Enzymatic Catalysis and Transition-State Theory

The application of transition-state theory to enzymatic catalysis provides an approach to understanding enzymatic catalysis in terms of the factors that determine the strength of binding of ligands to proteins. The prediction that the transition state should bind to the enzyme much more tightly than the substrate is supported by the experimental results with stable analogs of transition states. Transition-state analogs have great potential for use in understanding enzymatic catalysis and in inhibiting enzymes. Because of their potency and specificity as enzyme inhibitors, some of them may become very useful chemotherapeutic agents.

[1]  W. Jencks General acid-base catalysis of complex reactions in water , 1972 .

[2]  R. Wolfenden,et al.  Changes in absorption spectrum and crystal structure of triose phosphate isomerase brought about by 2-phosphoglycollate, a potential transition state analogue. , 1970, Journal of molecular biology.

[3]  George S. Hammond,et al.  A Correlation of Reaction Rates , 1955 .

[4]  A. North,et al.  Crystallographic studies of the activity of hen egg-white lysozyme , 1967, Proceedings of the Royal Society of London. Series B. Biological Sciences.

[5]  J. Kraut 7 Chymotrypsin-Chemical Properties and Catalysis , 1971 .

[6]  D. Koshland Molecular geometry in enzyme action. , 1956, Journal of cellular physiology. Supplement.

[7]  W. Rutter,et al.  Magnetic resonance studies of the role of the divalent cation in the mechanism of yeast aldolase. , 1971, Biochemistry.

[8]  D. Koshland,et al.  Covalent Enzyme-Substrate Intermediates , 1971, Science.

[9]  C. I. Pogson,et al.  Dihydroxyacetone phosphate. Its structure and reactivity with -glycerophosphate dehydrogenase, aldolase and triose phosphate isomerase and some possible metabolic implications. , 1971, The Biochemical journal.

[10]  G. Lienhard,et al.  P 1 ,P 5 -Di(adenosine-5')pentaphosphate, a potent multisubstrate inhibitor of adenylate kinase. , 1973, The Journal of biological chemistry.

[11]  Keith J. Laidler,et al.  Theories Of Chemical Reaction Rates , 1969 .

[12]  D G Rhoads,et al.  Initial velocity and equilibrium kinetics of myokinase. , 1968, The Journal of biological chemistry.

[13]  R. Wolfenden,et al.  Aldehydes as inhibitors of papain. , 1972, The Journal of biological chemistry.

[14]  B. S. Hartley,et al.  10 Pancreatic Elastase , 1971 .

[15]  B. Horecker,et al.  The mechanism of action of aldolases. , 1968, Advances in enzymology and related areas of molecular biology.

[16]  G. Lienhard,et al.  A transition state analog for lysozyme. , 1972, The Journal of biological chemistry.

[17]  W. Jencks,et al.  Entropic contributions to rate accelerations in enzymic and intramolecular reactions and the chelate effect. , 1971, Proceedings of the National Academy of Sciences of the United States of America.

[18]  R. Thompson Use of peptide aldehydes to generate transition-state analogs of elastase. , 1973, Biochemistry.

[19]  R. Wolfenden Binding of substrate and transition state analog to trisephosphate isomerase. , 1970, Biochemistry.

[20]  R. Wolfenden,et al.  Transition State Analogues for Enzyme Catalysis , 1969, Nature.