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Journal Abstract Search
167 related items for PubMed ID: 3657192
1. Energetics of enzyme catalysis. II. Oversaturation, case diagrams, reversible and irreversible behaviour. Albery WJ, Knowles JR. J Theor Biol; 1987 Jan 21; 124(2):173-89. PubMed ID: 3657192 [Abstract] [Full Text] [Related]
3. Kinetic study of an enzyme-catalysed reaction in the presence of novel irreversible-type inhibitors that react with the product of enzymatic catalysis. Navarro-Lozano MJ, Valero E, Varon R, Garcia-Carmona F. Bull Math Biol; 1995 Jan 21; 57(1):157-68. PubMed ID: 7833851 [Abstract] [Full Text] [Related]
4. Evolutionary optimization of the catalytic effectiveness of an enzyme. Burbaum JJ, Raines RT, Albery WJ, Knowles JR. Biochemistry; 1989 Nov 28; 28(24):9293-305. PubMed ID: 2611230 [Abstract] [Full Text] [Related]
5. Two rules of enzyme kinetics for reversible Michaelis-Menten mechanisms. Keleti T. FEBS Lett; 1986 Nov 10; 208(1):109-12. PubMed ID: 3770204 [Abstract] [Full Text] [Related]
7. Energetics of proline racemase: racemization of unlabeled proline in the unsaturated, saturated, and oversaturated regimes. Fisher LM, Albery WJ, Knowles JR. Biochemistry; 1986 May 06; 25(9):2529-37. PubMed ID: 3755058 [Abstract] [Full Text] [Related]
10. How enzymes work: analysis by modern rate theory and computer simulations. Garcia-Viloca M, Gao J, Karplus M, Truhlar DG. Science; 2004 Jan 09; 303(5655):186-95. PubMed ID: 14716003 [Abstract] [Full Text] [Related]
11. Catalytic efficiency, kinetic co-operativity of oligomeric enzymes and evolution. Ricard J, Noat G. J Theor Biol; 1986 Dec 21; 123(4):431-51. PubMed ID: 3657187 [Abstract] [Full Text] [Related]
12. Enzymes as biosensors. 1. Enzyme memory and sensing chemical signals. Ricard J, Buc J. Eur J Biochem; 1988 Sep 01; 176(1):103-9. PubMed ID: 3416866 [Abstract] [Full Text] [Related]
13. An investigation of the relationships between rate and driving force in simple uncatalysed and enzyme-catalysed reactions with applications of the findings to chemiosmotic reactions. Stoner CD. Biochem J; 1992 Apr 15; 283 ( Pt 2)(Pt 2):541-52. PubMed ID: 1533514 [Abstract] [Full Text] [Related]
14. Why do many Michaelian enzymes exhibit an equilibrium constant close to unity for the interconversion of enzyme-bound substrate and product? Pettersson G. Eur J Biochem; 1991 Feb 14; 195(3):663-70. PubMed ID: 1999189 [Abstract] [Full Text] [Related]