A Functional Arginine Residue in Rabbit-Muscle Aldolase
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1976.tb11043.x/fullpdf
Reference27 articles.
1. The Interaction of Enzymes with Small Ions. I. An Electrophoretic and Equilibrium Analysis of Aldolase in Phosphate and Acetate Buffers.
2. The binding-sites of rabbit muscle aldolase
3. Specific Anion Binding to Fructose Diphosphate Aldolase from Rabbit Muscle*
4. The effect of pyridoxal phosphate on rabbit muscle aldolase
5. Essential arginyl residues in Escherichia coli alkaline phosphatase
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1. Detection of local polarity and conformational changes at the active site of rabbit muscle creatine kinase with a new arginine-specific fluorescent probe;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2008-02
2. Irreversible inhibition of aldolase by a phosphorylated α-dicarbonyl compound;Journal of Enzyme Inhibition and Medicinal Chemistry;2008-01-01
3. Structure of a Fructose-1,6-bis(phosphate) Aldolase Liganded to Its Natural Substrate in a Cleavage-Defective Mutant at 2.3 Å,;Biochemistry;1999-09-01
4. Structure-based Reevaluation of the Mechanism of Class I Fructose-1,6-bisphosphate Aldolase;Journal of Molecular Modeling;1999-03-01
5. Kinetic and spectroscopic study of slow-binding inhibition processes in aldolase;Journal of Physical Organic Chemistry;1998-11
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