Michaelis-Menten equation


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Mi·chae·lis-Men·ten e·qua·tion

(mi-kā'lis men'tĕn),
an initial-rate equation for a single-substrate noncooperative enzyme-catalyzed reaction relating the initial velocity to the initial substrate concentration; v = Vmax [S]/(Km + [S]), where v is the initial velocity of the reaction, Vmax is the maximum velocity, [S] is the initial substrate concentration, and Km is the Michaelis constant. Similar equations can be derived for conditions in which the product is present and for multisubstrate enzymes.
[Leonor michaelis, Maud L. Menten]

Michaelis-Menten equation

An equation for evaluating enzyme kinetics in a system: v = VS/Km + S, where v = Initial velocity of reaction; V = Maximum (or limiting) velocity; S = Substrate concentration; and Km =  Michaelis constant.

The MME assumes that rapid equilibrium is reached among the enzyme, its substrate and the enzyme-substrate complex, and that the initial velocity of the reaction is proportional to the concentration of the enzyme-substrate complex.

Menten,

Maud Leonora, Canadian pathologist in U.S., 1879-1960.
Michaelis-Menten constant - Synonym(s): Michaelis constant
Michaelis-Menten equation - see under Michaelis
Michaelis-Menten hypothesis - see under Michaelis
Victor-Michaelis-Menten equation - Synonym(s): Michaelis-Menten equation

Michaelis,

Leonor, German-U.S. chemist and physician, 1875-1949.
Michaelis buffer
Michaelis constant - the true dissociation constant for the enzyme-substrate binary complex in a single-substrate rapid equilibrium enzyme-catalyzed reaction. Synonym(s): Michaelis-Menten constant
Michaelis-Gutmann body - a rounded homogenous body containing calcium and iron found within macrophages in the bladder wall in malacoplakia.
Michaelis-Menten constant - Synonym(s): Michaelis constant
Michaelis-Menten equation - an initial-rate equation for a single-substrate noncooperative enzyme-catalyzed reaction relating the initial velocity to the initial substrate concentration. Synonym(s): Victor-Michaelis-Menten equation
Michaelis-Menten hypothesis - that a complex is formed between an enzyme and its substrate (the O'Sullivan-Tompson hypothesis), which complex then decomposes to yield free enzyme and the reaction products (Brown hypothesis), the latter rate determining the overall rate of substrate-product conversion.
Victor-Michaelis-Menten equation - Synonym(s): Michaelis-Menten equation
References in periodicals archive ?
These values were determined based on the relationship between 1/[S] with 1/[I.sub.pa]] of the Michaelis-Menten equation and Lineweaver-Burk plot (Fig.
The values of [V.sub.max] and [K.sub.m], of AGIP were exactly determined from Lineweaver-Burk plots by using Michaelis-Menten equation and its reciprocal, and then the values of kcat, and catalytic activity were calculated.
The Michaelis-Menten equation determines the rate of reaction:
(37) described that processive enzymes such as cellulases also show a hyperbolic relationship between steady-state rate and substrate concentration, the kinetic parameters are more complex and may not be calculated directly from the Michaelis-Menten equation. Kinetics of ChiA from S.
The kinetic models Michaelis-Menten equation and substrate inhibition equation were fitted to the data of metabolic rates versus substrate concentrations and displayed in (1) and (2), respectively.
Usually, the process of photosynthesis is expressed using the Michaelis-Menten equation [2, 4, 13, 14].
The Michaelis-Menten equation was used by GraphPad (Version 6, GraphPad Software Inc., San Diego, CA) to calculate the apparent Michaelis-Menten constant ([K.sub.m]) and the apparent maximum velocity ([V.sub.max]).
Frontal analysis made it possible to treat chromatography as a saturation phenomenon and express the phenomenon by a simple equation equivalent to the Langmuir's adsorption isotherm and also to the Michaelis-Menten equation. Consequently, it allowed us to obtain parameters necessary for description of molecular interaction, i.e., equilibrium constant and binding capacity.
The activity is defined as the hydrolysis of ATC (mol) per minute.In order to analyze the efficiency of the enzyme catalysis, the substrate specificity was determined through enzyme kinetics utilizing Michaelis-Menten equation. Three different substrates i.e.
Then, for each trial, the initial velocity of ClpB was plotted versus the final concentration of ATP; and the data set was fit using nonlinear regression according to the Michaelis-Menten equation. According to the experimental results, the ATP-dependent maximum initial velocity of ClpB is 4.3 x 10-8 M s-1, the Michaelis constant is 370 pM, and the catalytic constant is 1.5 x 10-2 s-1.
The kinetic parameters of the Michaelis-Menten equation (Equation 7) for free and immobilized enzyme were determined by varying the concentration of olive oil from 1 to 70% in the enzymatic hydrolysis reaction, as described previously.
[K.sub.m] and [V.sub.max] were determined by fitting the velocities to Michaelis-Menten equation by nonlinear regression method using Origin 6.1: