Kinetic parameters of the acyl-enzyme mechanism

1990 ◽  
Vol 270 (2) ◽  
pp. 563-563
Author(s):  
Stephen G. Waley
Keyword(s):  
Kinetic Parameters ◽  
Enzyme Mechanism

MEASUREMENT OF STEROID BINDING PROTEINS

1970 ◽  
Vol 65 (1_Suppl) ◽  
pp. S104-S121 ◽  
Author(s):  
E. E. Baulieu ◽  
J. P. Raynaud ◽  
E. Milgrom
Keyword(s):  
Kinetic Parameters ◽  
Binding Proteins ◽  
Binding Specificity ◽  
Binding Parameters ◽  
Target Organs ◽  
Biological Mixtures ◽  
Steroid Binding Proteins ◽  
Steroid Binding ◽  
Steroid Binding Protein

ABSTRACT A brief review of the characteristics of steroid binding proteins found in the plasma and in some target organs is presented, followed by some general remarks on binding »specificity« and binding parameters. Useful techniques for measuring binding parameters at equilibrium are reported, both those which keep the equilibrium intact and those which implicate its disruption. A concept is developed according to which the determination of a specific steroid binding protein is based on the »differential dissociation« of the several steroid binding complexes present in most biological mixtures. Methods which allow determination of the kinetic parameters of the binding systems are also presented. Various representations of the binding and therefore different modes of graphic representation and calculation are discussed, including the recent »proportion graph« method.

THE INFLUENCE OF ETHANOL ON THE CONVERSION OF PREGNENOLONE TO PROGESTERONE BY HUMAN PLACENTAL MICROSOMES

1974 ◽  
Vol 76 (1) ◽  
pp. 178-188 ◽  
Author(s):  
H. Lübbert ◽  
K. Pollow ◽  
R. Wagner ◽  
J. Hammerstein
Keyword(s):  
Kinetic Parameters ◽  
Enzyme Preparation ◽  
Ethanol Concentration ◽  
Hydroxysteroid Dehydrogenase ◽  
Product Formation ◽  
Linear Increase ◽  
Maximal Velocity ◽  
Microsomal Enzyme ◽  
Temperature Optima ◽  
Substrate Concentrations

ABSTRACT The effects of ethanol on kinetic parameters of placental Δ5-3β-hydroxysteroid dehydrogenase were studied. In the presence of high pregnenolone concentrations (50 μm, [S] > Km) the microsomal enzyme preparation exhibited an almost linear increase in activity as the ethanol concentration in the medium was raised from 2.5 to 15 % (v/v). At lower substrate concentrations ([S] << Km) ethanol caused inhibition. Other effects of ethanol were: linearity of product formation with time was prolonged; the maximal velocity was markedly increased; the Km for pregnenolone slightly decreased with increasing ethanol concentrations (2.5 to 10 %, v/v) whereas the Km for NAD remained the same. The pH and temperature optima of the reaction were unaffected by ethanol. Other organic solvents caused similar effects.

Protein Flexibility Catalyzes a Cell Signaling Reaction of the Ras-GAP Complex

2019 ◽  
Author(s):  
Keiei Kumon ◽  
Masahiro Higashi ◽  
Shinji Saito ◽  
Shigehiko Hayashi
Keyword(s):  
Cell Signaling ◽  
Conformational Changes ◽  
Catalytic Reaction ◽  
Protein Complex ◽  
Enzyme Mechanism ◽  
Activation Free Energy ◽  
Chemical Catalysis ◽  
Simple Chemical ◽  
A Cell ◽  
Enzyme Molecules

Many enzyme molecules exhibit characteristic global and slow dynamics which furnish them with allostery realizing remarkable molecular functionalities more than simple chemical catalysis. However, molecular mechanism of a catalytic reaction associated with the molecular flexibility of enzymes is not well-understood. Here we report a hybrid molecular simulation study on GTPase activity of a Ras-GAP protein complex for cell signaling termination. We unveiled that extensive conformational changes of the protein complex and exclusion of internal water molecules are induced upon the transition state (TS) formation in the catalytic reaction and significantly lower the reaction activation free energy. We also revealed that tumor-related mutations perturb those conformational changes upon the TS formation, leading to reduction of the catalytic activity. The findings of the remarkably dynamic protein conformation directly linking to the catalytic reaction have broad implications for understanding of enzyme mechanism and for developments of allosteric drugs and novel catalysts.

Evaluation of Kinetic Parameters at the Transport of Indole-3-acetic Acid Through Bulk Liquid Membranes

2017 ◽  
Vol 68 (5) ◽  
pp. 903-907
Author(s):  
Ecaterina Anca Serban ◽  
Ioana Diaconu ◽  
Elena Ruse ◽  
Georgiana Ileana Badea ◽  
Adriana Cuciureanu ◽  
...  
Keyword(s):  
Acetic Acid ◽  
Kinetic Parameters ◽  
Trioctylphosphine Oxide ◽  
Bulk Liquid ◽  
Transport Parameters ◽  
Kinetics Parameters ◽  
First Order ◽  
Phase Concentration ◽  
Feed Phase ◽  
Indole 3 Acetic Acid

Indole-3-acetic acid is a growth phytohormone considered the most important representative of auxin class. This paper presents the assessment of some kinetic parameters in the process of transport of indole-3-acetic acid taking into consideration the kinetic model of consecutive irreversible first order reactions. It was pursued the influence upon the process of parameters such as: feed phase concentration, stripping phase concentration in the presence of two type carriers: tributyl phosphate (TBP) and trioctylphosphine oxide (TOPO). Depending on these transport parameters were calculated kinetics parameters such as: pseudo-first-order apparent membrane entrance and exit rate constants, the maximum flux at the entrance and exit out of the membrane. The highest values of the transport flux is obtained in the presence of carrier trioctylphosphine oxide (TOPO) at the concentration in the feed phase of 10-4 mol/L indole-3-acetic acid and a concentration of 10--2mol/L NaOH in the stripping phase.

A Technique to Determine Unsteady-State Inhibition Kinetics in the Activated Sludge Process

1989 ◽  
Vol 21 (6-7) ◽  
pp. 593-602 ◽  
Author(s):  
Andrew T. Watkin ◽  
W. Wesley Eckenfelder
Keyword(s):  
Activated Sludge ◽  
Kinetic Parameters ◽  
Curve Fitting ◽  
Glucose Utilization ◽  
Batch Reactor ◽  
Synthetic Data ◽  
Utilization Rate ◽  
Fitting Algorithm ◽  
Test Reactor ◽  
Two Parameter

A technique for rapidly determining Monod and inhibition kinetic parameters in activated sludge is evaluated. The method studied is known as the fed-batch reactor technique and requires approximately three hours to complete. The technique allows for a gradual build-up of substrate in the test reactor by introducing the substrate at a feed rate greater than the maximum substrate utilization rate. Both inhibitory and non-inhibitory substrate responses are modeled using a nonlinear numerical curve-fitting technique. The responses of both glucose and 2,4-dichlorophenol (DCP) are studied using activated sludges with various acclimation histories. Statistically different inhibition constants, KI, for DCP inhibition of glucose utilization were found for the various sludges studied. The curve-fitting algorithm was verified in its ability to accurately retrieve two kinetic parameters from synthetic data generated by superimposing normally distributed random error onto the two parameter numerical solution generated by the algorithm.

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