To answer your third question, proteases breakdown proteins into more simple amino acids for use in different proteins. Citation https://www.healthline.com/health/protein-digestion#:~:text=Once%20a%20protein%20source%20reaches,move%20into%20your%20small%20intestine.
In regards of your first question, the test for reducing sugars would be the Benedict test. The Benedict's solution will start off an aqua-blue and when heated will turn to yellow or orange. If a higher amount of reducing sugars is present, the color of the mixture will be more orange. I hope this helps...I got my info from this page: https://www.nku.edu/~whitsonma/Bio150LSite/Lab%203%20Organic/Bio150LRevMolec.html#:~:text=In%20lab%2C%20we%20used%20Benedict's,one%20particular%20reducing%20sugar%3A%20glucose.&text=Benedict's%20reagent%20starts%20out%20aqua,the%20concentration%20of%20reducing%20sugar.
1. How does a decrease in temperature affect enzymes and enzyme-bonding? 2. Can purposeful enzymatic reactions occur, can an enzyme come with the specific task of binding to specific substrates? 3. Can enzymes be renaturized?
To answer your first question, cooler temperatures lower the kinetic energy in the molecules leading to them moving less and thus bumping into one another less. This lessening in kinetic energy also can slow down the reactions.
For your second question the majority of enzymes are made to interact with a very specific substrate. This is called enzyme-substrate specificity. (Textbook)
For your third question, I found an article talking all about how they used a specific gel to retature enzymes but it went right over my head so I hope this information can answer your question. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4585781/
For your first question, I found that lowering the temperature slows the motions of the molecules and atoms which causes the flexibility to be lost. Because each enzyme has a specific optimal temperature range, decreasing the temperature slows enzyme activity. Link: https://education.seattlepi.com/enzyme-activity-affected-lower-temperatures-5527.html
Based on the information I read to answer your third question, I do not belive that enzymes can be naturally renatured but there are some solutions that can result in the partial renaturalization of enzymes. In general they can only be renatured if they were very gently denatured. https://www.britannica.com/science/renaturation
What would be considered the single most essential enzyme? Are there any enzymes with multiple binding sites?/Enzymes who can have more than 1 substrate bind to them? Are there enzymes where once denatured will continue to be functional?
To answer your third question, based on what I found, enzymes will no longer function after denaturation, and I have not found any exceptions, if there are exceptions they are exceptionally rare.
In response to your second question, there are enzymes with multiple bonding sites that are called multi-site enzymes. They serve many different roles. One example is creating a queue of substrates to speed up the enzymatic reactions.
Answering your first question, I found that Rubisco is the most abundant and important enzyme. It is the most abundant as it is found in every photosynthetic organism. It is the most important because it is in the first step of photosynthesis. Hope this helped :) Link: https://www.howplantswork.com/2010/01/19/a-step-toward-fixing-the-most-important-enzyme-on-earth/#:~:text=The%20world's%20most%20abundant%20and,sized%20trees%20in%20the%20tropics.
1) Why is Rubisco the most important enzyme? 2) How are enzymes used in other fields/ are they used for business? 3) How does the electron concentration in a solution affect the ph level?
To answer your first question, Rubisco is the most important enzyme because it is the catalyst for the first step in photosynthesis in all photosynthetic organisms.
For your second question, enzymes have many commercial purposes, which are usually fulfilled by immobilized enzymes. These industries include food, agriculture, cosmetics and pharmaceuticals
In regards of your third question, the pH of a solution is simply determined by the hydronium levels. If the hydronium concentration increases then the pH will in turn become more acidic. "The partial charge is caused by the fact that oxygen is more electronegative than hydrogen. This means that in the bond between hydrogen and oxygen, oxygen "pulls" harder on the shared electrons thus causing a partial negative charge on the molecule and causing it to be attracted to the positive charge of H+ to form hydronium" Because the hydronium is bent it causes the molecule to have a dipole moment and results in a partial charge. I hope that helps... https://chem.libretexts.org/Bookshelves/Physical_and_Theoretical_Chemistry_Textbook_Maps/Supplemental_Modules_(Physical_and_Theoretical_Chemistry)/Acids_and_Bases/Acids_and_Bases_in_Aqueous_Solutions/The_Hydronium_Ion#:~:text=The%20hydronium%20ion%20has%20a,the%20atoms%20is%20113%20degrees.
To answer your first question, Rubisco is the most important enzyme because it is in the first step of photosynthesis which converts CO2 to into sugars. Link: https://www.howplantswork.com/2010/01/19/a-step-toward-fixing-the-most-important-enzyme-on-earth/#:~:text=The%20world's%20most%20abundant%20and%20most%20important%20enzyme%20is%20RuBisCo.&text=It's%20also%20the%20most%20important,a.k.a.%2C%20the%20Calvin%20cycle).
1) Does the polarity of an enzyme affect the changes it will have towards a change in pH? 2) What happens if the substrates reaction goes wrong? Can it? 3) Can someone dumb down substrate reactions? I'm having trouble wrapping my head around the whole thing
For your third question: (Substrate turns into product) Extra simple: 1. Substrate attaches to enzyme 2. Enzyme makes substrate change shape 3. Substrate detaches and is now a product 4. Process restarts
More detailed but still simple: 1. Substrate attached to enzyme (they naturally fit together/are attracted to each other) 2. Attachment triggers enzyme to change shape, forcing the substrate to change shape. 3. Bond is now unstable between enzyme and substrate, substrate detaches and is now a product 4. Enzyme goes back to original shape 5. Process restarts
For your second question, I am not sure if substrates reactions can go wrong, if the enzyme and substrate do fit well together then I don’t belive that anything naturally could go wrong with the reaction. If something does happen like a dramatic change in tempurature or ph, then the enzyme could lose it’s ability to bind to a substrate. This could result in the denaturation of the enzyme.
In response to your first question, while it does not have an effect on the enzyme specifically, polar molecules have much weaker bonds, meaning that they break apart much easier, which would likely cause those bonds to break quickly in acidic pH levels.
1. How does the body or cell deal with denatured enzymes? 2. How quickly do enzymes normally break down substrates? Why? 3. Can molecules become stuck in the active site of enzymes and block it? Or is it just properly placed substrates that block the active site?
To answer your first question, in general I found that after an enzyme is denatured the amino acids/ monomers/ components will be recycled or if this is not possible they will become waste and excreted by the urea cycle. https://www.sciencelearn.org.nz/images/2264-denatured-enzyme
To answer your third question, it is possible for molecules to block the active site of an enzyme. These molecules are called competitive inhibitors. They are shaped very similarly to the enzyme's substrate which allows them to block the active site. For more information about inhibitors go here: https://sciencing.com/blocks-enzyme-activity-binding-active-enzyme-11545.html
To answer question two, enzyme speed is different for each type of enzyme, the fastest of which being carbonic ahydrase, being able to hydrate 1000000 CO2 molecules in one second. https://www.ncbi.nlm.nih.gov/books/NBK22380/#:~:text=In%20fact%2C%20carbonic%20anhydrase%20is,fast%20as%20the%20uncatalyzed%20one.&text=An%20enzyme%20usually%20catalyzes%20a,set%20of%20closely%20related%20reactions.
1- How, more specifically, are enzymes denatured? 2- In what ways can the enzyme catalyzing the substrate to create a product go wrong? 3- Can denatured enzymes be naturally renatured?
In response to your third question, it is highly unlikely that an enzyme can be renatured naturally. Some enzymes can be partially renatured if placed in the correct solution, however, more often then not it can't be done, even with human help.
Question 1- Enzymes are can be denatured based off of temperature and PH. For example, if the temperature is too high it can put stress oh hydrogen bonds and cause them to break.
In response to question 2, there is no clear corruptions that can arise from enzyme catalysis, the only thing that can stop a reaction from working is when the enzyme has lost it's shape and has begun denaturization.
1. What happens after the substrate is turned into the product? 2. What enzymes are the most prevalent in the human body? 3. Can a substrate reaction go wrong?
In response to your first question, after the substrate is turned into the product, the product disperses into the cell to carry out its function in the cell. Then the enzyme will go back to its original shape to wait for the next substrate.
Question 2- I would probably say Helicase and DNA polymerase are the most relevant since they are directly connected to the function and nature of our DNA. Without DNA, we wouldn't have bodies so I would say it's pretty important!!
Question 3- This is just a guess because I couldn't find anything about this question on the internet. I would think that yes, it's possible a substrate reaction can go wrong. Perhaps one example of a complication could be an enzyme losing its ability to function properly. In situations like the digestive system this could become catastrophic since we need enzymes for a lot of the digestive process. Again, I'm not sure because I didn't find a resource to back this up, but I would love to learn more about this!
1) How can external factors affect the structure of an enzyme? 2) Why/how are the substrates and enzymes drawn to one another? 3) How do Proteases work?
To answer your third question, protease breaks down protein in food into amino acid, as well as plays a role in blood clotting, cell division, recycling proteins, and immune support.
For more information about protease go here: https://enzyscience.com/blogs/news/what-are-protease
To answer your 1st question, on slide 8 of the 2.5 Enzymes PP, it states that the structure of an enzyme can and will denature because of extremes of heat/temp and because of extremes of pH levels
To answer your second question, substrates and enzymes are attracted to each other due to a physical or chemical force. Bonds between substrate and enzyme may include electrostatic or hydrophobic.
More information about the attractions between substrate and enzyme can be found here: https://www.britannica.com/science/protein/The-role-of-the-active-site
1. What about an enzyme causes it to create the product from a substrate? 2. How does someone attach an enzyme to something to immobilize it? 3. What are other examples of immobilized enzymes?
To answer your first question, enzymes catalyze certain chemical reactions that naturally converts substrate molecules into products https://courses.lumenlearning.com/boundless-biology/chapter/enzymes/#:~:text=Enzyme%20Active%20Site%20and%20Substrate,converting%20substrate%20molecules%20to%20products.
To answer your third question, some examples of immobilized enzymes are: penicillin G acylase, invertase, lipases, proteases,and more.
Here is a link to a article/website with more details about immobilized enzymes: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3787205/#:~:text=Several%20hundred%20enzymes%20have%20been,in%20various%20large%2Dscale%20processes.
Your second question - I found a couple of resources! Essentially, the enzyme is attached through "weak attractive forces." Some of these we have learned about, such as hydrogen bonding, Van der walls forces, and ionic/covalent binding. There are many factors involved that can impact the process, including pH and temperature. Video resource: https://www.youtube.com/watch?v=sL_iEOuvK80 Article resource (look for the subsection titled "2.23.2.1 Adsorption"): https://www.sciencedirect.com/topics/agricultural-and-biological-sciences/immobilized-enzymes#:~:text=The%20simplest%20way%20to%20immobilize,per%20enzyme%20molecule%20%5B8%5D.
1. Could an active area be forcibly changed via pH and temperature to fit a different substrate? 2. How many active areas are there and how many can fit into one space at a time 3. What is the lifespan of an enzyme or how long can an active area change substrates before denaturing?
For your third question, I had to take a while to try to find an answer. I didn't find many resources that had the type of answer you were looking for. However, I found that it depends on their amino acid sequence. I found this at https://www.quora.com/Do-enzymes-have-a-lifespan-where-after-they-degrade
To answer your second question, each enzyme has two active areas, both fitting one specific type of substrate. These are specific to the jobs these enzymes were created to perform, meaning that many enzymes and their active sites will vary. I hope this helped!
1. What's the most abundant enzyme 2. Do enzymes ever get replaced after creation within a cell? 3. Are there any enzymes that can cause injury to an organism?
Your 3rd question - While researching this, I found an interesting Washington Post article about digestive enzyme supplements. Some conditions require patients to take medications with enzymes in them, to make up for a lack thereof in the body. For example, alpha-galactosidase makes foods such as beans easier to digest, and lactase pills provide the enzyme necessary for lactose-intolerant patients to consume dairy. There are, however, over-the-counter medications with a variety of enzymes that people are taking without medical advice. Many of these enzymes come from plants or animals, and can interact poorly with other medications. These combinations can cause more digestive problems and introduce more impurities to the body. Article: https://www.washingtonpost.com/lifestyle/wellness/why-you-should-be-wary-of-some-digestive-enzyme-supplements/2019/02/18/4531ef3e-2fdc-11e9-8ad3-9a5b113ecd3c_story.html
To answer your first question, the most abundant enzyme is RuBisCO. https://www.iomcworld.org/medical-journals/abundant-protein-50938.html#:~:text=And%2C%20the%20most%20abundant%20protein,first%20step%20in%20carbon%20fixation.
To answer your 2nd question, since enzymes are protein catalysts that biochemical reactions they are able to adapt to different cells and changes. Enzymes have the ability to bind with substrates molecules and there are various enzyme powered pathways. source: https://www.nature.com/scitable/topicpage/cell-metabolism-14026182/
To answer your second question, yes, enzymes can be replaced! Eukaryotic cells create new enzymes within it's endoplasmic reticulum, using instructions from the cell's RNA sequence as a guide. Enzymes can't truly die, which mean's they are constantly working until they are denatured or dissolved. When this happens, however, the ER is ready to make some new enzymes to keep your cells running smoothly. I hope this helped!
1) Could somebody give an example of when using immobilized enzymes would be beneficial? I'm a little bit confused on this concept. 2) I was confused on one of the DBQ's about digesting jello cubes. What is the correlation between pH and the loss in mass in a substrate as it is digested by an enzyme? 3) How exactly does the shape-changing of an enzyme occur according to the induced-fit model?
After researching your first question, I found that "The use of the immobilized enzyme has provided significant advantages over a chemical process, such as the possibility to use equimolar concentration of substrates, obtain an enantiomeric excess > 99%, use relatively low temperatures (< 60 °C) in organic solvent, obtain a single enantiomer instead of the racemate as in the chemical process and use a column configuration that allows dramatic increases in productivity. This process would not have been possible without the use of an immobilized enzyme, since it runs in organic solvent [1].", this quote was found from https://www.sciencedirect.com/science/article/pii/S2468823119304560#:~:text=The%20use%20of%20the%20immobilized,of%20the%20racemate%20as%20in
To help answer your first questions, immobilized enzymes is primarily used in industries for catalyzing specific reactions. Other benefits include reusing of enzymes (which saves money), resistance to denaturalization, and keeps products from being contaminated with enzymes. source: IB study guide textbook :)
I hope this answers your third question. Induced Fit: According to the induced fit model, both enzyme and substrate undergo dynamic conformational changes upon binding. The enzyme contorts the substrate into its transition state, thereby increasing the rate of the reaction.
1. What would happen to the body if it did not conduct enough metabolic reactions? 2. Because some people who are lactose intolerant have to take lactase pills, what exactly do those pills do? 3. What happens to the enzymes that denaturize? Do they get absorbed, broken up, etc.?
Your 2nd question - People who are lactose intolerant don't have enough lactase in their body to effectively break down lactose in the small intestine in a way that the body can use. This is because their bodies stopped producing these enzymes after childhood. The lack of the enzyme lactase causes the lactose from dairy to remain undigested in the system, which causes a range of uncomfortable GI symptoms. Lactase pills contain this enzyme and should be taken prior to eating in order to break down the lactose that their bodies naturally can't.
to help answer your 1st question, if the body did not conduct enough metabolic reactions it would make difficult to sustain bodily functions and maintain body structure. As an organism, food is ingested to be used for energy and without metabolic reactions present the energy can not be converted into fuel for movement. Hope this helped! source: https://courses.lumenlearning.com/nemcc-ap/chapter/functions-of-human-life/
To answer your third question, when enzymes denaturize, their shapes get warped, but specifically the shape of the active site, which is where the substrate is received. If the enzyme can no longer receive substrate, it cannot function how its supposed to. However, in many cases denaturation can be reversed (during a process called renaturation), so it's often not completely destroyed. I hope this helped!
1. How does the renaturation process work? 2. How far gone and denaturized does an enzyme have to be for the renaturation process to not work? 3. Can substrates change to fit different active sites, and vice versa?
To answer your last question, The induced fit model states an substrate binds to an active site and both change shape slightly, creating an ideal fit for catalysis. When an enzyme binds its substrate it forms an enzyme-substrate complex.
3- from what I can find no substrates don't change shape at all. It is a specific material and the current model used in the concept is induced- fit. This means the enzyme adjusts its shape slightly for the active site to better fit the substrate after collision.
1- I had a hard time finding information on this. In fact, I didn't even know renaturation was possible. I don't believe there is much information about it. It is uncommon for proteins to be able to return to its proper shape. I believe it is sometimes possible when the cause of denaturation is removed. I think it mostly happens in labs. When they experiment to identify it's structure after finishing it can some time revert to its shape. https://www.biologyonline.com/dictionary/renaturation
1. what are some important enzymes reactions in the body? 2. when were enzymes discovered and how? 3. how have enzymes changed the scientific field in modern time?
To answer your first question, heres three specific enzymes and their jobs/ reaction: Lipases – a group of enzymes that help digest fats in the gut. Amylase – helps change starches into sugars. Amylase is found in saliva. Maltase – also found in saliva; breaks the sugar maltose into glucose. Maltose is found in foods such as potatoes, pasta, and beer.
Heres the link to where I found this information: https://www.medicalnewstoday.com/articles/319704#examples
The first enzyme was discovered in 1833 by French chemist Anselme Payen. I had a difficult time finding a lot more information than this. I couldn't find much on how they discovered it.I believe it was found in the process of malting for alcohol. I don't have a lot of knowledge about the subject. https://jamanetwork.com/journals/jama/article-abstract/246007
1. I don't understand why pH can denature an enzyme. Why does a higher concentration of hydrogen ions change the shape? 2. How was the induced fit model discovered or considered in place of the lock and key model? 3. One part says the substrate may collide at any angle but it also says it must be correctly aligned. Did I interpret this wrong (top of 98)?
1. What does a calorimeter measure?
ReplyDelete2.What is the test for reducing sugars and how does it work?
3. What type of enzymes break down proteins?
To answer your first question, a calorimeter measures the levels of heat involved in chemical reactions
DeleteTo answer your third question, proteases breakdown proteins into more simple amino acids for use in different proteins.
DeleteCitation
https://www.healthline.com/health/protein-digestion#:~:text=Once%20a%20protein%20source%20reaches,move%20into%20your%20small%20intestine.
In regards of your first question, the test for reducing sugars would be the Benedict test. The Benedict's solution will start off an aqua-blue and when heated will turn to yellow or orange. If a higher amount of reducing sugars is present, the color of the mixture will be more orange. I hope this helps...I got my info from this page:
Deletehttps://www.nku.edu/~whitsonma/Bio150LSite/Lab%203%20Organic/Bio150LRevMolec.html#:~:text=In%20lab%2C%20we%20used%20Benedict's,one%20particular%20reducing%20sugar%3A%20glucose.&text=Benedict's%20reagent%20starts%20out%20aqua,the%20concentration%20of%20reducing%20sugar.
1. How does a decrease in temperature affect enzymes and enzyme-bonding?
ReplyDelete2. Can purposeful enzymatic reactions occur, can an enzyme come with the specific task of binding to specific substrates?
3. Can enzymes be renaturized?
To answer your first question, cooler temperatures lower the kinetic energy in the molecules leading to them moving less and thus bumping into one another less. This lessening in kinetic energy also can slow down the reactions.
DeleteFor your second question the majority of enzymes are made to interact with a very specific substrate. This is called enzyme-substrate specificity. (Textbook)
DeleteFor your third question, I found an article talking all about how they used a specific gel to retature enzymes but it went right over my head so I hope this information can answer your question. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4585781/
DeleteFor your first question, I found that lowering the temperature slows the motions of the molecules and atoms which causes the flexibility to be lost. Because each enzyme has a specific optimal temperature range, decreasing the temperature slows enzyme activity.
DeleteLink:
https://education.seattlepi.com/enzyme-activity-affected-lower-temperatures-5527.html
Based on the information I read to answer your third question, I do not belive that enzymes can be naturally renatured but there are some solutions that can result in the partial renaturalization of enzymes. In general they can only be renatured if they were very gently denatured. https://www.britannica.com/science/renaturation
DeleteWhat would be considered the single most essential enzyme?
ReplyDeleteAre there any enzymes with multiple binding sites?/Enzymes who can have more than 1 substrate bind to them?
Are there enzymes where once denatured will continue to be functional?
To answer your first question, Rubisco is the most prevalent and important enzyme.
DeleteTo answer your third question, based on what I found, enzymes will no longer function after denaturation, and I have not found any exceptions, if there are exceptions they are exceptionally rare.
DeleteIn response to your second question, there are enzymes with multiple bonding sites that are called multi-site enzymes. They serve many different roles. One example is creating a queue of substrates to speed up the enzymatic reactions.
Deletehttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3996589/#:~:text=Multi%2Dsite%20enzymes%2C%20defined%20as,ClpXP%20a%20well%2Dstudied%20example.
Answering your first question, I found that Rubisco is the most abundant and important enzyme. It is the most abundant as it is found in every photosynthetic organism. It is the most important because it is in the first step of photosynthesis. Hope this helped :)
DeleteLink: https://www.howplantswork.com/2010/01/19/a-step-toward-fixing-the-most-important-enzyme-on-earth/#:~:text=The%20world's%20most%20abundant%20and,sized%20trees%20in%20the%20tropics.
1) Why is Rubisco the most important enzyme?
ReplyDelete2) How are enzymes used in other fields/ are they used for business?
3) How does the electron concentration in a solution affect the ph level?
To answer your first question, Rubisco is the most important enzyme because it is the catalyst for the first step in photosynthesis in all photosynthetic organisms.
DeleteFor your second question, enzymes have many commercial purposes, which are usually fulfilled by immobilized enzymes. These industries include food, agriculture, cosmetics and pharmaceuticals
DeleteIn regards of your third question, the pH of a solution is simply determined by the hydronium levels. If the hydronium concentration increases then the pH will in turn become more acidic. "The partial charge is caused by the fact that oxygen is more electronegative than hydrogen. This means that in the bond between hydrogen and oxygen, oxygen "pulls" harder on the shared electrons thus causing a partial negative charge on the molecule and causing it to be attracted to the positive charge of H+ to form hydronium" Because the hydronium is bent it causes the molecule to have a dipole moment and results in a partial charge. I hope that helps...
Deletehttps://chem.libretexts.org/Bookshelves/Physical_and_Theoretical_Chemistry_Textbook_Maps/Supplemental_Modules_(Physical_and_Theoretical_Chemistry)/Acids_and_Bases/Acids_and_Bases_in_Aqueous_Solutions/The_Hydronium_Ion#:~:text=The%20hydronium%20ion%20has%20a,the%20atoms%20is%20113%20degrees.
To answer your first question, Rubisco is the most important enzyme because it is in the first step of photosynthesis which converts CO2 to into sugars.
DeleteLink: https://www.howplantswork.com/2010/01/19/a-step-toward-fixing-the-most-important-enzyme-on-earth/#:~:text=The%20world's%20most%20abundant%20and%20most%20important%20enzyme%20is%20RuBisCo.&text=It's%20also%20the%20most%20important,a.k.a.%2C%20the%20Calvin%20cycle).
This comment has been removed by the author.
ReplyDelete1) Does the polarity of an enzyme affect the changes it will have towards a change in pH?
ReplyDelete2) What happens if the substrates reaction goes wrong? Can it?
3) Can someone dumb down substrate reactions? I'm having trouble wrapping my head around the whole thing
For your third question: (Substrate turns into product)
DeleteExtra simple:
1. Substrate attaches to enzyme
2. Enzyme makes substrate change shape
3. Substrate detaches and is now a product
4. Process restarts
More detailed but still simple:
1. Substrate attached to enzyme (they naturally fit together/are attracted to each other)
2. Attachment triggers enzyme to change shape, forcing the substrate to change shape.
3. Bond is now unstable between enzyme and substrate, substrate detaches and is now a product
4. Enzyme goes back to original shape
5. Process restarts
For your second question, I am not sure if substrates reactions can go wrong, if the enzyme and substrate do fit well together then I don’t belive that anything naturally could go wrong with the reaction. If something does happen like a dramatic change in tempurature or ph, then the enzyme could lose it’s ability to bind to a substrate. This could result in the denaturation of the enzyme.
DeleteIn response to your first question, while it does not have an effect on the enzyme specifically, polar molecules have much weaker bonds, meaning that they break apart much easier, which would likely cause those bonds to break quickly in acidic pH levels.
DeleteThis comment has been removed by the author.
ReplyDelete1. How does the body or cell deal with denatured enzymes?
ReplyDelete2. How quickly do enzymes normally break down substrates? Why?
3. Can molecules become stuck in the active site of enzymes and block it? Or is it just properly placed substrates that block the active site?
To answer your first question, in general I found that after an enzyme is denatured the amino acids/ monomers/ components will be recycled or if this is not possible they will become waste and excreted by the urea cycle. https://www.sciencelearn.org.nz/images/2264-denatured-enzyme
DeleteTo answer your third question, it is possible for molecules to block the active site of an enzyme. These molecules are called competitive inhibitors. They are shaped very similarly to the enzyme's substrate which allows them to block the active site.
DeleteFor more information about inhibitors go here:
https://sciencing.com/blocks-enzyme-activity-binding-active-enzyme-11545.html
To answer question two, enzyme speed is different for each type of enzyme, the fastest of which being carbonic ahydrase, being able to hydrate 1000000 CO2 molecules in one second. https://www.ncbi.nlm.nih.gov/books/NBK22380/#:~:text=In%20fact%2C%20carbonic%20anhydrase%20is,fast%20as%20the%20uncatalyzed%20one.&text=An%20enzyme%20usually%20catalyzes%20a,set%20of%20closely%20related%20reactions.
Delete1- How, more specifically, are enzymes denatured?
ReplyDelete2- In what ways can the enzyme catalyzing the substrate to create a product go wrong?
3- Can denatured enzymes be naturally renatured?
In response to your third question, it is highly unlikely that an enzyme can be renatured naturally. Some enzymes can be partially renatured if placed in the correct solution, however, more often then not it can't be done, even with human help.
Deletehttps://link.springer.com/chapter/10.1007%2F978-3-642-69148-5_12
Question 1- Enzymes are can be denatured based off of temperature and PH. For example, if the temperature is too high it can put stress oh hydrogen bonds and cause them to break.
DeleteIn response to question 2, there is no clear corruptions that can arise from enzyme catalysis, the only thing that can stop a reaction from working is when the enzyme has lost it's shape and has begun denaturization.
Delete1. What happens after the substrate is turned into the product?
ReplyDelete2. What enzymes are the most prevalent in the human body?
3. Can a substrate reaction go wrong?
In response to your first question, after the substrate is turned into the product, the product disperses into the cell to carry out its function in the cell. Then the enzyme will go back to its original shape to wait for the next substrate.
Deletehttps://www.khanacademy.org/science/ap-biology/cellular-energetics/enzyme-structure-and-catalysis/a/enzymes-and-the-active-site
Question 2- I would probably say Helicase and DNA polymerase are the most relevant since they are directly connected to the function and nature of our DNA. Without DNA, we wouldn't have bodies so I would say it's pretty important!!
DeleteQuestion 3- This is just a guess because I couldn't find anything about this question on the internet. I would think that yes, it's possible a substrate reaction can go wrong. Perhaps one example of a complication could be an enzyme losing its ability to function properly. In situations like the digestive system this could become catastrophic since we need enzymes for a lot of the digestive process. Again, I'm not sure because I didn't find a resource to back this up, but I would love to learn more about this!
Delete1) How can external factors affect the structure of an enzyme?
ReplyDelete2) Why/how are the substrates and enzymes drawn to one another?
3) How do Proteases work?
To answer your third question, protease breaks down protein in food into amino acid, as well as plays a role in blood clotting, cell division, recycling proteins, and immune support.
DeleteFor more information about protease go here:
https://enzyscience.com/blogs/news/what-are-protease
To answer your 1st question, on slide 8 of the 2.5 Enzymes PP, it states that the structure of an enzyme can and will denature because of extremes of heat/temp and because of extremes of pH levels
DeleteTo answer your second question, substrates and enzymes are attracted to each other due to a physical or chemical force. Bonds between substrate and enzyme may include electrostatic or hydrophobic.
DeleteMore information about the attractions between substrate and enzyme can be found here:
https://www.britannica.com/science/protein/The-role-of-the-active-site
1. What about an enzyme causes it to create the product from a substrate?
ReplyDelete2. How does someone attach an enzyme to something to immobilize it?
3. What are other examples of immobilized enzymes?
To answer your first question, enzymes catalyze certain chemical reactions that naturally converts substrate molecules into products
Deletehttps://courses.lumenlearning.com/boundless-biology/chapter/enzymes/#:~:text=Enzyme%20Active%20Site%20and%20Substrate,converting%20substrate%20molecules%20to%20products.
To answer your third question, some examples of immobilized enzymes are: penicillin G acylase, invertase, lipases, proteases,and more.
DeleteHere is a link to a article/website with more details about immobilized enzymes: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3787205/#:~:text=Several%20hundred%20enzymes%20have%20been,in%20various%20large%2Dscale%20processes.
Your second question - I found a couple of resources! Essentially, the enzyme is attached through "weak attractive forces." Some of these we have learned about, such as hydrogen bonding, Van der walls forces, and ionic/covalent binding. There are many factors involved that can impact the process, including pH and temperature.
DeleteVideo resource: https://www.youtube.com/watch?v=sL_iEOuvK80
Article resource (look for the subsection titled "2.23.2.1 Adsorption"): https://www.sciencedirect.com/topics/agricultural-and-biological-sciences/immobilized-enzymes#:~:text=The%20simplest%20way%20to%20immobilize,per%20enzyme%20molecule%20%5B8%5D.
1. Could an active area be forcibly changed via pH and temperature to fit a different substrate?
ReplyDelete2. How many active areas are there and how many can fit into one space at a time
3. What is the lifespan of an enzyme or how long can an active area change substrates before denaturing?
For your third question, I had to take a while to try to find an answer. I didn't find many resources that had the type of answer you were looking for. However, I found that it depends on their amino acid sequence. I found this at https://www.quora.com/Do-enzymes-have-a-lifespan-where-after-they-degrade
DeleteTo answer your second question, each enzyme has two active areas, both fitting one specific type of substrate. These are specific to the jobs these enzymes were created to perform, meaning that many enzymes and their active sites will vary. I hope this helped!
DeleteSources :)
https://flexbooks.ck12.org/cbook/ck-12-biology-flexbook-2.0/section/1.18/primary/lesson/enzyme-function-bio
https://www.britannica.com/science/active-site
https://en.wikipedia.org/wiki/Active_site#:~:text=Usually%2C%20an%20enzyme%20molecule%20has,one%20specific%20type%20of%20substrate.
1. What's the most abundant enzyme
ReplyDelete2. Do enzymes ever get replaced after creation within a cell?
3. Are there any enzymes that can cause injury to an organism?
Your 3rd question - While researching this, I found an interesting Washington Post article about digestive enzyme supplements. Some conditions require patients to take medications with enzymes in them, to make up for a lack thereof in the body. For example, alpha-galactosidase makes foods such as beans easier to digest, and lactase pills provide the enzyme necessary for lactose-intolerant patients to consume dairy. There are, however, over-the-counter medications with a variety of enzymes that people are taking without medical advice. Many of these enzymes come from plants or animals, and can interact poorly with other medications. These combinations can cause more digestive problems and introduce more impurities to the body.
DeleteArticle: https://www.washingtonpost.com/lifestyle/wellness/why-you-should-be-wary-of-some-digestive-enzyme-supplements/2019/02/18/4531ef3e-2fdc-11e9-8ad3-9a5b113ecd3c_story.html
To answer your first question, the most abundant enzyme is RuBisCO. https://www.iomcworld.org/medical-journals/abundant-protein-50938.html#:~:text=And%2C%20the%20most%20abundant%20protein,first%20step%20in%20carbon%20fixation.
DeleteTo answer your 2nd question, since enzymes are protein catalysts that biochemical reactions they are able to adapt to different cells and changes. Enzymes have the ability to bind with substrates molecules and there are various enzyme powered pathways. source: https://www.nature.com/scitable/topicpage/cell-metabolism-14026182/
DeleteTo answer your second question, yes, enzymes can be replaced! Eukaryotic cells create new enzymes within it's endoplasmic reticulum, using instructions from the cell's RNA sequence as a guide. Enzymes can't truly die, which mean's they are constantly working until they are denatured or dissolved. When this happens, however, the ER is ready to make some new enzymes to keep your cells running smoothly. I hope this helped!
DeleteSources :)
https://quatr.us/biology/enzymes-cell-biology.htm
https://education.seattlepi.com/mean-enzyme-denatured-5339.html
1) Could somebody give an example of when using immobilized enzymes would be beneficial? I'm a little bit confused on this concept.
ReplyDelete2) I was confused on one of the DBQ's about digesting jello cubes. What is the correlation between pH and the loss in mass in a substrate as it is digested by an enzyme?
3) How exactly does the shape-changing of an enzyme occur according to the induced-fit model?
After researching your first question, I found that "The use of the immobilized enzyme has provided significant advantages over a chemical process, such as the possibility to use equimolar concentration of substrates, obtain an enantiomeric excess > 99%, use relatively low temperatures (< 60 °C) in organic solvent, obtain a single enantiomer instead of the racemate as in the chemical process and use a column configuration that allows dramatic increases in productivity. This process would not have been possible without the use of an immobilized enzyme, since it runs in organic solvent [1].", this quote was found from https://www.sciencedirect.com/science/article/pii/S2468823119304560#:~:text=The%20use%20of%20the%20immobilized,of%20the%20racemate%20as%20in
DeleteTo help answer your first questions, immobilized enzymes is primarily used in industries for catalyzing specific reactions. Other benefits include reusing of enzymes (which saves money), resistance to denaturalization, and keeps products from being contaminated with enzymes. source:
DeleteIB study guide textbook :)
I hope this answers your third question. Induced Fit: According to the induced fit model, both enzyme and substrate undergo dynamic conformational changes upon binding. The enzyme contorts the substrate into its transition state, thereby increasing the rate of the reaction.
Delete1. What would happen to the body if it did not conduct enough metabolic reactions?
ReplyDelete2. Because some people who are lactose intolerant have to take lactase pills, what exactly do those pills do?
3. What happens to the enzymes that denaturize? Do they get absorbed, broken up, etc.?
Your 2nd question - People who are lactose intolerant don't have enough lactase in their body to effectively break down lactose in the small intestine in a way that the body can use. This is because their bodies stopped producing these enzymes after childhood. The lack of the enzyme lactase causes the lactose from dairy to remain undigested in the system, which causes a range of uncomfortable GI symptoms. Lactase pills contain this enzyme and should be taken prior to eating in order to break down the lactose that their bodies naturally can't.
Deleteto help answer your 1st question, if the body did not conduct enough metabolic reactions it would make difficult to sustain bodily functions and maintain body structure. As an organism, food is ingested to be used for energy and without metabolic reactions present the energy can not be converted into fuel for movement. Hope this helped!
Deletesource: https://courses.lumenlearning.com/nemcc-ap/chapter/functions-of-human-life/
To answer your third question, when enzymes denaturize, their shapes get warped, but specifically the shape of the active site, which is where the substrate is received. If the enzyme can no longer receive substrate, it cannot function how its supposed to. However, in many cases denaturation can be reversed (during a process called renaturation), so it's often not completely destroyed. I hope this helped!
DeleteHere's a source or two :)
https://www.khanacademy.org/science/high-school-biology/hs-energy-and-transport/hs-enzymes/a/hs-enzymes-review
https://education.seattlepi.com/mean-enzyme-denatured-5339.html#:~:text=Enzymes%20work%20consistently%20until%20they,cause%20enzymes%20to%20become%20denatured.&text=Novozymes%3A%20What%20Are%20Enzymes%3F
1. How does the renaturation process work?
ReplyDelete2. How far gone and denaturized does an enzyme have to be for the renaturation process to not work?
3. Can substrates change to fit different active sites, and vice versa?
To answer your last question, The induced fit model states an substrate binds to an active site and both change shape slightly, creating an ideal fit for catalysis. When an enzyme binds its substrate it forms an enzyme-substrate complex.
Delete3- from what I can find no substrates don't change shape at all. It is a specific material and the current model used in the concept is induced- fit. This means the enzyme adjusts its shape slightly for the active site to better fit the substrate after collision.
Delete1- I had a hard time finding information on this. In fact, I didn't even know renaturation was possible. I don't believe there is much information about it. It is uncommon for proteins to be able to return to its proper shape. I believe it is sometimes possible when the cause of denaturation is removed. I think it mostly happens in labs. When they experiment to identify it's structure after finishing it can some time revert to its shape.
Deletehttps://www.biologyonline.com/dictionary/renaturation
1. what are some important enzymes reactions in the body?
ReplyDelete2. when were enzymes discovered and how?
3. how have enzymes changed the scientific field in modern time?
To answer your first question, heres three specific enzymes and their jobs/ reaction: Lipases – a group of enzymes that help digest fats in the gut. Amylase – helps change starches into sugars. Amylase is found in saliva. Maltase – also found in saliva; breaks the sugar maltose into glucose. Maltose is found in foods such as potatoes, pasta, and beer.
DeleteHeres the link to where I found this information: https://www.medicalnewstoday.com/articles/319704#examples
The first enzyme was discovered in 1833 by French chemist Anselme Payen. I had a difficult time finding a lot more information than this. I couldn't find much on how they discovered it.I believe it was found in the process of malting for alcohol. I don't have a lot of knowledge about the subject.
Deletehttps://jamanetwork.com/journals/jama/article-abstract/246007
my response was for question 2
Delete1. I don't understand why pH can denature an enzyme. Why does a higher concentration of hydrogen ions change the shape?
ReplyDelete2. How was the induced fit model discovered or considered in place of the lock and key model?
3. One part says the substrate may collide at any angle but it also says it must be correctly aligned. Did I interpret this wrong (top of 98)?