+ Site Statistics
+ Search Articles
+ PDF Full Text Service
How our service works
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ Translate
+ Recently Requested

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



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



Biochimica et Biophysica Acta 488(1): 13-24



Theoretical aspects of the kinetics of interaction of enzymes with lipid substrates are presented. Rate equations were written and used to simulate v versus S curves for the following cases: (a) The substrate is adsorbed onto non-catalytic sites of the enzyme or to other proteins accompanying the enzyme. (b) The enzyme is adsorbed, via non-catalytic sites to aggregated forms of the substrate. (c) The substrate is adsorbed onto an externally added protein such as albumin. Although all rate equations are based on the Michaelis-Menten kinetic theory, most of the simulated v vs. S curves were not hyperbolic and some of the v vs. E curves not linear.

Please choose payment method:






(PDF emailed within 0-6 h: $19.90)

Accession: 041175430

Download citation: RISBibTeXText

PMID: 889854

DOI: 10.1016/0005-2760(77)90118-7


Related references

Rate equations and simulation curves for enzymatic reactions which utilize lipids as substrates. I. Interaction of enzymes with the monomers and micelles of soluble, amphiphilic lipids. Biochimica et Biophysica Acta 488(1): 1-12, 1977

Rate equations and simulation curves for enzymatic reactions utilizing lipids as substrates. Israel Journal of Medical Sciences 11(11): 1172, 1975

Calculation of steady-state rate equations and the fluxes between substrates and products in enzyme reactions. Biochemical Journal 161(3): 517-526, 1977

Quantitative determination of the steady-state kinetics of multienzyme reactions using the algebraic rate equations for the component single-enzyme reactions. Biochemical Journal 291: 585-593, 1993

Simple and direct derivation of steady-state rate equations for enzyme catalysed reactions involving two substrates and two products. Biochemical Education 24(2): 106-108, 1996

The effect of hydrogen ions on the steady state multiplicity of substrate-inhibited enzymatic reactions. III. Asymmetrical steady states in enzyme membranes. Applied Biochemistry and Biotechnology 9(5-6): 455-474, 1984

Multiple Intermediates in Steady State Enzyme Kinetics. V. Effect of Ph on the Rate of a Simple Enzymatic Reaction. Journal of Biological Chemistry 238: 2804-2810, 1963

The computerized derivation of steady-state rate equations for enzyme kinetics. Biochemical Journal 223(2): 551-553, 1984

The kinetics of enzyme-catalyzed reactions with two or more substrates or products. I. Nomenclature and rate equations. Biochimica et Biophysica Acta 67: 104-137, 1963

Effective rate constants and general isotope effect equations for steady state enzymatic reactions with multiple isotope sensitive steps. Bioorganic Chemistry 20(2): 95-106, 1992

Steady-state enzyme kinetics with high-affinity substrates or inhibitors. A statistical treatment of dose-response curves. Biochemical Journal 135(1): 101-107, 1973

Integrated Steady-State Rate Equations For Enzyme-Catalyzed Reactions. Biochimica et Biophysica Acta 85: 1-10, 1964

Evaluation of the steady state rate equation for two substrate enzymatic reactions. Biokhimiya 56(9): 1661-1664, 1991

The kinetics of enzyme-catalyzed reactions with two or more substrates or products. I. Nomenclature and rate equations. 1963. Biochimica et Biophysica Acta 1000: 213-220, 1989

The probability of obtaining complex kinetic curves for enzyme mechanisms with cubic terms in the pseudo steady state rate equations. Journal of Theoretical Biology 95(3): 465-488, 1982