184 related articles for article (PubMed ID: 8518291)
1. Optimal kinetic design of enzymes in a linear metabolic pathway.
Pettersson G
Biochim Biophys Acta; 1993 Jun; 1164(1):1-7. PubMed ID: 8518291
[TBL] [Abstract][Full Text] [Related]
2. Evolutionary optimization of the catalytic efficiency of enzymes.
Pettersson G
Eur J Biochem; 1992 May; 206(1):289-95. PubMed ID: 1587280
[TBL] [Abstract][Full Text] [Related]
3. A new approach for determination of the selectively favoured kinetic design of enzyme reactions.
Pettersson G
J Theor Biol; 1996 Nov; 183(2):179-83. PubMed ID: 8977876
[TBL] [Abstract][Full Text] [Related]
4. A kinetic description of sequential, reversible, Michaelis-Menten reactions: practical application of theory to metabolic pathways.
Brooks SP; Storey KB
Mol Cell Biochem; 1992 Sep; 115(1):43-8. PubMed ID: 1435764
[TBL] [Abstract][Full Text] [Related]
5. 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; 195(3):663-70. PubMed ID: 1999189
[TBL] [Abstract][Full Text] [Related]
6. Kinetic parameters of enzymatic reactions in states of maximal activity; an evolutionary approach.
Heinrich R; Hoffmann E
J Theor Biol; 1991 Jul; 151(2):249-83. PubMed ID: 1943142
[TBL] [Abstract][Full Text] [Related]
7. Mathematical modelling of dynamics and control in metabolic networks. I. On Michaelis-Menten kinetics.
Palsson BO; Lightfoot EN
J Theor Biol; 1984 Nov; 111(2):273-302. PubMed ID: 6513572
[TBL] [Abstract][Full Text] [Related]
8. Rates of reactions catalysed by a dimeric enzyme. Effects of the reaction scheme and the kinetic parameters on co-operativity.
Ishikawa H; Ogino H; Oshida H
Biochem J; 1991 Nov; 280 ( Pt 1)(Pt 1):131-7. PubMed ID: 1741741
[TBL] [Abstract][Full Text] [Related]
9. Mathematical modelling of dynamics and control in metabolic networks. V. Static bifurcations in single biochemical control loops.
Palsson BO; Lightfoot EN
J Theor Biol; 1985 Mar; 113(2):279-98. PubMed ID: 3999779
[TBL] [Abstract][Full Text] [Related]
10. Modelling of chemical reactions catalysed by membrane-bound enzymes. Determination and significance of the kinetic constants.
Heirwegh KP; Meuwissen JA; Van den Steen P; De Smedt H
Biochim Biophys Acta; 1989 Apr; 995(2):151-9. PubMed ID: 2930793
[TBL] [Abstract][Full Text] [Related]
11. Henri-Michaelis-Menten kinetics of reversible enzymic reactions, and the determination of rate constants from kinetic constants.
Barnsley EA
Sci Prog; 2022; 105(2):368504221100027. PubMed ID: 35549765
[TBL] [Abstract][Full Text] [Related]
12. Validity of the Michaelis-Menten equation--steady-state or reactant stationary assumption: that is the question.
Schnell S
FEBS J; 2014 Jan; 281(2):464-72. PubMed ID: 24245583
[TBL] [Abstract][Full Text] [Related]
13. Evaluation of rate law approximations in bottom-up kinetic models of metabolism.
Du B; Zielinski DC; Kavvas ES; Dräger A; Tan J; Zhang Z; Ruggiero KE; Arzumanyan GA; Palsson BO
BMC Syst Biol; 2016 Jun; 10(1):40. PubMed ID: 27266508
[TBL] [Abstract][Full Text] [Related]
14. Exact and approximate solutions for the decades-old Michaelis-Menten equation: Progress-curve analysis through integrated rate equations.
Goličnik M
Biochem Mol Biol Educ; 2011; 39(2):117-25. PubMed ID: 21445903
[TBL] [Abstract][Full Text] [Related]
15. Rate equations and simulation curves for enzymatic reactions which utilize lipids as substrates. II. Effect of adsorption of the substrate or enzyme on the steady-state kinetics.
Gatt S; Bartfai T
Biochim Biophys Acta; 1977 Jul; 488(1):13-24. PubMed ID: 889854
[TBL] [Abstract][Full Text] [Related]
16. Efficiency and design of simple metabolic systems.
Heinrich R; Holzhütter HG
Biomed Biochim Acta; 1985; 44(6):959-69. PubMed ID: 4038290
[TBL] [Abstract][Full Text] [Related]
17. Single-molecule Michaelis-Menten equations.
Kou SC; Cherayil BJ; Min W; English BP; Xie XS
J Phys Chem B; 2005 Oct; 109(41):19068-81. PubMed ID: 16853459
[TBL] [Abstract][Full Text] [Related]
18. Deviations from Michaelis-Menten kinetics. The possibility of complicated curves for simple kinetic schemes and the computer fitting of experimental data for acetylcholinesterase, acid phosphatase, adenosine deaminase, arylsulphatase, benzylamine oxidase, chymotrypsin, fumarase, galactose dehydrogenase, beta-galactosidase, lactate dehydrogenase, peroxidase and xanthine oxidase.
Bardsley WG; Leff P; Kavanagh J; Waight RD
Biochem J; 1980 Jun; 187(3):739-65. PubMed ID: 6821369
[TBL] [Abstract][Full Text] [Related]
19. Description of enzyme kinetics in reversed micelles. 1. Theory.
Verhaert RM; Hilhorst R; Vermuë M; Schaafsma TJ; Veeger C
Eur J Biochem; 1990 Jan; 187(1):59-72. PubMed ID: 2298210
[TBL] [Abstract][Full Text] [Related]
20. The reversible Hill equation: how to incorporate cooperative enzymes into metabolic models.
Hofmeyr JH; Cornish-Bowden A
Comput Appl Biosci; 1997 Aug; 13(4):377-85. PubMed ID: 9283752
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
