The concentration of the reactants decreases.
Enzymes catalyse the reaction, which basically means they are what makes the substance react. If you have less enzymes, then you have less collisions between the enzymes and the substrate, so less enzyme substrate complexes are formed, and so the reaction is slower. Remember enzymes don't get used up!
As the reaction progresses the concentration of the reactants decreases, this generally decreases the rate of reaction. the effect can be obscured if the reaction is exothermic when the increase in temperature compensates for the reduction in concentration.
There are formulae to explain this. But today let's use an analogy. In a barn filled with hundreds of men and women that are randomly distributed a line dance caller shouts "men, hold hands with the first woman you see!" At first, the boys and girls pair up quickly. (reaction rate is fast) But as more and more pair up, those still looking have to look harder and further to find a free partner. The first 30 pairs find each other quickly. The next 15 take a bit longer. The next couple a bit longer. But those last couple of men and women in a crowd of hundred might take quite a while to pair up.
It's the same for molecules except instead of hundreds, we are talking hundreds of billions. Now, there is an exception. Suppose that that same barn were filled with 1000 men and only 100 women. When the dance caller made his announcement the girls would all pair up very quickly since there are so many men to choose from. And then the rest of the men are just out of luck.
Same for molecules. If one reagent is in extreme excess, very little slowing in the reaction rate is detectable (there can still be some but very slight). So slight in fact, that it is really negligible.
If you want the formulas... flag this as not detailed enough and I will come back and write in the actual math.
Statistically this is a contradiction like: Is there a smaller chance of people meeting each other when there are LESS people at a meeting?? However some reaction kinetic models (e.g. Monod) explain that at increasing concentration of a reactant the rate doesn't increase (=it stays constant), the so called zero-order reaction-kinetic model (saturation-model)
isn't the reason for this site iis your suppost to know the answer ??
Metabolic enzymes are the most active for human cells. The reason for this is because they regulate each biochemical reaction.
An induced fit is a change in the shape of an enzyme which allows it to react effectively with a substrate. The reason for the alteration is to speed up a chemical reaction.
expressed in the stomach, but not in the cells of the small intestine castlelearning. lol
The increase of enzyme concentration increase the rate of reaction. Given a fixed amount of substrates, it means that the substrates will be digested faster as there are more enzymes to do the work. Substrate concentration, temperature, and pH value of the surrounding where the enzymes work on also affects the rate.
humidification
Statistically this is a contradiction like: Is there a smaller chance of people meeting each other when there are LESS people at a meeting?? However some reaction kinetic models (e.g. Monod) explain that at increasing concentration of a reactant the rate doesn't increase (=it stays constant), the so called zero-order reaction-kinetic model (saturation-model)
The rate of chemical reaction increase as the concentration of the chemicals increase. The reason is obvious. There is more opportunity for the atoms to come in contact with each other. This facilitates rate of chemical reaction.
Yes. For this reason, increasing the concentration of the molecules involved increases the rate of reaction.
isn't the reason for this site iis your suppost to know the answer ??
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.
Metabolic enzymes are the most active for human cells. The reason for this is because they regulate each biochemical reaction.
The principle reason a little bit of enzyme can catalyze a reaction involving many molecules is that enzymes are not consumed by the reactions they catalyze. Enzymes are typically multi-use entities and will continue acting until all substrates are reacted.
The active site of an enzyme is the specific region where the substrate molecule(s) bind and undergo a chemical reaction. It is typically a small and highly specific pocket or groove that accommodates the substrate molecule(s) and facilitates the catalysis of the reaction by lowering the activation energy. The active site is formed by amino acid residues and often contains key functional groups that participate in the enzymatic reaction.
A reason for the decrease in net profit margin is when an increase in business running expenses incur.
An induced fit is a change in the shape of an enzyme which allows it to react effectively with a substrate. The reason for the alteration is to speed up a chemical reaction.