Examples of 'kcat' in a sentence
Meaning of "kcat"
kcat (noun) - The catalytic constant, a measure of the efficiency of an enzyme or chemical catalyst in converting a substrate into product within a given unit of time
How to use "kcat" in a sentence
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kcat
The rate of incorporation is determined by kcat and km.
Km and kcat are measured in accordance with known procedures.
The conversion of binding energy into catalysis dictates kcat.
The reciprocal of kcat is the time taken for a single event.
This screening provides an additional level of differentiation between low kcat vehicles.
The catalytic rate constant kcat is given for each compound.
Errors in kcat and km for all values reported are less than five percent.
The activators increase kcat but have no effect on Km.
The low kcat choices will ideally include substrates that are not cleaved at all.
Profile II with high concentration of low kcat substrate.
The concentration of each high kcat substrate in the cocktail is also maintained.
This increase in efficiency may be due to an increase kcat and a decreased KM.
The means by which both kcat and km are increased can involve a variety of mechanisms.
But in oligopeptide substrate aminopeptidase from Bacillus licheniforms had still higher kcat value.
The concentration of the high kcat substrates in the TOP cocktail is increased.
See also
The kcat and Km values were obtained with the aid of the Hanes linearization method.
Determination of high and low kcat substrates This is another screening procedure.
Profile I with low concentration of high kcat substrates.
The enzyme kinetic parameters kcat and km were determined from initial rates by Hanes plot.
Analysis of the kinetic data obtained in this fashion indicates that Pep4A prevalently affects kcat.
According to the invention, the kcat values are calculated in the following way,.
Eadie-Hofstee plots were then used to calculate km and kcat.
Values for km and kcat can be calculated by the Michaelis-Menton equation.
Vmax is the maximum velocity or maximum rate . k2 is often called kcat.
Both methods produced comparable kcat values, which are shown in the table below.
The ratio kcat / km defines a measure of the catalytic efficiency of an enzyme-substrate pair.
These mutations produce smaller effects on kcat that run parallel to the effects on 1/km.
Since kcat is a direct function of Vmax, these values can be determined rather quickly.
The kinetic parameters km and kcat are shown in Table 3.
Generally, kcat / km is measured under steady state condition.
Substrates that are not well cleaved ( low kcat substrates ) are also identified.
The kcat or turnover number of the reaction was 7/minute.
Product formation in time can be described as, E . kcat.
The effect of pH on kcat for these enzymes is shown in Table 8.
This was followed by the determination of Km, Vm, kcat and the ratio kcat / Km.
It is preferred that the kcat value is determined under the conditions described in Example 7.
Thus, a strain of S. pristinaespiralis expressing a variant with a Kcat PAPA.
The kinetic parameters kcat and Km were determined for compounds with X = methyl and ethyl.
The normal catalytic rate of pyruvate decarboxylase is kcat 10 s-1.
The definition of Vmax = kcat • [ E ] total when the enzyme substrate concentration was at saturation levels.
The thiopeptolide substrate concentration is varied from 10 to 800 µM to obtain km and Kcat values.
For all other compounds the kcat was measured at pH 7.4.
For kcat values marked with an asterisk, the kcat was measured at a pH of 8.1.
R132H enzyme also displays a reduced Vmax, suggestive of a lower kcat.
