which of the following describes an enzyme ALLOSTERIC site?
Q: How does the optimum pH and optimum temperature can affect the enzyme function? Explain shortly with…
A: Temperature: Raising temperature generally speeds up a reaction, and lowering temperature slows down…
Q: Each of the amino acid residues in the catalytic triad is part of what polypeptide chain?
A: The enzymes carry out the catalysis of various reactions in metabolism. The catalytic triad helps…
Q: In covalent catalysis, either nucleophilic catalysis or electrophilic catalysis occurs. Do you agree…
A: Enzymes are known as biological catalysts, which perform an essential role in various biochemical…
Q: Indicate whether each of the following phrases descrubes a simple or a conjugated enzyme. An enzyme…
A: Introduction: An enzyme whose complete breakdown yields only amino acids is called a simple enzyme…
Q: What happens to the activity of an allosteric enzyme if an allosteric inhibitor binds the alloster…
A: Allosteric mode of inhibition is also called non-competitive inhibition where an inhibitor…
Q: When calculating the order of a reaction, the enzyme doesnot appear in the equation. Explain.
A: Enzyme are the biocatalysts which increase the rate of biochemical reaction by decreasing the…
Q: The protein portion of a conjugated enzyme is called a(n).
A: Enzymes are proteins that facilitate in the speeding up of our bodies' metabolism, or chemical…
Q: What happens to the functionality of a denatured enzyme? How can that resul be explained with the…
A: Enzymes are the biological catalysts that increase the rate of a biochemical reaction. They are…
Q: Why is an inhibitor that mimics the transition state more effective at enzyme inhibition than an…
A: Introduction: Enzymes can be inhibited by molecules that mimic the substrate or enzyme-substrate…
Q: Why do we say "an enzyme is reusable"?
A: Enzymes are catalyst molecules that help to increase the rate or speed up the chemical reactions…
Q: enzyme inhibition.
A:
Q: Discuss the behavior of enzymes as described by the Michaelis-Menten Equation
A: Enzymes are proteins with the capability to accelerate the rate of a biochemical reactions. Enzymes…
Q: How does the optimum pH and optimum temperature can affect the enzyme function? Explain with…
A: Enzymes are biocatalysts that can increase the rate of biochemical reaction without themselves being…
Q: What is the advantage for an organism to have isozymic forms of an enzyme?
A: Introduction: Isozymes or isoenzymes are different enzymes catalyzing the same reaction. These…
Q: To which class of enzymes does each of the following belong?
A: Enzyme classification in needed to name the enzymes. According to the Enzyme Commission there are…
Q: What is regulate enzyme stability?
A: Enzymes are the biological catalysts that have the ability to increase the rate of metabolic…
Q: What proof do you have that an enzyme–substrate complex exists?
A: Introduction to the concept Enzymes are biocatalysts that are also proteins. They are made by live…
Q: Why are allosteric enzymes crucial for the control of metabolism?
A: Allosteric enzymes are considered as an enzyme, which changes its structure upon binding to the…
Q: Which of the following statements describes a dimeric allosteric enzyme following the concerted…
A: Introduction: Enzymes are proteins that serves as biological catalysts. They increase the pace of…
Q: Within an enzyme active site, how does the aspartate carboxyl group activate the histidine nitrogen…
A: An enzyme is a special class of proteins that catalyze biochemical reactions. Proteolytic enzymes…
Q: What is the explanation for enzyme specificity?
A: All biological chemical reaction reactions in living organisms are controlled by enzymes. If enzymes…
Q: If an enzyme has a maximal activity of pH 6.8 and your reaction buffer is a pH 5.8, what do you need…
A: Every Enzyme has an optimum pH range for its maximuim acitivity. change in the pH will affect the…
Q: Why would enzymes be found as isozymes?
A: An enzyme is a biocatalyst that helps to increase the rate of a biochemical reaction. The site to…
Q: Which of the following statements describes an enzyme ALLOSTERIC site? O It is where an inhibitor…
A: Allosteric site is the site that allows enzyme activity to be activated or inhibited by molecules.
Q: what are the covalent modification that regulates enzyme kinetics ?
A: Covalent modification: The activity of the enzymes may be increased or decreased by covalent…
Q: Which one is the most likely to be a catalytic triad of an enzyme that follows general acid base…
A: Enzymes are specialized proteins that catalyze all the biochemical reactions. They are divided based…
Q: Each type of enzyme contains a unique, intricately shaped binding surface called a(n) _____________.
A: Enzymes are proteins act as a biocatalyst which increases the rate of a chemical reaction. All…
Q: nhibitor always binds to the allosteric site of an enzyme
A: By adhering to the active site, an inhibitor can bind to an enzyme and prevent the substrate from…
Q: In this process of enzyme inhibition, a molecule binds to a site on the enzyme that is NOT the…
A: An enzyme inhibitor are molecules that interrupt or decreases the rate of an enzyme catalyzed…
Q: The enzyme that catalyzes the following reaction belongs to which class?
A: Enzymes are biocatalysts that accelerate chemical reactions. The molecules upon which enzymes act…
Q: What happens when an enzyme is denatured? Can a denatured enzyme be "re-natured"? Explain.
A: Enzymes are proteinaceous structure found in the cells. They act as a biological catalyst. Enzymes…
Q: What is the definition of an allosteric site of an enzyme? any site other than the active site the…
A: An enzyme is a biological catalysts that increases or catalyzes the reactions that occur naturally…
Q: What type of bonds in the tertiary structure of the enzyme break at high temperatures? Which ones…
A: Enzymes are proteins that act as biocatalysts. They accelerate chemical reactions. The molecules…
Q: Why are such allosteric enzymes composed of more than one catalytic subunit?
A: Many enzymes are composed of multiple subunits.
Q: What is cooperativity in terms of allosteric enzymes?
A: Allosteric Enzymes means their work is to fasten the rate of reaction inside the body without…
Q: Each type of enzyme contains a unique, intricately shapedbinding surface called an…
A: Enzymes are essentially proteins that act as a catalyst for biological reactions. They act by…
Q: How do an activator and an inhibitor have differenteffects on an allosterically regulated enzyme?
A: ALLOSTERIC REGULATION:- The site beside the active site certain enzymes possess site for attachment…
Q: What is meant by core enzyme ?
A: Enzyme: are made up of proteins and involved biological reaction which occurs in the living body.…
Q: Why is the shape of the active site on an enzyme important to the enzyme's function?
A: Amino acids builds together to forms an Enzyme, in a linear chain. These amino acid are…
Q: Why do allosteric enzymes have two types of binding sites?
A: Allosteric enzyme : It are enzymes that change their conformational ensemble upon binding of an…
Q: Define enzyme denaturation in terms of protein structure. What environmental factors can denature…
A: Proteins are macromolecules that consists of one or more long chains of amino acid (aa) residues.…
Q: What is a potential disadvantage of having many catalytic sites together on one very long…
A: A catalytic site is the small, high conserved constellation of residues within the active site that…
Q: What classification of enzyme is catalase? Give the Enzyme Commission (E.C.) number of catalase.
A: Enzymes are biocatalysts that increase the rate of the chemical reaction without undergoing any…
Q: The site on the enzyme surface where the reactant fits is referred to as the __________
A: An enzyme It can be defined as a substance that acts as a catalyst in the living organisms. It…
Q: what is enzyme inhibition?
A: Enzymes are the protein molecules which are of biological origins or sometimes may be produced…
Q: While every level of a protein's structure is important to the function of that protein, which level…
A: Proteins are biological heteropolymers, which are composed of amino acids. Series of amino acids are…
which of the following describes an enzyme ALLOSTERIC site?
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- An inhibitor was added to an enzyme and the expected rate of the reaction was not detected and the substrate was not utilized at all. This inhibitor is (choose one answer only): Is un-competitive, meaning the inhibitor binds to a site near the active site. Is competitive, meaning the inhibitor binds directly to the same active site as the subtrate. Is non-competitive, meaning the inhibitor binds to site other than the active site as the subtrate. Is irreversible, meaning the inhibitor binds covalently to the enzyme keeping the enzyme inactive permanently.Which of the following is characteristic of competitive inhibitors? the inhibitor could bind to the active site or to an allosteric site on the enzyme. the enzyme will mistake the inhibitor for its substrate, so that the inhibitor will end up covalently bound to the enzyme. the inhibitor can bind only AFTER the substrate has bound (i.e. it binds only to the ES complex). the inhibitor can bind reversibly at the substrate-binding site (the active site). the inhibitor will lower the characteristic Vmax of the enzyme.Which of the following statements regarding enzymes and transition states is true? stabilization of the transition state must be less than stabilization of ES for catalysis to occur binding of substrate to an enzyme often causes strain, thus promoting transition state formation the transition state conformation of an enzyme catalyzed reaction is identical to the conformation seen in the uncatalyzed transition state formation of the transition state always assures that the reaction will proceed to product none of the above are true
- Which of the following are characteristics of catabolic metabolic pathways? (Choose all correct answers). Overall oxidation of initial substrates so redox reactions involve use of NAD+ as oxidizing agent, converted to NADH. Large initial substrates are broken down to smaller final products. Overall reduction of intial substrates so redox reactions involve use of NADPH as reducing agent, converted to NADP+. The pathways are overall exergonic (negative delta G). Net production of ATP as a result of the pathway. Essentially irreversibleClassify the inhibitor characteristics according to one of three types of inhibition: reversible competitive, reversible noncompetitive, or irreversible. Reversible competitive inhibitor binds noncovalently at site other than active site 0° Reversible noncompetitive inhibitor structure resembles substrate structure inhibitor does not alter the maximum reaction rate Irreversible inhibitor binds.covalently and permanently at site other than active sitehich of the following are advantages of quaternary structure? Choose all correct nswers 1) The genes may be for single subunits, rather than requirement for transcription and translation of giant sequences 2) Subunit construction may provide the structural basis for protein regulation 3) Multi-subunit proteins are more water soluble than single subunit proteins of the same size 4) Defects in protein synthesis may be fixed at the subunit level, rather than giant polypeptide level 5) May have multiple active sites - one on each subunit
- Which of the following statements regarding enzyme catalysis is false? All options are false. Once formed, the transition state slowly proceeds to forming the product at a rate determined by cofactor binding The free energy of binding of the enzyme to the transition state is more favorable than the free energy of binding of the enzyme to the substrate The substrate and active site of the enzyme are solvated to promote enzyme-substrate interaction Once formed, the product dissociates from the enzyme after ATP hydrolysis in order to regenerate the active siteWhen the enzyme hexokinase binds to glucose and ATP it undergoes a conformational change. All of the following are true about this enzyme-substrate binding EXCEPT: The active site changes shape so that it binds more tightly to the substrates The substrates are optimally positioned for the reaction to occur The substrates become contorted or strained, which increases their reactivity The activation energy of the reaction increasesIn the following example an enzyme is being inhibited. This is an example of Active site Inhibitor Altered active site O Non-competitive inhibition O Competitive inhibition MacBook Air
- If you can clearly visualize the chymotrypsin mechanism of action, you should be able to picture the structure of the transition state right after the enzyme attacks the first substrate. Think hard about what we have covered, and visualize that transition state accurately:Classify the items as competitive or noncompetitive inhibitors for control of enzyme action. Bind to the allosteric site on the enzyme Not influenced by the concentration of substrate Resemble the substrate Do not resemble thhe substrate Bind to active site of the enzymeCatalysis through proximity and orientation effects involves: (select all that applies) Group of answer choices binding of acidic and/or basic groups in the binding site facilitating chemical reactions by binding substrates close to specific groups binding of substrate in specific, restrictive orientations depending on metal ions for catalysis