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its how enzymes and substrates are attracted to each other
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∙ 11y ago
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What happens to the affinity between the substate and enzyme when the enzyme becomes denatured?
Affinity decreases as the enzyme's geometry is modified by being denatured. It will no longer properly fit the active site.
What does each enzyme have a high affinity for in cellular metabolism?
solute
How can an enzymes affinity be altered?
Almost all enzymes are proteins, and like other proteins, they can be denatured by exposure to heat, radiation, electricity, certain chemicals, or fluids with extreme pH values.For example, many enzymes become inactive at 45°C, and nearly all of them are denatured at 55°C.
Can you find agonist affinity from EC50?
no agonist affinity can be found from IC50 values where as antagonist affinity can be determined using EC50
Why is it necessary for a cell to produce one enzyme molecule for every substrate molecule that needs to be catalyzed?
Because evey substrate needs its own enzyme. Every substance has it depends upon the dissociation constant for the enzyme/substrate interaction. Some enzymes can catalyze reactions for low-affinity substrates, as long as the concentration of substrate molecules is great enough.
What happens to the affinity between the substate and enzyme when the enzyme becomes denatured?
Affinity decreases as the enzyme's geometry is modified by being denatured. It will no longer properly fit the active site.
What does it mean when an enzyme has a low value for its Michaelis constant?
It indicates that the enzyme has a high affinity for the substrate.
Where does an enzyme bind to the substrate?
In the active site, with high affinity.
What does each enzyme have a high affinity for in cellular metabolism?
solute
What is Km in an enzyme?
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 maximum speed. Thus, a low Km value means that the enzyme has a high affinity for the substrate (as a "little" substrate is enough to run the reaction at half its max speed). This is only true for reactions where substrate is limiting and the enzyme is NOT allosteric.
When was Affinity - Affinity album - created?
Affinity - Affinity album - was created in 1970.
What are three examples where Michael mensten equation can be applied?
The MM equation can be appliedTo determine the activity and specific activity of an enzymeTo determine the affinity of an enzyme to its substrate (also known as the Kd value)To see if an enzyme catalyzed reaction is being inhibited by a molecule
What has the author David A Shapiro written?
David A. Shapiro has written: 'Developmental of a novel affinity ELISA and ita application to the analysis of affinity maturation in trout' -- subject(s): Enzyme-linked immunosorbent assay, Immunology, Rainbow trout 'Changes in the curve of Spee in orthodontically treated and untreated individuals'
What is affinity?
Affinity is close relationship.
How do you determine Vmax in enzyme kinetics?
Vmax is the maxim initial velocity (Vo) that an enzyme can achieve. Initial velocity is defined as the catalytic rate when substrate concentration is high, enough to saturate the enzyme, and the product concentration is low enough to neglect the rate of the reverse reaction. Therefore, the Vmax is the maximum catalytic rate that can be achieved by a particular enzyme. Km is determined as the substrate concentration at which 1/2 Vmax is achieved. This kinetic parameter therefore importantly defines the affinity of the substrate for the enzyme. These two parameters for a specific enzyme defines: Vmax - the rate at which a substrate will be converted to product once bound to the enzyme. Km - how effectively the enzyme would bind he substrate, hence affinity.
What element has no electron affinity?
Helium has no electron affinity.
Use affinity in a sentence?
He has an affinity for diet Cokes.
