Rate equations for two enzyme-catalyzed Ping Pong bi bi reactions in series: General formulation for two reaction loops joined by a common vertex and deduction of a reaction loop selectivity factor

2021 ◽  
pp. 108234
Author(s):  
Dominicky Cristina Serrano ◽  
David Alexander Mitchell ◽  
Nadia Krieger
Keyword(s):  
Rate Equations ◽  
Common Vertex ◽  
Selectivity Factor ◽  
Ping Pong ◽  
In Series ◽  
Reaction Loop

Developing the rate equations for two enzymatic Ping-Pong reactions in series: Application to the bio-synthesis of Bis(2-ethylhexyl) azelate

2020 ◽  
Vol 161 ◽  
pp. 107691 ◽  
Author(s):  
M. Gómez ◽  
M.D. Murcia ◽  
M. Serrano-Arnaldos ◽  
E. Gómez ◽  
J.L. Gómez ◽  
...  
Keyword(s):  
Rate Equations ◽  
Ping Pong ◽  
In Series ◽  
Bio Synthesis

scholarly journals Studies on the mechanism and kinetics of the 2-oxoglutarate dehydrogenase system from pig heart

1977 ◽  
Vol 161 (3) ◽  
pp. 569-581 ◽  
Author(s):  
C L McMinn ◽  
J H Ottaway
Keyword(s):  
Initial Rate ◽  
Optimization Technique ◽  
Random Order ◽  
The Other ◽  
Rate Equations ◽  
Kinetic Properties ◽  
Ping Pong ◽  
System 2 ◽  
Dehydrogenase System ◽  
Oxoglutarate Dehydrogenase

1. The kinetic properties of the 2-oxoglutarate dehydrogenase system were investigated. To this end, initial-velocity studies were carried out by the method of Fromm [(1967) Biochim. Biophys. Acta 139, 221-230]. Reciprocal plots of the results did not agree with those expected for the Hexa Uni Ping Pong mechanism previously proposed for the system. 2. The measured initial velocities were fitted to initial-rate equations corresponding to several possible mechanisms by using a computer optimization technique. Statistical analyses performed on the results of the optimization studies indicated that one mechanism was a significantly better fit to the experimental data than the other mechanisms tested. This mechanism is one in which there is a random order of binding of NAD+ and CoA and release of succinyl-CoA, although the binding of 2-oxoglutarate and release of CO2 is still given a Ping Pong mechanism, which precedes the binding of the other substrates. These conclusions were supported by NADH-inhibition studies. 3. The usefulness of the method of fitting initial-rate data to rate equations and the applicability of the proposed enzymic mechanism to the enzyme complex are discussed.

scholarly journals Calculation of steady-state rate equations and the fluxes between substrates and products in enzyme reactions

1977 ◽  
Vol 161 (3) ◽  
pp. 517-526 ◽  
Author(s):  
H G Britton
Keyword(s):  
Steady State ◽  
Enzyme Reaction ◽  
Rate Equations ◽  
Enzyme Mechanisms ◽  
Algebraic Form ◽  
Ping Pong ◽  
Steady State Rate ◽  
Enzyme Intermediates ◽  
State Rate ◽  
Velocity Equation

1. Two methods are described for deriving the steady-state velocity of an enzyme reaction from a consideration of fluxes between enzyme intermediates. The equivalent-reaction technique, in which enzyme intermediates are systematically eliminated and replaced by equivalent reactions, appears the most generally useful. The methods are applicable to all enzyme mechanisms, including three-substrate and random Bi Bi Ping Pong mechanisms. Solutions are obtained in algebraic form and these are presented for the common random Bi Bi mechanisms. The steady-state quantities of the enzyme intermediates may also be calculated. Additional steps may be introduced into enzyme mechanisms for which the steady-state velocity equation is already known. 2. The calculation of fluxes between substrates and products in three-substrate and random Bi Bi Ping Pong mechanisms is described. 3. It is concluded that the new methods may offer advantages in ease of calculation and in the analysis of the effects of individual steps on the overall reaction. The methods are used to show that an ordered addition of two substrates to an enzyme which is activated by another ligand will not necessarily give hyperbolic steady-state-velocity kinetics or the flux ratios characteristic of an ordered addition, if the dissociation of the ligand from the enzyme is random.

Effects of modifiers on the kinetics of two-substrate enzyme reactions

1968 ◽  
Vol 46 (11) ◽  
pp. 1381-1396 ◽  
Author(s):  
J. Frank Henderson
Keyword(s):  
Steady State ◽  
Binding Sites ◽  
Rate Equations ◽  
Enzyme Reactions ◽  
Ping Pong ◽  
Steady State Rate ◽  
State Rate ◽  
Kinetics Of

Steady state rate equations have been derived for ordered bi bi and ping pong bi bi reactions in which there are (a) one or two nonsubstrate modifiers, (b) two different binding sites for a single nonsubstrate modifier, (c) one or two substrates acting as modifiers, and (d) both nonsubstrate modifiers and substrates acting as modifiers. The deviation of these equations from the Michaelis–Menten equation is shown and methods are suggested by which many of these mechanisms can be distinguished experimentally.

scholarly journals Rat liver mitochondrial monoamine oxidase. A change in the reaction mechanism on solubilization

1975 ◽  
Vol 145 (2) ◽  
pp. 311-321 ◽  
Author(s):  
M D Houslay ◽  
K F Tipton
Keyword(s):  
Monoamine Oxidase ◽  
Rat Liver ◽  
Bound State ◽  
Monoamine Oxidase A ◽  
Rate Equations ◽  
British Library ◽  
Ping Pong ◽  
Mitochondrial Monoamine Oxidase ◽  
Lending Library ◽  
Membrane Bound

1. The kinetics of benzylamine oxidation by a soluble preparation of rat liver mitochondrial monoamine oxidase were investigated and were shown to conform to adouble-displacement (or Ping Pong) mechanism. 2. The pathway differs in detail from that followed by other amine oxidases, including the membrane-bound enzyme in rat liver mitochondrial outer membranes. 3. It is suggested taht the conformation of the protein in the soluble state differs from that in the membrane-bound state. 4. The full rate equations for this mechanism have been deposited as Supplementary Publication SUP 50039 (5pages) at the British Library (lending Division) (formely the National Lending Library for Science and Technology), Boston Spa, Yorks, LS237BQ, U.K.. from whom copies can be obtained on the terms indicated in Biochem. J (1975) 145,5.

The Kinetic Analysis of Bod and Nitrogen Removal in an Oxidation Ditch

1985 ◽  
Vol 17 (2-3) ◽  
pp. 291-302 ◽  
Author(s):  
Y. Terashima ◽  
M. Ishikawa
Keyword(s):  
Nitrogen Removal ◽  
Kinetic Models ◽  
Design Procedure ◽  
Operating Conditions ◽  
Rate Equations ◽  
Simultaneous Removal ◽  
Organic Substances ◽  
Oxidation Ditch ◽  
In Series ◽  
Typical Design

The simultaneous removal of nitrogen as well as organic substances is one of important characteristics of the oxidation ditch process. To describe this phenomena, synthetic kinetic models including the rates of BOD oxidation, nitrification, denitrification, DO and alkalinity changes, and sludge growth were proposed in this study. Rate equations for these mechanisms were mainly based on Monod type kinetics taking into account several limiting effects among these mechanisms. To develop the design procedure, these kinetic models were combined with the tank-in-series model having circulating and back flows. They were analyzed numerically for typical design and operating conditions. From these computer simulations, successful results to explain these complicated phenomena and several design and operating bases were obtained.

Dielectronic Recombination in the Average-Atom Model

1988 ◽  
Vol 102 ◽  
pp. 215
Author(s):  
R.M. More ◽  
G.B. Zimmerman ◽  
Z. Zinamon
Keyword(s):  
Detailed Balance ◽  
Systematic Errors ◽  
Dielectronic Recombination ◽  
Rate Equations ◽  
Strong Correlations ◽  
Dense Plasmas ◽  
Atom Model ◽  
New Feature ◽  
Average Atom Model ◽  
Attachment Process

Autoionization and dielectronic attachment are usually omitted from rate equations for the non–LTE average–atom model, causing systematic errors in predicted ionization states and electronic populations for atoms in hot dense plasmas produced by laser irradiation of solid targets. We formulate a method by which dielectronic recombination can be included in average–atom calculations without conflict with the principle of detailed balance. The essential new feature in this extended average atom model is a treatment of strong correlations of electron populations induced by the dielectronic attachment process.

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