Predict the effect of mutating Asp 102 of trypsin to Asn (a) on substratebinding and (b) on catalysis.

Q: How does ground state destabilization, transition state stabilization, and proximity lead to…

A: Enzymes are protein molecules that speed up the biochemical reactions by decreasing the activation…

Q: Structural similarity between the SARS-CoV-2 Mpro protease and chymotrypsin suggests that they would…

A: Coronaviruses are positive sense RNA viruses which are enveloped by capsid. They can cause severe…

Q: Consider the pathway for catabolizing galactose. What are the potential control points for this…

A: Galactose is metabolized mainly in the liver, which is an important dietary sugar. Lactose gives…

Q: Propose a metabolic I pathway for methotrexate

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Q: While R256T and K364R are at different positions, both mutations are present in the active site.…

A: Two substitution mutations are made in the active site of the given protein or enzyme. The active…

Q: Phosphoglycerate kinase shows induced fit resulting from the binding of both substrates to form the…

A: Phosphoglycerate kinase is a glycolysis enzyme that catalyses the seventh reaction in the ten-step…

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: Explain why several biochemical pathways start by putting a coenzyme A onto the molecule that…

A: For the functioning of an enzyme, a non-protein compound is usually needed. They loosely bind to…

Q: Catalase breaks down hydrogen peroxide about107times faster than the uncatalyzed reaction. If the…

A: Enzyme catalysis is the increase in the rate of a process by a biological molecule, an enzyme by…

Q: The active site of lysozyme contains two amino acid residues essential for catalysis: Glu35 and…

A: Lysozyme is an antibacterial enzyme that plays a crucial role in prevention of bacterial infections.…

Q: a) Based on the mechanism shown in Figure 2A, what type of enzyme is transpeptidase? : Lyase…

A: Note : Hi ! Thank you for the question. We are authorized to answer three subparts at a time. Since…

Q: An inhibitor that specifically labels chymotrypsin at histidine 57 is N-tosylamido-l-phenylethyl…

A: Trypsin is an enzyme that helps to digest protein. It breaks down the process of digestion that…

Q: Comment on Figure 2a and Figure 2b regarding stabilization of the transition state and…

A: From the given energy diagrams; It is seen that the enzyme (E) and the substrate (S) at the start of…

Q: Identify the effect of lowering the KM of phosphoglucoseisomerase on Phosphofructokinase activity. O…

A: There is no change in the activity  level by lowering the KM of phosphoglucoseisomerase on…

Q: Chymptrysin preferentially binds thetransition state. Explain what is meant by this.

A: Chymotrypsin is defined as a “hydrolytic enzyme”. It is a member of the super-family, belonging to…

Q: Graphically explain the term saturation of the enzyme? Why is the rate of an enzymecatalyzed…

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

Q: Briefly, describe enzyme multiplicity and broad substrate selectivity for cytochrome P450.

A: Enzyme cytochrome P450 is an important enzyme in many metabolism processes. It is primarily present…

Q: What is the evidence that aspartate transcarbamoylase (ATCase) effects catalysis primarily by…

A: Aspartate carbamyl transferase or astartate transcarbamoylase, transfers a carbamoyl group from…

Q: Explain the biochemical importance of the components of the cholesterol biosynthetic pathway.

A: Cholesterol levels in the body is found from 2 major sources: Dietary intake and the process of…

Q: Chymotrypsin, trypsin, and elastase all share the same catalytic mechanism, but have different…

A: Proteases are enzymes that cleave polypeptide chains. They all hydrolyze the peptide bond present in…

Q: propose a mechanism for the TPP- dependent step in isoleucine biosynthesis. draw the prdicted…

A: Co-factors are non-protein components of holoenzyme that helps in the functional activity of an…

Q: Lysozyme is an antibacterial enzyme found in animals.  Residues Asp 101 and Arg 114  are required…

A: Introduction- Lysozyme helps in catalyzation of binding energy where it catalysis the peptidoglycan…

Q: In the "biochemical assay of b-galactosidase activity", what is o-nitrophenyl-b-D-galactosidase…

A: Introduction The lac operon model was first proposed by F. Jacob and J. Monod.  Lac operon  an…

Q: Explain the basis for the following statement: As a coenzyme, pyridoxal phosphate is covalently…

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Q: Diagram the hydrogen-bonding interactions of the catalytic triad His–Lys–Ser during catalysis in a…

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Q: From the complete oxidation of glucose (glucose → 6CO2), how many total nucleotide triphosphates are…

A: Glucose is metabolized through the glycolytic pathway to yield energy in the form of ATP and NADH.…

Q: b) Lysozyme cleaves the peptidoglycan layer of bacteria. Briefly explain the roles of the residues…

A: Lysozyme catalyzes the hydrolysis of glycosidic bonds in bacterial cell wall peptidoglycan.

Q: Given the active site below, which best describes the mechanism(s) of catalysis?

A: Active site of the enzyme is the region present on the enzyme where enzymatic catalysis occurs and…

Q: In addition to the reactions mentioned in Section 23.5, PLP can catalyze b-substitution reactions.…

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Q: Sketch curves for reaction velocity versus [fructose-6-phosphate] for the phosphorylated and…

A: Phosphofructokinase 2 (PFK2) is an enzyme that is responsible for the regulation of glycolysis rate.…

Q: How Does Destabilization of ES Affect EnzymeCatalysis?

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Q: Consider applying biocatalytic reduction with carrots to the following two ketones: tert-butyl…

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Q: Glutamine affects the regulatory system for E. coli glutamine synthetase so as to promote the…

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Q: . (a) Explain the biochemical basis for the fact that one can synchro- nize cell populations by…

A: dATP is a nucleotide used in cells for DNA synthesis, as a substrate of DNA polymerase. It is…

Q: We talked about the types (mechanisms) of catalysis, including acid-base catalysis, covalent bond…

A: Mechanism for Peptidoglycan cleavage by Lysozyme- lysozyme is an enzyme which lyses the bacterial…

Q: @) so this eniyme catalytically pufet ? Explain your keasoning. , ik (b) What is Vmaz, |-4 nomol /me…

A: a) Given, K1 = 1.4 X 108 M-1s-1                K2 = 2.5 X 105 s-1               K3 =  1.5 X 103 s-1…

Q: Using the principles described in the text regarding pyridoxal phosphate mechanisms, propose a…

A: Introduction: The exchange of an amino (- NH2) group from an amino acid to a keto acid is known as…

Q: Under standard conditions, is the oxidation of free FADH2 by ubiquinonesufficiently exergonic to…

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Q: Why cAMP is an important player for the regulation of enzymes by covalent modification mechanism?

A: A covalent modification can be defined as the mechanisms in which the covalent bonding of another…

Q: An uncatalyzed reaction has keq=50. in the presence of an appropriate enzyme.the forward rate of the…

A: The enzyme does not change the equilibrium constant (Keq) of a reaction. Hence the value of the…

Q: Given the active site diagram below, indicate the mechanism(s) of catalysis.

A: The given enzyme substrate complex diagram indicates that the enzyme is phosphatases and substrate…

Q: Serine esterase contains a catalytic triad at its active site. Which amino acid in serine esterase…

A: Serine esterase contains three amino acids, His 57,Ser 195 and Asp 102.These three residues form a…

Q: What are the amino acids of the catalytic triad of chymotrypsin? State the mode catalysis shown by…

A: To get the remaining sub-parts solved, please repost the complete question and mention the sub-parts…

Q: What is the biochemical rationale for ATP serving as a positive regulator of ATCase?

A: Introduction: The first step in the pyrimidine biosynthetic pathway is catalysed by aspartate…

Q: The mitochondrial form of carbamoyl phosphate synthetase is allosterically activated by…

A: The organelle mitochondria is known as one of the most crucial organelle in the cell because there…

Q: Some bacteria contain three different forms of aspartokinase, each with its own mode of regulation.…

A: Aspartokinase is an enzyme which catalyzes the phosphorylation of aspartate, an amino acid.  It…

Q: In 1966, Ferdinand showed that a random-order ternary-complex mechanism for a two-substrate…

A: Ferdinand in the year 1966 showed that a randon order reaction for the two substrate enzyme…

Metabolic pathways

Metabolism is defined as the group of life-supporting, enzyme-mediated chemical reactions in organisms. A metabolic pathway is a set of these chemical reactions that involve anabolism (synthesis of complex biomolecules) and catabolism (breakdown of biomolecules into small molecules) that occur inside a cell. Metabolites are the reacting substances, products, and intermediate substances of an enzymatic process that are altered by a series of chemical events catalyzed by enzymes.