You have discovered a new enzyme that has a nearly identical active site to chymotrypsin. This new enzyme uses the same catalytic triad and the same reaction mechanism as chymotrypsin. Your new enzyme differs from chymotrypsin because it cuts peptides at the C terminus of polar, non- ionizable R groups. A) Beginning with the first tetrahedral intermediate, draw the mechanism of catalysis that occurs to cleave the tripeptide Asn- Phe- Lys substrate ending your answer with the product and free enzyme.

Q: The following data were obtained in a study of an enzyme that is known to follow the…

A: Michaelis menten constant, Km is the substrate concentration required to produce half maximum…

Q: What is the relationship between a transitionstate analog and the induced-fit model of enzyme…

A: Induced-fit model : A model of enzyme catalysis in which the enzyme conformation changes in response…

Q: Would you expect an “enzyme” designed to bind to its target substrate astightly as it binds the…

A: An enzyme is a substance that acts as a catalyst in living organisms, regulating the rate at which…

Q: You have discovered a new enzyme that has a nearly identical active site to chymotrypsin. This new…

A: As given peptide is Asn-Phe-lys, and discovered enzyme cleaves at C terminal of non ionizable polar…

Q: , non-ionizable R groups.

A: Introduction  Beginning with the first tetrahedral middle of the road, draw the instrument of…

Q: Where do each of these 5 main themes occur in the chymotrypsin mechanism?

A: Chymotrypsin is also called a serine protease as it has a serine residue in its active site. Ser-195…

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: How many molecules of urea can one molecule of urease act on in 12.0 min ?

A: Number of molecules of urea in one molecule or urease act on in 12.0 min is given below in the 2nd…

Q: Beginning with the 1st tetrahedral intermediate, show the complete steps in chymotrypsin mechanism…

A: The peptides are formed by linking different amino acids through peptide bonds. The enzyme involved…

Q: Circle and label one place on the mechanism where covalent catalysis is occurring. Suggest an amino…

A: Glycolysis is a catabolic breakdown of Glucose into pyruvate which consist of 10 metabolic steps. so…

Q: Based on the kinetic constants below, which enzyme will most efficiently catalyze conversion of the…

A: Enzymes are protein molecules that increase the rate of reaction by decreasing the rate of reaction.…

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: Substrates and reactive groups in an enzyme’s active site must be precisely aligned in order for a…

A: An enzyme is a biological compound (protein) that is capable of speeding up biochemical reactions.…

Q: This question should be answered with two or three sentences using relevant biochemical vocabulary.

A: Serine endopeptidases or serine proteases are enzymes with nucleophilic serine at active sites which…

Q: For a simple enzyme-catalyzed reaction, double reciprocal plots were determined for three different…

A: If ET is increased, Vmax will increase, because Vmax= k2[ET]. But KM= (k-1 + k2); i.e. it is…

Q: why is biocatalysis over inorganic catalysts in enzyme catalysis favored?

A: Those substances that increase the pace of the chemical reaction without undergoing any change…

Q: What happens to the enzyme’s native conformation once it is denatured? What structural organization…

A: " Since you have asked multiple question, we will solve the first question for you. If you want any…

Q: Consider the metabolic pathway show below that converts substrate A to B with the enzyme A-ase, B to…

A: For regulation of A-ase: Feedback inhibition refers to the inhibition of the enzymes's activity by…

Q: What Role Does Transition-State Stabilization Play inEnzyme Catalysis?

A: The enzymes are the protein molecules used to catalyze a chemical reaction by speeding up the rate…

Q: What is the difference between the lock-and-key model of enzyme action and the induced-fit model?

A: Enzyme is a catalytic molecule that increases the rate of any chemical reaction without being used…

Q: Many isolated enzymes, if incubated at 37°C, will be denatured. However, if the enzymes are…

A: The enzyme is a protein that depends on many factors for its stability. It needs an optimal range of…

Q: When free water molecules are excluded from an enzyme’s catalytic pocket, is a catalytic −OH group…

A: Enzymes are the catalytic protein, which has the active site to bind with the substrate and result…

Q: How can we test the validity of the mechanism proposed for the catalytic triad?

A: A set of the 3 coordinated amino acids that can be present on the active site of some of the enzymes…

Q: Are enzyme-catalyzed reactions examples of homogeneous or heterogeneous catalysis?

A: Homogenous catalysis refers to a catalytic system in which the catalysts and the substances are in…

Q: Suppose that you measure the pH-dependence of an enzymatic reaction and you see a bell-shaped curve.…

A: Enzymes are specialized proteins that catalyze all biochemical reactions. Enzymes are categorized…

Q: Which of the following statements about ribozyme catalytic residues is INCORRECT? General acid…

A: Solution :-  the ribozyme Catalytic residues which are RNA molecules and it's fuction as chemical…

Q: The hydrolysis of a phenylalanine-containing peptide is catalyzed by a-chymotrypsin with the…

A: Enzymes are protein molecules that increase the rate of reaction by decreasing the activation energy…

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: Help me, please

A: Proteases are enzymes that catalyze the breakdown of the peptide bonds in the protein. Serine…

Q: When the final product of a series of enzymatically-catalyzed reactions binds to the first enzyme in…

A: Enzymes are the biocatalyst which are responsible for enhancing the rate of a reaction by decreasing…

Q: The following is the chemical structure of nicotinamide adenine dinucleotides, a coenzyme commonly…

A: Coenzymes are the complex organic molecules which pump up activity of enzyme and function as…

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: What features distinguish enzymes that undergo allosteric control from those that obey the…

A: Enzymes are the biocatalyst molecules that increase the rate of reaction by decreasing the…

Q: In a particular enzyme, an alanine residue is located in a cleft where the substrate binds. A…

A: Alanine have nonpolar side chain and if this nonpolar side chain is involved in some of hydrophobic…

Q: The chemical structure of Coenzyme A contains the following EXCEPT—     a β-mercaptoethylamine…

A: The correct  answer is LIPOIC ACID RESIDUE

Q: Mevalonate is a component of which biochemical pathway?

A: The carboxylate anion of mevalonic acid is known as mevalonate is of major pharmaceutical…

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: Match each reaction description to the type of enzyme that catalyzes the reaction.

A: Those proteins or biological catalysts which help to speed up the chemical reaction are termed…

Q: What roles do proximity and orientation play in enzymatic catalysis?

A: Enzymes are the catalytic protein which helps to produce the product when the enzyme act on the…

Q: Is the term KM used with allosteric enzymes? What aboutcompetitive and noncompetitive inhibition?…

A: Enzymes are biocatalysts that increase the rate of a reaction without getting used up in the…

Q: In an enzyme kinetics study, three inhibitors resulted to the following results: Inhibitor ABC…

A: The rate of a enzyme catalyzed reaction increases with temperature until a point and once the…

Q: Enolase has a glutamic acid residue in its active site. Describe the experiment that was done that…

A: Enolase is a metalloenzyme used in the 9th step of glycolysis it other name is PG i.e…

Q: The oxyanion hole is comprised of hydrogen bonding atoms that project into a space on the active…

A: Oxyanion hole is generally found in proteases and are located in catalytic site of enzymes.…

Q: create a single illustration that will interrelate or link the two opposing pathways, the…

A: Answer :- The glycogenesis synthesis of glycogen from glucose in liver and muscles is known as…

Q: In the pentose phosphate pathway reaction that produces subtrate used for nucleiuc acid synthesis,…

A: The Pentose Phosphate Pathway is an anabolic pathway which is carried out to synthesize NADPH and…

Q: You obtain a calculated Vmax of 4.26uM/s and a Km of 122.5uM from a kinetics experiment performed…

A: Ans- In order t find out catalytic efficiency, first we have to calculate turnover number (Kcat) .…

Q: What is the mechanism of an enzyme reaction involving a coenzyme for Nucleophilic Addition Rxns?…

A: Enzymes are essential components of all metabolic processes in the body. They are catalytic…

Q: . Would you expect an "enzyme" designed to bind to its target substrate as tightly as it binds the…

A: Enzymes are a special class of proteins that can catalyze a biochemical reaction. There are six…