Identification of highly reactive cysteinyl and methionyl residues of rabbit muscle phosphofructokinase.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference18 articles.
1. Reactivity of the sulfhydryl groups of muscle phosphofructokinase
2. Rabbit Muscle Phosphofructokinase
3. Allosteric properties of muscle phosphofructokinase. I. Binding of magnesium adenosine triphosphate to the inhibitory site
4. Allosteric properties of muscle phosphofructokinase. II. Kinetics of native and thiol-modified enzyme
5. Beeinflussung der katalytischen Eigenschaften von Phosphofructokinase durch chemische Modifikation funktionell wichtiger Aminosäuren
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2. Reversible High Affinity Inhibition of Phosphofructokinase-1 by Acyl-CoA;Journal of Biological Chemistry;2011-04
3. Chemical Modification of SH Groups of E. coli Phosphofructokinase-2 Induces Subunit Dissociation: Monomers Are Inactive but Preserve Ligand Binding Properties;Archives of Biochemistry and Biophysics;2000-04
4. Site-directed mutagenesis of rabbit muscle phosphofructokinase cDNA. Mutations at glutamine 200 affect the allosteric properties of the enzyme.;Journal of Biological Chemistry;1993-11
5. Modification of the ATP inhibitory site of the Ascaris suum phosphofructokinase results in the stabilization of an inactive T state;Biochemistry;1991-10-01
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