Jun 1, 2024 · The Michaelis constant (Km) is a means of characterising an enzyme's affinity for a substrate. The Km in an enzymatic reaction is the substrate concentration at which the reaction rate is half its ...

Mar 16, 2019 · The units of Km are generally in terms of concentration (e.g. molar), so Km is not a rate. Km is usually interpreted to be a measure of the enzyme's affinity for the substrate. When the substrate concentration is greater than Km, the enzyme is easily able to grab onto the substrate, while when the substrate concentration is less than Km,

Feb 7, 2025 · To calculate Vmax and Km for enzyme activity data, you can use the Michaelis-Menten equation. Vmax is the maximum reaction rate of the enzyme, and Km is the substrate concentration at which the ...

Jan 19, 2025 · Uncompetitive inhibition decreases the Michaelis-Menten constant (Km) in enzyme kinetics. This is because uncompetitive inhibitors bind to the enzyme-substrate complex, preventing the release of ...

Sep 15, 2009 · We know that Vmax depends on enzyme concentration since Vmax = k2[E] However, what I have trouble grasp is that why Km does not depend on enzyme concentration if Km is the substrate concentration where V = 1/2 Vmax. If you increase Vmax, shouldn't Km increase as well since it is dependent on...

Oct 2, 2012 · I'm reading a reference right now on an enzyme I'm interested in, and the reported Km for the enzyme is in the mM range, which is much higher than the typical concentration of the enzyme's substrate that is found in the cell. The reference mentions "Enzymes often work at substrate concentrations below the Km, because the regulation of the

Mar 25, 2004 · If let's say enzyme A has a higher value of kcat, then in order to have an equivalent ratio enzyme B must have an appreciably smaller value of KM. This means that enzyme B has an very strong affinity for its substrate and is not likely to be as promiscuous with its binding as enzyme A .

Feb 6, 2025 · Uncompetitive inhibitors decrease Km in enzyme kinetics because they bind to the enzyme-substrate complex, preventing the release of the substrate. This results in a lower apparent affinity of the ...

Feb 6, 2025 · The kcat/Km value in enzyme kinetics is significant because it represents the efficiency of an enzyme in converting substrate to product. It is a measure of how quickly an enzyme can catalyze a ...

Feb 6, 2025 · Km represents the substrate concentration at which the enzyme works at half of its maximum speed, while kcat is the turnover number, indicating how quickly the enzyme can convert substrate into ...