In concerted model, all subunits in the enzyme are either in the low affinity or high affinity forms.
Q: Glycogen phosphorylase is an example of an enzyme that is regulated both by allosteric control and…
A: The enzyme's noncovalent contact can also be used to promote or inhibit the activity of the enzyme.…
Q: Based on some preliminary measurements, you suspect that a sample of enzyme contains an irreversible…
A: A molecule that connects to an enzyme and inhibits its activity is called an enzyme inhibitor.…
Q: Other things being equal, what is a potential disadvantage of an enzyme having a very high affinity…
A: Enzymes are the catalytic proteins that are known to catalyze the reaction and forms the product.
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A: The Michaelis-Menton equation is the equation for one substrate enzyme catalyzed reaction. This…
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A: Note: Since you have posted multiple independent questions in the same request, we will solve the…
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A: Enzymes are the biological catalysts that increase the rate of a biochemical reaction. They are…
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A: Enzyme kinetics deals with the rate of chemical reactions catalyzed by enzymes. The study of the…
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A: Enzymes are proteins that bind with the substrate to form a substrate-enzyme complex. Later, the…
Q: What happens to a denatured enzyme regarding its functionality? How can that result be explained…
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Q: name and explain the model that most likely accounts for cooperativity in enzymeNADH Also indicate…
A: Co-operativity is a phenomenon that is exhibited by enzymes or receptors. The enzymes/receptors are…
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Q: Draw a Lineweaver-Burke plot with two lines, one representing an uninhibited enzyme and another…
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Q: _____________ allosteric effects of enzymes involve ligands that are different from substrate…
A: Allostery is a direct and efficient means for regulation of biological macromolecule function,…
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A: Introduction: The organic molecules that are necessary for the growth and development of the body…
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A: Introduction: Enzymes are biological catalysts that are synthesized by the living cells of the body.…
Q: Which of the following statements about the dUTP substrate for a dUTPase is true?
A: Option 2 is correct. The dUMP product is more easily formed when catalyzed by the dUTPase because…
Q: Since KM is an intrinsic property of an enzyme, its value does not depend on the enzyme…
A: Km is the Michaelis constant. It is defined as the substrate concentration at which half of the Vmax…
Q: a) ; Construct a Lineweaver -Burk plot using the kinetic data shown in Table 1.. Determine Vmax and…
A: Michaelis menten constant, Km is the substrate concentration required to produce half maximum…
Q: Distinguish between the lock-and-key and induced-fit models for binding of a substrate to an enzyme.
A: The enzyme-substrate complex is a temporary molecule formed when an enzyme comes into perfect…
Q: In the induced-fit model of enzyme action, the active site on the enzyme provides an exact fit for…
A: Enzyme are substances that catalyze chemical reactions. They bind to reactant molecules, called…
Q: An example of an enzyme-catalyzed reaction proceeding via a transition-state stabilization mechanism…
A: Chymotrypsin is synthesized by the pancreas as inactive chymotrypsinogen. Chymotrypsin is a…
Q: Suggest a reason why heating a solution containing an enzyme markedly decreases its activity. Why is…
A: Enzymes are proteins. They are biocatalyst that increases the rate of a reaction. Enzymatic activity…
Q: Enzymes are stereochemically specific; that is, they oftenconvert only one stereoisomeric form of…
A: enzymes are proteins that are made up of amino acids. Enzymes contain active sites. These active…
Q: Why must enzyme activity be monitored under standard conditions?
A: The enzyme is a biocatalyst where the enzyme attracts subtract for the binding to its active site…
Q: Distinguish between the lock-andkey and induced-fit models for binding of a substrate to an enzyme.
A: Introduction: Enzymes are proteins that serve as biological catalysts. Catalysts help to speed up…
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Q: Each type of enzyme contains a unique, intricately shaped binding surface called a(n) _____________.
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A: “Since you have asked multiple question, we will solve the first question for you. If you want any…
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Q: If we describe an enzyme like aspartate transcarbamoylase and say that it exhibits cooperativity,…
A: Enzyme cooperativity is a phenomenon in which the shape of one subunit of an enzyme consisting of…
Q: In mathematical terms, what characteristic of a graphed line is a measure of enzyme reaction rate?
A: Introduction: Enzymes are macromolecular biological catalysts. Enzymes accelerate chemical…
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Q: effectors of enzyme kinetics
A: Enzyme kinetics is the process of understanding the chemical reactions which are catalyzed by the…
Q: Km value of an enzyme
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Q: Why do structural analogs of the transition-state intermediate of an enzyme inhibit the enzyme…
A: Transition state structural analogs of enzymes are chemicals with a structure that resembles the ES…
Q: What are the two types of enzyme inhibitors? Give anexample of each.
A: Introduction: Enzyme inhibitors are the molecules that bind to the enzyme and decrease its activity.…
Q: An enzyme with a low Km is considered to have a higher affinity for the substrate. Provide…
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A: DNS or Dinitrosalicylic acid reaction is used to detect the presence of reducing sugars present in…
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…
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Q: Based on the relative increase in purity, place the purification procedures used for this enzyme in…
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Q: In enzyme catalysed reactions, the energy level of the enzyme/substrate (or ES) complex is higher…
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Q: Calculate the specific activity and kcat for this enzyme
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Q: Please discuss the following statement. "If two ligands involve in the same number and type of…
A: Asked : Statement is true or false
Q: What TYPE of inhibition is observed in the following: S E S
A: A chemical that binds to an enzyme and inhibits its activity is known as an enzyme inhibitor.…
Q: Why is ATP alone not an effective allosteric regulator of enzyme activity?
A: Allosteric regulation is a type of regulation in which a regulator binds to the enzyme and controls…
Q: What are the similarities and differences in the regulation of monomeric, single substrate and…
A: Monomeric enzymes are the one which have a single polypeptide chain like lysozyme and hexokinase…
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- How would chymotrypsin's catalytic triad be affected by extremely low and extremely high pH values (assuming the rest of the protein remains intact)?>1HPL_1|Chains A, B|LIPASE|Equus caballus (9796) NEVCYERLGCFSDDSPWAGIVERPLKILPWSPEKVNTRFLLYTNENPDNFQEIVADPSTIQSSNFNTGRKTRFIIHGFIDKGEESWLSTMCQNMFKVESVNCICVDWKSGSRTAYSQASQNVRIVGAEVAYLVGVLQSSFDYSPSNVHIIGHSLGSHAAGEAGRRTNGAVGRITGLDPAEPCFQGTPELVRLDPSDAQFVDVIHTDIAPFIPNLGFGMSQTAGHLDFFPNGGKEMPGCQKNVLSQIVDIDGIWQGTRDFAACNHLRSYKYYTDSILNPDGFAGFSCASYSDFTANKCFPCSSEGCPQMGHYADRFPGRTKGVGQLFYLNTGDASNFARWRYRVDVTLSGKKVTGHVLVSLFGNKGNSRQYEIFQGTLKPDNTYSNEFDSDVEVGDLEKVKFIWYNNVINLTLPKVGASKITVERNDGSVFNFCSEETVREDVLLTLTAC Can you find the biological Function of horse pancreatic acid and highlight the catalytic amino acids in a row and active sites from the above sequence of 1HPLa. Suppose that you have the peptide Ala-Gly-Tyr-His-Leu and you treat it with FDNB and then 6M HCl. Draw the structures of all the products that you will have in solution (assume all reactions to go to completion).
- Globular proteins with multiple disulfide bonds must be heated longer and at higher temperature to denature them. Bovinepancreatic trypsin inhibitor (BPTI), having 58 amino acids in a single chain and 3 disulfide linkages, loses its catalytic activity whenheated at nearly 90°C for 5-10 minutes. Explain the molecular basis of this observed thermal property of BPTI relative to the nativestructure and function of the protein. please do not copy from other answers hereCarboxypeptidase Y (CPY) contains ten cysteine residues that form five disulfide bonds in the native structure of CPY. Suppose CPY is reduced and unfolded in urea.Part AIf the reduced unfolded protein were oxidized prior to the removal of the urea, what fraction of the resulting mixture would you expect to possess native disulfide bonds?Express your answer using three significant figures.Globular proteins with multiple disulfide bonds must be heated longer and at higher temperature to denature them. Bovinepancreatic trypsin inhibitor (BPTI), having 58 amino acids in a single chain and 3 disulfide linkages, loses its catalytic activity whenheated at nearly 90°C for 5-10 minutes. Explain the molecular basis of this observed thermal property of BPTI relative to the nativestructure and function of the protein. do not coy from other answers here
- Consider the complete oxidation of a mixed TAG containing the following fatty acid residues:At carbon 1: cerotic acidAt carbon 2: heptadecanoic acidAt carbon 3: palmitoleic acid Draw the structure of the mixed TAG.Studies at diff erent pH’s show that an enzyme has two catalytically important residues whose pKs are ∼4 and ∼10. Chemical modifi cation experiments indicate that a Glu and a Lys residue are essential for activity. Match the residues to their pKs and explain whether they are likely to act as acid or base catalysts.Bovine chymotrypsinogen has a molecular massof 25.6 kDa. Amino acid analysis shows that thisenzyme is 4.7% Gly (Mr 75.1).b. Calculate how many glycine residues are present in amolecule of bovine chymotrypsinogen
- With the aid of the simple generic diagram, identify and explain how the type of chemical bonding stabilizes a secondary structure present in 3GRS (glutathione reductase).With regards to arganine illustrate the pH-dependent transitions on a titration graph from most to least protonated. Indicate also the relevant part of the amino acid which is associated with the transition on that part of the graph.The pKa for histidine is pKa = 6.1 while that for cysteine is pKa = 8.0 2. Assume that both histidine and cysteine are catalytic groups for a particular enzyme. Assume also that the side chain of cysteine must be in the deprotonated form. Estimate the pH at which the catalytic activity of this enzyme is the maximum and sketch a pH-activity graph.