Based on our class discussion of the currently accepted mechanism for ribosome catalysis, draw a graph show what the likely pH vs. rate profile looks like over the pH range 6.0-8.0
Q: enzymatic activity. Which of the following procedures might help you to obtain soluble,…
A: Introduction: Genetically modified organisms are those in which genetic engineering techniques are…
Q: Bacterial species that are capable of synthesising the amino acid histidine do not need it in their…
A: Introduction Histidine is synthesized from phosphoribosyl pyrophosphate (PRPP), which is made from…
Q: Which of the following is false regarding Serine Proteases? O They employ general acid-base…
A: Answer is a.) they employ general acid base catalysis.
Q: The rate of the peptidyl transferase reaction increases as the pH increasesfrom 6 to 8. Explain…
A: Peptidyl transferase is an enzyme that catalyzes the addition of an amino acid residue in order to…
Q: Adenine phosphoribosyltransferase converts adenine to AMP. If you were to determine whether a…
A: Thymidine kinase enzyme helps to convert AMP to deoxyribonucleotide. There are four different…
Q: The diagram below shows the substrate binding cleft for a protease, providing the substrate…
A: Note : Hi ! Thank you for the question. We are authorized to answer one question at a time. Since…
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: To approximate the concentration of enzymes in a bacterial cell, assume that the cell contains equal…
A: An enzyme is a substance that acts as a catalyst in living organisms regulating the rate at which…
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: 1 Specify the role each of the following amino acids play within the crystal structure and/or active…
A: "Since you have asked multiple questions, we will solve the first question for you. If you want a…
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: What does a graph of fluorescent relative units (RFUs) vs. time (s) tell about kinetic parameters…
A: The term enzyme inhibition is referred to a decrease in the activity of an enzyme-like decrease in…
Q: H3. Draw the Lineweaver-Burk plots for the reaction that your selected enzyme is involved with and…
A: Inhibitors are substances which inhibit the activity of an enzyme. Inhibitors bind to the active…
Q: You plot a reaction progress curve and find the equation of the line to be y = -0.0961x + 0.7142.…
A: Introduction :- Lysozyme is a naturally occurring enzyme which is found in our body secretions such…
Q: The key catalytic amino acids of the lysozyme active site in the free enzyme are Glu 35 with a…
A: The catalytic mechanism of lysozyme involves both general acid and general base catalysis.
Q: The enzyme Lysozyme is present in human nasal mucus and catalyzes the breakdown of a component of…
A: Enzyme kinetics determines the kinetic parameters of enzyme such as the maximum rate of the reaction…
Q: Describe a common feature at the active site of serine proteases and acetyl cholinesterase
A: Acetylcholinesterase is an enzyme that catalyzes the hydrolysis of acetylcholine (which is a…
Q: Phosphatidylserine (PS) is considered to be an intermediate in the biosynthesis of…
A: Phosphatidylserine is a lipid molecule that is negatively charged. It is composed of a backbone of…
Q: Sydney Brennen isolated Salmonella typhimurium mutants that were implicated in the biosynthesis of…
A: By the use of minimal and deficit medium scientist can characterize different classes of mutants and…
Q: A yeast disaccharidase can hydrolyze sucrose and maltose according to the following table: Use…
A:
Q: You receive kinetic data for a transferase reaction where AX and B are substrates, while A and BX…
A: Enzymes are biological molecules that act as catalysts in the conversion of substrate to products.…
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: 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: Using the word anomeric carbon, “acceptor” nucleophilic substrate, and activated “donor”, describe…
A: In polysaccharides the monosaccharide units are linked by glycosidic linkages.
Q: Urease enzyme hydrolysed urea at [S]= 0.03 mmol/L with a Km value of around 0.06 mmol/L. The initial…
A: Vmax is the reaction's maximum speed at which all of the enzymes become saturated with the…
Q: The Shine-Dalgarno sequence binds to sequence within the large ribosomal subunit so that ribosomes…
A: in order to address the question, we'll first weigh out each option to arrive at the correct option.…
Q: Lysozyme catalyzes a "bi-bi" reaction. List, in order, the reactants that bind and the products that…
A: Enzymes are biological molecules (typically protein) that significantly speed up the rate of…
Q: Describe the mechanism of catalysis Thiamine Pyrophosphate (TPP), (Vit. B1) Pyridoxal Phosphate…
A: Introduction: The substance that increases the rate of the chemical reaction without changing itself…
Q: Please describe the information on transferase and draw its Michaelis-Menten Plot and annotate Km…
A: Enzymes are 3D tertiary globular proteins that function as reusable biological catalysts. Enzymes…
Q: If a small amount of [1−14C] glucose is added to an aerobic yeast culture, where will the 14C label…
A: In the glycolytic process, the glucose is get converted or formed into 3 molecules of pyruvate. In…
Q: The enzymatic activity of lysozyme is optimal at pH 5.2 and decreases above and below this pH value.…
A: The enzyme lysozyme cleaves the glycosidic bond that connects N-acetyl muramic acid with the N-…
Q: The enzyme Lysozyme is present in human nasal mucus and catalyzes the breakdown of a component of…
A: Hi! Thank you for the question. We are authorized to answer three subparts at a time, since you have…
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: Discuss the reaction catalyzed by helicases and key aspects of their mechanisms.
A: During the DNA replication, the two strands are separated with the help of motor protein and result…
Q: pH will you try to bind lysozyme to a cation exchanger
A: Lysozyme is an antimicrobial enzyme that catalyzes the breakdown of peptidoglycan in the cell wall…
Q: i) Explain the pH dependence of lysozyme catalysis shown in the Figure 1 below 100 50 4 8. 10 pH…
A: Lysozyme It is enzyme which is found in secretions of body like tears, mucus, saliva, etc. This…
Q: Mechanisms of catalysis: 2.6 Mechanism of lysozyme summary. These mechanisms involve several of…
A:
Q: The diagram below shows the substrate binding cleft for a protease, providing the substrate…
A: Proteases are enzymes which digest the proteins by cleaving the peptide bonds at specific locations.…
Q: hat is the initial velocity measurement for the hydrolysis of 50 μM amoxicillin by the enzyme
A: Generally, the initial velocity is the velocity of the object before the effect of acceleration that…
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: . Phosphatidylserine (PS) is considered to be an intermediate in the biosynthesis of…
A: Phosphatidylserine : It is fatty substance produced in the body that covers and protects every cell…
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 isoelectric point, pl, of the protein deoxyribonuclease I is 10.2 , while that of pepsin is 1.…
A: Amino acids contain at least two ionizable groups-alpha the carboxylic acid group and the…
Q: A single polypeptide chain houses the transferase and debranching enzyme. Cite a potential advantage…
A: Carbohydrates are the preferred biomolecule for the production of energy in the cell. Glucose is…
Q: The turnover number for an enzyme is known to be 5000min-1. Given the following set of data,…
A: Enzyme kinetics is defined as the study of chemical reactions which are catalyzed by enzymes. Km is…
Q: Is the following statement correct or incorrect? It is only possible to employ enzymes that are…
A: Biocatalysts are chemicals that are used to speed up biological processes. Biocatalysts are used to…
Q: Based on your understanding of the structure and function of the enzyme chymotrypsin, explain why…
A: Enzymes are highly specialized proteins that have extraordinary catalytic power, greater than that…
Q: calculate the turnover number for an enzyme, assuming Vmax is 0.5M.sec-1 and the concentration of…
A: Turnover number is the maximal number of molecules of substrate converted to product per active site…
Q: Using the word anomeric carbon, “acceptor” nucleophilic substrate, and activated “donor”, describe…
A: The oligosaccharides are formed by connecting monosaccharides via glycosidic linkages.
Based on our class discussion of the currently accepted mechanism for ribosome catalysis, draw a graph show what the likely pH vs. rate profile looks like over the pH range 6.0-8.0
Step by step
Solved in 2 steps with 1 images
- Describe the experimental evidence that supports lysozyme’s catalysis by acid– base catalysis, covalent catalysis, and transition state stabilization.Using the catalytic mechanism of serine proteases, draw and label a reaction coordinate diagram/graph of the chymotrypsin-catalyzed hydrolysis of a peptide bond.To approximate the concentration of enzymes in a bacterial cell, assume that the cell contains equal concentrations of 1,000 different enzymes in solution in the cytosol and that each protein has a molecular weight of 100,000. Assume also that the bacterial cell is a cylinder (diameter 1.0 μm, height 2.0 μm), that the cytosol (specific gravity 1.20) is 20% soluble protein by weight, and that the soluble protein consists entirely of enzymes. Calculate the average molar concentration of each enzyme in this hypothetical cell.
- if the reaction pH drops significantly (pH=2 for example), how would reaction catalyzed be serine proteases be affected? why? (assumin that the rest of the protein structure remain intact)Trypsin, a peptidase that hydrolyzes polypeptides, functions in the small intestine at an optimum pH of 7.7–8.0. How is the rate of a trypsin-catalyzed reaction affected by each of the following conditions?The protease used in this procedure functions best at 50°C. Would you expect this enzyme to be isolated from Escherichia coli bacteria? Explain your answer. Hint: Where does E. coli live?
- Lysosyme catalyzes the hydrolysis of the carbohydrate linkage in part of the bacterial cell wall (peptidoglycan layer). 1. Propose a mechanism using general acid/base catalysis 2. Propose a mechanism using covalent catalysis. (An intermediate has been observed that indicates a glycosidic bond to the aspartate).An enzyme catalysed reaction has a Km of 8 mM and a Vmax of 13 nM.s-1. Use the Michaelis-Menten equation to calculate the reaction velocity when the substrate concentration is 18 mM.Based on your understanding of the structure and function of the enzyme chymotrypsin, explain why proteolytic activation by Trypsin in the intestine is required for chymotrypsin to bind its substrates with high affinity. Your answer should include a description of the amino acid residue or residues involved AND a kinetic experiment that suggested this.
- Consider the following mechanism: Circle and label one place on the mechanism where covalent catalysis is occurring. Suggest an amino acid that could fill the role of residue “A” in the mechanism above and draw its structure at pH 7.4. Suggest an amino acid that could fill the role of residue “B” in the mechanism above and draw its structure at pH 7.4. Under standard conditions, this reaction is unfavorable (DG¢° = 23.8 kJ/mol). What conditions in the cell allow for the actual free energy change to be lower (DG » 0), making the reaction readily reversible? Explain your answer. *please help and explain as well as you can*Using the word anomeric carbon, “acceptor” nucleophilic substrate, and activated “donor”, describe how Glycosyl transferase's (and glycosidases) catalyze glycan and glycoconjugate formation Please answer asapConstruct the mechanism of a serine-protease with a catalytic triad.