LIGAND‐ENZYME INTERACTIONS AND ENZYME REGULATION *

One of the basic problems in biochemistry is how enzymes are regulated to provide control of metabolism. Two of the processes of switching an enzyme “on” and “off’ involve the binding of regulatory ligands and chemical modifications of the enzyme. Most of the regulatory enzymes studied so far have been found to have several subunits. The interaction between these subunits is assumed responsible for the observed cooperativity of the binding of regulatory ligands. Often the initial signal for the enzyme activation is small and is amplified by having a cascade of enzymes each one of which activates the next. A good example of this is the system of enzymes which regulate the breakdown of glycogen.

[1]  I. Campbell,et al.  Studies on the interaction of ligands with phosphorylase b using a spin-label probe. , 1972, European journal of biochemistry.

[2]  R. Dwek,et al.  Probes for the Conformational Transitions of Phosphorylase a , 1972 .

[3]  R. Dwek,et al.  Probes for the conformational transitions of phosphorylase b. Effect of ligands studied by proton relaxation enhancement, fluorescence and chemical reactivities. , 1971, European journal of biochemistry.

[4]  J. Leigh ESR Rigid-Lattice Line Shape in a System of Two Interacting Spins , 1970 .

[5]  N. C. Price,et al.  The reactivity of SH groups with a fluorogenic reagent , 1970, FEBS letters.

[6]  L. L. Kastenschmidt,et al.  The effect of temperature on the allosteric transitions of rabbit skeletal muscle phosphorylase b. , 1968, Biochemistry.

[7]  J. H. Wang,et al.  Studies on the allosteric activation of glycogen phosphorylase b by Nucleotides. I. Activation of phosphorylase b by inosine monophosphate. , 1968, The Journal of biological chemistry.

[8]  L. L. Kastenschmidt,et al.  Subunit interactions and their relationship to the allosteric properties of rabbit skeletal muscle phosphorylase b. , 1968, Biochemistry.

[9]  D. Graves,et al.  Circular dichroism and optical rotatory dispersion of glycogen phosphorylase. , 1966, Biochemistry.

[10]  E. Fischer,et al.  On the role of pyridoxal 5'-phosphate in phosphorylase. II. Resolution of rabbit muscle phosphorylase b. , 1966, Biochemistry.

[11]  J. Hedrick,et al.  An optical rotary dispersion study of glycogen phosphorylase. , 1966, Archives of biochemistry and biophysics.

[12]  J. Changeux,et al.  ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL. , 1965, Journal of molecular biology.

[13]  K. Sheridan,et al.  Regular Pulses from the Sun and a Possible Clue to the Origin of Solar Cosmic Rays , 1971, Nature.