What are some real life examples of the effects of temperature and pH on enzyme activity?
Q. What are some real life examples of the effects of temperature and pH on enzyme activity? Please and thank you.
Asked by nicolejclark - Sat Mar 8 23:39:12 2008 - - 1 Answers - 0 Comments
A. hey, click on the link and scroll down to read under the heading that says real life applications, "the body, food, and digestion" The only thing I can think of is that you can say in your answer that a change in temperature or pH (where appropriate) will disrupt the proper function of those things, and just list some stuff from that section of the article. I hope this helps even a little. I tried to find you something since nobody has answered your question in a while.
Answered by star - Sun Mar 9 00:34:05 2008
Q. What are some real life examples of the effects of temperature and pH on enzyme activity? Please and thank you.
Asked by nicolejclark - Sat Mar 8 23:39:12 2008 - - 1 Answers - 0 Comments
A. hey, click on the link and scroll down to read under the heading that says real life applications, "the body, food, and digestion" The only thing I can think of is that you can say in your answer that a change in temperature or pH (where appropriate) will disrupt the proper function of those things, and just list some stuff from that section of the article. I hope this helps even a little. I tried to find you something since nobody has answered your question in a while.
Answered by star - Sun Mar 9 00:34:05 2008
why is it important to know rate of enzyme activity?
Q. The purpose of the lab I'm doing is to determine the affect of enzyme concentration, substrate concentration, and environmental factors, such as temperature and pH on the rate of enzyme activity. but i was wondering, why is it important to learn about the affect that these factors cause on the rate of enzyme activity?
Asked by bjm_116 - Sun Oct 21 15:41:55 2007 - - 2 Answers - 0 Comments
A. The reason this stuff is important is because you have to understand the basics of enzyme kinetics in order to understand all other things involving enzymes. And believe me, enzymes are very important in our phsysiology. So, for example, its important to know that the more substrate you have, the faster the rate of the reaction, up to a maximum rate.
Answered by Simonizer1218 - Sun Oct 21 15:53:33 2007
Q. The purpose of the lab I'm doing is to determine the affect of enzyme concentration, substrate concentration, and environmental factors, such as temperature and pH on the rate of enzyme activity. but i was wondering, why is it important to learn about the affect that these factors cause on the rate of enzyme activity?
Asked by bjm_116 - Sun Oct 21 15:41:55 2007 - - 2 Answers - 0 Comments
A. The reason this stuff is important is because you have to understand the basics of enzyme kinetics in order to understand all other things involving enzymes. And believe me, enzymes are very important in our phsysiology. So, for example, its important to know that the more substrate you have, the faster the rate of the reaction, up to a maximum rate.
Answered by Simonizer1218 - Sun Oct 21 15:53:33 2007
Why do you use hydrogen peroxide to test enzyme activity?
Q. I did a lab at school. My question was "What effect does acidic pH have on enzyme activity?" I poured hydrogen peroxide to test it. I know hydrogen peroxide creates a chemical reaction, but why exactly did I have to pour hydrogen peroxide? This is a really stupid question, but my teacher did not clarify.
Asked by Linaaa. - Thu Dec 3 19:09:57 2009 - - 2 Answers - 0 Comments
A. Pouring hydrogen peroxide onto the enzyme is what will "denature" it. Denature = disruption of the chemical bonds so that it goes from "functioning enzyme" to "non-functioning enzyme"
Answered by california_love - Thu Dec 3 19:48:50 2009
Q. I did a lab at school. My question was "What effect does acidic pH have on enzyme activity?" I poured hydrogen peroxide to test it. I know hydrogen peroxide creates a chemical reaction, but why exactly did I have to pour hydrogen peroxide? This is a really stupid question, but my teacher did not clarify.
Asked by Linaaa. - Thu Dec 3 19:09:57 2009 - - 2 Answers - 0 Comments
A. Pouring hydrogen peroxide onto the enzyme is what will "denature" it. Denature = disruption of the chemical bonds so that it goes from "functioning enzyme" to "non-functioning enzyme"
Answered by california_love - Thu Dec 3 19:48:50 2009
Factors affecting enzyme activity - how can this be applied to real life?
Q. Lab on factors affecting enzyme activity. Can anyone give me a good example of how this can be applied to real life?
Asked by x0bl0ndie0x - Thu Oct 23 18:28:32 2008 - - 1 Answers - 0 Comments
A. it is real life...
Answered by Will B - Thu Oct 23 18:50:42 2008
Q. Lab on factors affecting enzyme activity. Can anyone give me a good example of how this can be applied to real life?
Asked by x0bl0ndie0x - Thu Oct 23 18:28:32 2008 - - 1 Answers - 0 Comments
A. it is real life...
Answered by Will B - Thu Oct 23 18:50:42 2008
What can be some possible sources of error when writing a lab report about enzyme activity?
Q. We tested the effect of concentration on enzyme activity by measuring the amount of product produced.
Asked by Pulse - Sun Feb 22 07:52:40 2009 - - 1 Answers - 0 Comments
A. well sources of error depends on what you used to do the experiment. i mean for measuing concentration you mayb used photometer and read the abs from that. and if you didnt get a reasonable result so it can be that didnt use the photometer as it has to be use. maybe the light in the photometer didnt gross the glass with the enzyme or maybe when reading the result you made some mistakes. a sources of errors always depends on your experiment and the matrial you use. i hope it helps you
Answered by stylediya18 - Sun Feb 22 08:03:30 2009
Q. We tested the effect of concentration on enzyme activity by measuring the amount of product produced.
Asked by Pulse - Sun Feb 22 07:52:40 2009 - - 1 Answers - 0 Comments
A. well sources of error depends on what you used to do the experiment. i mean for measuing concentration you mayb used photometer and read the abs from that. and if you didnt get a reasonable result so it can be that didnt use the photometer as it has to be use. maybe the light in the photometer didnt gross the glass with the enzyme or maybe when reading the result you made some mistakes. a sources of errors always depends on your experiment and the matrial you use. i hope it helps you
Answered by stylediya18 - Sun Feb 22 08:03:30 2009
Investigating an aspect of enzyme activity in fruit?
Q. Biology Investigation Research Question: Investigating an aspect of enzyme activity in fruit. Any ideas anyone? Please include enzyme name and fruit as well as how to do the experiment (basic outline of methods). Much appreciated.
Asked by ShunYang - Mon Dec 7 07:21:25 2009 - - 1 Answers - 0 Comments
A. There is an enzyme called Bromelin (Sp?) In pineapple that decomposes protein. Weigh some ground beef then put it on there for a bit, pull it off and weigh.
Answered by __A_YAHOO_USER__ - Mon Dec 7 07:32:00 2009
Q. Biology Investigation Research Question: Investigating an aspect of enzyme activity in fruit. Any ideas anyone? Please include enzyme name and fruit as well as how to do the experiment (basic outline of methods). Much appreciated.
Asked by ShunYang - Mon Dec 7 07:21:25 2009 - - 1 Answers - 0 Comments
A. There is an enzyme called Bromelin (Sp?) In pineapple that decomposes protein. Weigh some ground beef then put it on there for a bit, pull it off and weigh.
Answered by __A_YAHOO_USER__ - Mon Dec 7 07:32:00 2009
What would pH do to enzyme activity, and why?
Q. What would pH do to enzyme activity, and why?
Asked by pc4ethio e - Wed Oct 15 00:54:08 2008 - - 3 Answers - 0 Comments
A. Just like enzymes have optimal temperatures, they also have optimal pH's. In fact they are actually more important than the temperature in most cases. If your enzyme is at the wrong pH, it won't work because it can denature or alter the protein in some way. They generally work around physiological pH (7.4ish)
Answered by Julia B - Wed Oct 15 01:24:49 2008
Q. What would pH do to enzyme activity, and why?
Asked by pc4ethio e - Wed Oct 15 00:54:08 2008 - - 3 Answers - 0 Comments
A. Just like enzymes have optimal temperatures, they also have optimal pH's. In fact they are actually more important than the temperature in most cases. If your enzyme is at the wrong pH, it won't work because it can denature or alter the protein in some way. They generally work around physiological pH (7.4ish)
Answered by Julia B - Wed Oct 15 01:24:49 2008
What is the effect of enzyme concentration on enzyme activity?
Q. How does enzyme activity changes as enzyme concentration decreases and why it occurs
Asked by joeklum04 - Sat Oct 7 16:30:19 2006 - - 3 Answers - 0 Comments
A. Enzymes can only react with a certain amount of substrate in a given amount of time, so by decreasing enzyme concentration you'll decrease the speed of the reaction. The individual enzyme molecules will be reacting at the same speed, but there'll be less of them.
Answered by caladria - Sat Oct 7 16:32:57 2006
Q. How does enzyme activity changes as enzyme concentration decreases and why it occurs
Asked by joeklum04 - Sat Oct 7 16:30:19 2006 - - 3 Answers - 0 Comments
A. Enzymes can only react with a certain amount of substrate in a given amount of time, so by decreasing enzyme concentration you'll decrease the speed of the reaction. The individual enzyme molecules will be reacting at the same speed, but there'll be less of them.
Answered by caladria - Sat Oct 7 16:32:57 2006
Substrate concentration on enzyme activity experiment?
Q. I'm designing an experiment to test the effect of substrate concentration on enzyme activity.I'm using starch and amylase. The total volume of the substrate (starch) will always be 10cm3. The amylase is 1%. How much amylase should I use to get some good results? Thanks.
Asked by Car. - Fri Jan 9 13:13:51 2009 - - 1 Answers - 0 Comments
A. Well it will be hit and miss unless you know of the degree of amylase with starch. Try large increments (0, 20, 40, 60, etc.). But if you're testing substrate concentration, why are you changing the enzyme amount and not the substrate amount? You should have plates of different starch amounts and add the same amount of amylase to each.
Answered by Polo - Sat Jan 10 02:38:45 2009
Q. I'm designing an experiment to test the effect of substrate concentration on enzyme activity.I'm using starch and amylase. The total volume of the substrate (starch) will always be 10cm3. The amylase is 1%. How much amylase should I use to get some good results? Thanks.
Asked by Car. - Fri Jan 9 13:13:51 2009 - - 1 Answers - 0 Comments
A. Well it will be hit and miss unless you know of the degree of amylase with starch. Try large increments (0, 20, 40, 60, etc.). But if you're testing substrate concentration, why are you changing the enzyme amount and not the substrate amount? You should have plates of different starch amounts and add the same amount of amylase to each.
Answered by Polo - Sat Jan 10 02:38:45 2009
What effect does pH 3 have on enzyme activity?
Q. What effect does pH 3 have on enzyme activity? a. it slows down or stops the enzyme activity b. it speeds up the enzyme activity c. the pH has no effect on enzyme activity
Asked by whoaaaa - Tue Apr 22 15:25:59 2008 - - 4 Answers - 0 Comments
A. it depends on the environment youre talking about because normal pH in different organisms and organ systems varies id say A id the correct answer because im assuming that the normal pH should be closer to neutral and any deviation from that will slow down enzyme activity. but keep in mind that places like the stomach in humans should have a very acidic pH and 3 may be optimal in some organisms
Answered by Sarah - Tue Apr 22 15:31:36 2008
Q. What effect does pH 3 have on enzyme activity? a. it slows down or stops the enzyme activity b. it speeds up the enzyme activity c. the pH has no effect on enzyme activity
Asked by whoaaaa - Tue Apr 22 15:25:59 2008 - - 4 Answers - 0 Comments
A. it depends on the environment youre talking about because normal pH in different organisms and organ systems varies id say A id the correct answer because im assuming that the normal pH should be closer to neutral and any deviation from that will slow down enzyme activity. but keep in mind that places like the stomach in humans should have a very acidic pH and 3 may be optimal in some organisms
Answered by Sarah - Tue Apr 22 15:31:36 2008
Explain the effect of temperature on enzyme activity ?
Q. Explain the effect of temperature on enzyme activity ?
Asked by LIZA - Mon Nov 19 09:46:02 2007 - - 4 Answers - 0 Comments
A. as temperature increases, the speed of the substrate and the enzyme increase. This increases the enzyme activity - its simply more probable that that the enzyme and the substrate will meet and bond. The activity increases till an optimum is reached (optimum termperature). From that point on, the activity of the enzyme decreases as it starts to denature (i.e. loses its tertiary structure - remember that for enzymes structure and function are highly related!). It will eventually reach zero when the enzyme has lost its shape completely and can no longer work. hope this helps!
Answered by Lara M. - Mon Nov 19 09:56:08 2007
Q. Explain the effect of temperature on enzyme activity ?
Asked by LIZA - Mon Nov 19 09:46:02 2007 - - 4 Answers - 0 Comments
A. as temperature increases, the speed of the substrate and the enzyme increase. This increases the enzyme activity - its simply more probable that that the enzyme and the substrate will meet and bond. The activity increases till an optimum is reached (optimum termperature). From that point on, the activity of the enzyme decreases as it starts to denature (i.e. loses its tertiary structure - remember that for enzymes structure and function are highly related!). It will eventually reach zero when the enzyme has lost its shape completely and can no longer work. hope this helps!
Answered by Lara M. - Mon Nov 19 09:56:08 2007
different experiments to try to extend knowledge of enzyme activity?
Q. as many as possible please we just did the one where you test 4 variables (pH, temp, concentration of substrate and concentration of enzyme) and saw how long it took for the reaction to complete... does anyone know of anything else you could do to extend knowledge of enzyme activity? Thanks a bunch! :D
Asked by asddfasdf - Sat Feb 16 15:46:45 2008 - - 1 Answers - 0 Comments
A. Enzyme activity can be affected by other molecules. Inhibitors are molecules that decrease enzyme activity; activators are molecules that increase activity. Many drugs and poisons are enzyme inhibitors. Activity is also affected by temperature, chemical environment (e.g. pH), and the concentration of substrate. Some enzymes are used commercially, for example, in the synthesis of antibiotics. In addition, some household products use enzymes to speed up biochemical reactions (e.g., enzymes in biological washing powders break down protein or fat stains on clothes; enzymes in meat tenderizers break down proteins, making the meat easier to chew). So you might explore these possibilities to identify some experiments you could design.
Answered by ScSpec - Sat Feb 16 15:54:35 2008
Q. as many as possible please we just did the one where you test 4 variables (pH, temp, concentration of substrate and concentration of enzyme) and saw how long it took for the reaction to complete... does anyone know of anything else you could do to extend knowledge of enzyme activity? Thanks a bunch! :D
Asked by asddfasdf - Sat Feb 16 15:46:45 2008 - - 1 Answers - 0 Comments
A. Enzyme activity can be affected by other molecules. Inhibitors are molecules that decrease enzyme activity; activators are molecules that increase activity. Many drugs and poisons are enzyme inhibitors. Activity is also affected by temperature, chemical environment (e.g. pH), and the concentration of substrate. Some enzymes are used commercially, for example, in the synthesis of antibiotics. In addition, some household products use enzymes to speed up biochemical reactions (e.g., enzymes in biological washing powders break down protein or fat stains on clothes; enzymes in meat tenderizers break down proteins, making the meat easier to chew). So you might explore these possibilities to identify some experiments you could design.
Answered by ScSpec - Sat Feb 16 15:54:35 2008
The effect of enzyme concentration on enzyme activity?
Q. Summarize the effects of enzyme concentration on enzyme activity. Explain the mechanisms that causes this effect. What would cause the rate of enzyme activity to level off on a enzyme concentration? Also, what is a description of how this graph looks like? I drew a rough S-shaped curve, however I am not sure if that's right. Thorough explanations are helpful. Have a good day/night. :) And thank you!!
Asked by cobrafan - Sun Sep 20 14:23:12 2009 - - 1 Answers - 0 Comments
A. hey there 1) if you have a large concentration of your enzyme then it will act faster as more enzyme will have more active sites for the substrate to bind to this will speed up your enzymes activity 2)not sure what you mean but i think this will answer enzyme activity is based on substrate concentration if there is a lot of substrate the the enzyme will work its way through at a constant pace (it will level off on a graph) however towards the end the substrate starts to get rarer then the enzyme will have to take more time to find new substrate to act on so it will slow down 3 the graph should have two slanted sides and a flat bit across the top hope i helped
Answered by tim3000 - Sun Sep 20 17:29:08 2009
Q. Summarize the effects of enzyme concentration on enzyme activity. Explain the mechanisms that causes this effect. What would cause the rate of enzyme activity to level off on a enzyme concentration? Also, what is a description of how this graph looks like? I drew a rough S-shaped curve, however I am not sure if that's right. Thorough explanations are helpful. Have a good day/night. :) And thank you!!
Asked by cobrafan - Sun Sep 20 14:23:12 2009 - - 1 Answers - 0 Comments
A. hey there 1) if you have a large concentration of your enzyme then it will act faster as more enzyme will have more active sites for the substrate to bind to this will speed up your enzymes activity 2)not sure what you mean but i think this will answer enzyme activity is based on substrate concentration if there is a lot of substrate the the enzyme will work its way through at a constant pace (it will level off on a graph) however towards the end the substrate starts to get rarer then the enzyme will have to take more time to find new substrate to act on so it will slow down 3 the graph should have two slanted sides and a flat bit across the top hope i helped
Answered by tim3000 - Sun Sep 20 17:29:08 2009
Temperature and enzyme activity?
Q. At low temperatures the rate of enzyme reaction is very slow. An increase in temperature increases the enzyme activity. But what does it do that? What is the point?
Asked by ~CarterRose~ - Fri Oct 9 11:32:08 2009 - - 1 Answers - 0 Comments
Q. At low temperatures the rate of enzyme reaction is very slow. An increase in temperature increases the enzyme activity. But what does it do that? What is the point?
Asked by ~CarterRose~ - Fri Oct 9 11:32:08 2009 - - 1 Answers - 0 Comments
How does enzyme activity vary with concentration?
Q. How does enzyme activity vary with concentration
Asked by montena000 - Sun Oct 25 09:51:49 2009 - - 2 Answers - 0 Comments
A. Concentration of what: the enzyme or the substrate? If it's the substrate, then increasing the concentration of the substrate won't affect the rate of reaction since the same amount of enzyme will be available to act per unit time. But if you are increasing enzyme concentration, then the rate of reaction will increase accordingly since more enzymes are now available to work on the substrate but even then the rate of reaction cannot keep on increasing since there is a limited amount of substrate.(this is called the limiting factor: in this case the substrate)
Answered by SkyE - Sun Oct 25 10:08:56 2009
Q. How does enzyme activity vary with concentration
Asked by montena000 - Sun Oct 25 09:51:49 2009 - - 2 Answers - 0 Comments
A. Concentration of what: the enzyme or the substrate? If it's the substrate, then increasing the concentration of the substrate won't affect the rate of reaction since the same amount of enzyme will be available to act per unit time. But if you are increasing enzyme concentration, then the rate of reaction will increase accordingly since more enzymes are now available to work on the substrate but even then the rate of reaction cannot keep on increasing since there is a limited amount of substrate.(this is called the limiting factor: in this case the substrate)
Answered by SkyE - Sun Oct 25 10:08:56 2009
How do you test the effect of PH on enzyme activity?
Q. I know that you'd go about it by creating 5 different solutions of different phs by mixing the catalase with the h2o2 accordingly, but I am unsure of the measurements to use. Also, the catalase is the contents of a cows's liver...so is there anything special I need to do on that note? Also, what's the PH of the contents of a cow's liver? I know this seems like a lot but every little bit helps.
Asked by Eren B - Sun Oct 14 15:40:09 2007 - - 2 Answers - 0 Comments
A. if u were using 5 different solutions i would use 10ml h2o2 0ml h20 7.5ml h2o2, 2.5ml h20 5ml h2o2, 5ml h20 2.5ml h202, 7.5ml h2o 0ml h2o0 ,10ml h20 in each testube. you must always keep the volume constant eg 10ml. add a constant amount of catalase eg 1ml or a chunk of liver to each testube and time how long before bubbles start to appear. that will give u the rate of reaction. obviously the stronger the h2o2 conc, the more acidic it is. if u were wanting to be really accurate u could test the pH of each solution with a pH meter before adding the catalase. u shouldn't need to do anything special with the cows liver! just use gloves and roughly equal amounts. hope that helps!
Answered by LipglossScientist - Sun Oct 14 16:46:40 2007
Q. I know that you'd go about it by creating 5 different solutions of different phs by mixing the catalase with the h2o2 accordingly, but I am unsure of the measurements to use. Also, the catalase is the contents of a cows's liver...so is there anything special I need to do on that note? Also, what's the PH of the contents of a cow's liver? I know this seems like a lot but every little bit helps.
Asked by Eren B - Sun Oct 14 15:40:09 2007 - - 2 Answers - 0 Comments
A. if u were using 5 different solutions i would use 10ml h2o2 0ml h20 7.5ml h2o2, 2.5ml h20 5ml h2o2, 5ml h20 2.5ml h202, 7.5ml h2o 0ml h2o0 ,10ml h20 in each testube. you must always keep the volume constant eg 10ml. add a constant amount of catalase eg 1ml or a chunk of liver to each testube and time how long before bubbles start to appear. that will give u the rate of reaction. obviously the stronger the h2o2 conc, the more acidic it is. if u were wanting to be really accurate u could test the pH of each solution with a pH meter before adding the catalase. u shouldn't need to do anything special with the cows liver! just use gloves and roughly equal amounts. hope that helps!
Answered by LipglossScientist - Sun Oct 14 16:46:40 2007
how do you set up an experiment about the effect of temperature on enzyme activity?
Q. What is the procedure, method and apparatus needed? how do you observe the results?
Asked by Rebaone P - Thu Mar 6 05:18:08 2008 - - 1 Answers - 0 Comments
A. the question is not clear enough mate, but to setup an experiment to observe the effect of temperature on it's activity. you have to find an indicator to show you the amount of the material that enzyme is going to digest it and then by that indicator you can find the amount of that material in the reference temp. (23 normally) and then in elevated temperatures you have to do this again and when you compare the amounts of the material that has been digested by the enzyme then you will find out temperatures effect on the enzyme's activity, as far as i know the digestion process is an endothermic reaction and so by increasing the temperature by Arrhenius law it will lead to higher activity of enzyme.
Answered by Amir - Thu Mar 6 05:25:28 2008
Q. What is the procedure, method and apparatus needed? how do you observe the results?
Asked by Rebaone P - Thu Mar 6 05:18:08 2008 - - 1 Answers - 0 Comments
A. the question is not clear enough mate, but to setup an experiment to observe the effect of temperature on it's activity. you have to find an indicator to show you the amount of the material that enzyme is going to digest it and then by that indicator you can find the amount of that material in the reference temp. (23 normally) and then in elevated temperatures you have to do this again and when you compare the amounts of the material that has been digested by the enzyme then you will find out temperatures effect on the enzyme's activity, as far as i know the digestion process is an endothermic reaction and so by increasing the temperature by Arrhenius law it will lead to higher activity of enzyme.
Answered by Amir - Thu Mar 6 05:25:28 2008
How does pH affect enzyme activity? Other than the fact that enzymes work best at certain pH levels...?
Q. i know that enzymes have optimal ph levels but why? how does pH affect enzymes to make them work better at certain levels?
Asked by LoStOnE - Sun Mar 8 14:45:57 2009 - - 1 Answers - 0 Comments
A. Depending on the pH of the solution, a particular amino acid may or may not be protonated (depending on its pKa). This will change the charge on that particular amino acid from positive or negative to neutral (or the other way). Charge affects the hydrophobicity of that amino acid. A neutral amino acid will want to hide away from water (ie inside the protein). A charged amino acid will want to be out and about in the solution. Where an amino acid resides in relation to the solution determines the form of the protein (enzyme in this case). Form affects function. Also, the charge of an amino acid also affects how it interacts with molecules other than just the solution in which its in. For example, if the enzyme's active site… [cont.]
Answered by Erin H - Sun Mar 8 14:58:13 2009
Q. i know that enzymes have optimal ph levels but why? how does pH affect enzymes to make them work better at certain levels?
Asked by LoStOnE - Sun Mar 8 14:45:57 2009 - - 1 Answers - 0 Comments
A. Depending on the pH of the solution, a particular amino acid may or may not be protonated (depending on its pKa). This will change the charge on that particular amino acid from positive or negative to neutral (or the other way). Charge affects the hydrophobicity of that amino acid. A neutral amino acid will want to hide away from water (ie inside the protein). A charged amino acid will want to be out and about in the solution. Where an amino acid resides in relation to the solution determines the form of the protein (enzyme in this case). Form affects function. Also, the charge of an amino acid also affects how it interacts with molecules other than just the solution in which its in. For example, if the enzyme's active site… [cont.]
Answered by Erin H - Sun Mar 8 14:58:13 2009
How do changes in concentration of either the enzyme or the substrate affect enzyme activity?
Q. Consider both scenarios separatley.
Asked by speargirl - Thu May 8 09:12:29 2008 - - 1 Answers - 0 Comments
A. more enzymes make the reaction occur faster because more enzymes = more active sites for the substrate to bind with and be broken down. more substrate means reaction will get faster until a certain point when the enzymes are working at their optimum turnover rate and cannot break down substrates any faster.
Answered by Fry - Thu May 8 09:23:10 2008
Q. Consider both scenarios separatley.
Asked by speargirl - Thu May 8 09:12:29 2008 - - 1 Answers - 0 Comments
A. more enzymes make the reaction occur faster because more enzymes = more active sites for the substrate to bind with and be broken down. more substrate means reaction will get faster until a certain point when the enzymes are working at their optimum turnover rate and cannot break down substrates any faster.
Answered by Fry - Thu May 8 09:23:10 2008
How does enzyme activity vary with enzyme concentration?
Q. If possible please give a detail answer.
Asked by goofyc33023 - Mon Oct 6 14:45:42 2008 - - 3 Answers - 0 Comments
A. Enzyme activity increases linearly with enzyme concentration. This is not true for substrate concentration. Activity is asymptotic with the rate slowing down as the enzyme reaches saturation.
Answered by vballannie - Mon Oct 6 14:56:31 2008
Q. If possible please give a detail answer.
Asked by goofyc33023 - Mon Oct 6 14:45:42 2008 - - 3 Answers - 0 Comments
A. Enzyme activity increases linearly with enzyme concentration. This is not true for substrate concentration. Activity is asymptotic with the rate slowing down as the enzyme reaches saturation.
Answered by vballannie - Mon Oct 6 14:56:31 2008
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Inhibition of PI3-kinase not only blocked stimulation of methionine synthase by dopamine and IGF-1, but also reduced . enzyme activity. to zero (Table 1), indicating an absolute dependence on PI3-kinase in the human neuroblastoma cells we ...
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