biochemical journal,
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Fructose 1,6-bisphosphate aldolase from rabbit muscle. The isomerization of the enzyme-dihydroxyacetone phosphate complex.
November 1977, The Biochemical journal,
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July 1985, Biochemistry,
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Fructose-1,6-bisphosphate aldolase from rabbit muscle: different catalytic behavior of the dihydroxyacetone phosphate binding sites at low temperature.
September 1984, Archives of biochemistry and biophysics,
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April 1968, Biochemistry,
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October 1977, European journal of biochemistry,
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Fructose-1,6-bisphosphate-aldolase from rabbit muscle. Half of the sites reactivity at low temperature.
January 1983, Biochemical and biophysical research communications,
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Fructose-bisphosphate aldolase from rabbit muscle. A thermodynamic study on the formation of the enzyme-dihydroxyacetone phosphate complex.
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