Q: is an enzyme that exhibits covalent catalysis is the name of the metal present in the active site of…
A: Enzymes are proteins which accelerate the rate of a biochemical reaction. Enzymes require substances…
Q: Explain the about Enzyme Cofactors ?
A: The enzymes are chemical substances that enhance the speed of the reaction. They act as catalysts in…
Q: d. If the active site of an enzyme were mutated so that its affinity (kM) for the substrate was…
A: Enzymes are biological catalysts that help in catalyzing or speeding up biological reactions by…
Q: Expand the biological abbrevation (i) ACTH (ii) TSH.
A: These two are abbreviations of hormones. Hormones are chemical messengers that are secreted…
Q: The term ____________________ refers to the sum total ofall the low-molecular-weight metabolite…
A: The metabolome includes compounds such as fatty acids, amino acids, vitamins, and carbohydrates that…
Q: dentify a competitive inhibitor and the enzyme that it impacts. Describe how the competitive…
A: Competitive inhibitors are those substances that compete with the substrates to bind to an active…
Q: Four process that may be used to refine oil
A: Refining of oil is an industrial process that involves the conversion of crude oil into useful…
Q: Identify the statements that are TRUE regarding cofactors and/or coenzymes. SELECT ALL THAT APPLY…
A: Enzymes are the biological catalysts that increase the rate of a biochemical reaction. Enzymes are…
Q: Enzyme Inhibitors inhibit the activity of the enzyme. i) Competitive Inhibitors: ii) Non-Competitive…
A: Enzyme inhibitors: Many substances can prevent enzymes from catalyzing or substantially diminish…
Q: The use of substrate analogues summary
A: Substrate analogs are chemical compounds resembling the substrate molecule in an enzyme-catalyzed…
Q: The term anaerobic describes a reaction occurring I Select ]
A: Cells are the basic structural and functional unit of an organism and is of two types namely…
Q: Q: What is maple syrup urine disease? which enzyme is defective in this disease?
A: Maple syrup urine disease is a genetic disorder in which there is a deficiency of enzyme known as…
Q: Distinguish between an oxidizing agent and a reducing agent
A: Oxidizing agent and reducing agent are chemical compounds involved in redox reactions. They are the…
Q: The secondary metabolite whose effect is highly dependent upon volatility is:
A: Many microbes, fungi, and plants synthesize a number of organic compounds or biomolecules which are…
Q: Explain what changes occur in the bioreactor in the phases marked 1, 2, and 3 in the following…
A: Microbes grown in a closed or batch culture in which certain conditions are that no nutrients are…
Q: Explain the pH
A: PH is generally the way to determine of acidity and alkalinity of a solution that is a number on a…
Q: ndicate whether each of the following changes represents oxidation or reduction. a. FADH2h FAD b.…
A: Cellular respiration is a catabolic pathway of the process of metabolism, where a series of chemical…
Q: Define the following terms: a. turnover b. cyt P450 c. detoxication d. detoxification e. epoxide
A: Enzyme is a biological molecule that catalyzes a biochemical reaction and increases the rate of…
Q: E Explain about Hunters disease. Which enzyme deficiency causes the disease?
A: Hunter's disease is a rare and inherited disorder which is caused when body does not properly…
Q: 25. Describe how enzyme action is affected by temperature, pH, enzyme concentration, and substrate…
A: The rate of enzyme reaction depends on various factors which includes temperature, pH, enzyme…
Q: Using appropriate examples, explain how environmental factorsaffect enzyme activity.
A: Enzymes are referred to as molecules of proteins that helps in increasing the metabolism rate and…
Q: Define the following terms: a. licensing factors b. RPA c. TEBP d. TRF e. RFC
A: DNA replication can be described as a molecular biology process during which two identical DNA are…
Q: The optimum temperature for enzyme activity in the body: O A. OC B. 10C O c. 40C O D. 60C 47
A: Introduction :- Proteins called enzymes aid in accelerating our bodies' chemical reactions, or…
Q: Identify the metabolic pathway or reaction based on the products produced. 4ATP +4 Hydrogen ions...…
A: METABOLIC PATHWAY: A sequence of chemical reactions that takes place in a cell which makes up and…
Q: Which of these is likely to reduce enzyme activity? Increasing pH level II. Decreasing temperature…
A: Introduction Enzyme activity:- Enzyme activity is the amount of substrate converted by the enzyme in…
Q: D. Describe the effect that each of the following changes would have on the rate of a biochemical…
A: Enzymes are substances that increase the rate or velocity of a reaction, causing the reaction to…
Q: The vitamin necessary to help as an antioxidant is a. A. b. D. c. K. d. E.
A: Vitamins are essential sources required in an animal's body but only in small quantities. Each…
Q: acts as a detoxifying agent. O Phosphorus B12 Sulfur O fluoride O vitamin C
A: Detoxification (detox, in short) is the process of allowing the body to eliminate the toxins in it.…
Q: (e) Explain the lock and key' mechanism of enzyme action.
A: The enzymes are capable of recognizing their substrates with high degree of specificity. The two…
Q: Write one controlling rate limiting enzyme from any pathway or cycle and clarify the following: a-…
A: An enzyme is a cellular catalyst that speeds up chemical reactions. Proteins that bind to…
Q: How would you be able to increase the rate of reaction after C? * A substrate concentration Late
A: As the substrate approaches the enzyme's active site, the enzyme-substrate complex is formed as a…
Q: Give four enzymes that are being used in medical therapy. Report two industrial uses of enzymes and…
A: Enzymes - Used for catalyzing various reactions for therapeutic , industrial uses
Q: C. Describe the effect that each of the following changes would have on the rate of a biochemical…
A: Enzymes are proteins molecules that increase the rate of a biochemical reaction. Enzymes have an…
Q: Suggest a reason why partially hydrogenated vegetable oils are used so extensively in packaged…
A: Partial hydrogenation of vegetable oils leads to the formation of trans fats. The process of partial…
Q: Show reaction mechanisms involving a coenzyme by (a) transfer reaction (b) redox reaction
A: Enzymes are substances which acts as biocatalysts in living organisms which increases the efficiency…
Q: Define the following terms:a. cofactorb. coenzymec. apoenzymed. holoenzymee. velocity
A: Introduction:
Q: Explain the relationship between enzyme sensitivity and theadaptations microbes make to their…
A: Enzymes can be defined as the proteins which are known as biological catalysts on the basis of their…
Q: 1. Cite five diseases that could be diagnosed with the determination of enzyme concentration. 2.…
A: Note : Hi ! Thank you for the question. We are authorized to answer one question at a time. Since…
Q: The acidic nature of chyme is neutralized by ________. a. potassium hydroxide b. sodium hydroxide c.…
A: The food entering the duodenum is acidic and due to which gastric activity occurs with the help of…
Q: Identify the type of reaction or mechanism undergone in each case
A: Methylbenzene has a methyl group attached to a benzene ring. There is a carbon atom at each corner…
Q: Identification of the active site of an enzyme: 1.6 The effect of changing pH
A: Enzymes are biological catalysts that carry out the essential biochemical reactions without…
Q: 9) What is a metabolic pathwa
A: Metabolic pathway is a series of chemical reactions happening within a cell. It consists of various…
Q: 2a) explain the difference between the net free energy change of a reaction and the activation…
A: This minimum energy with that molecules should be acquiring order for a collision to lead to a…
Q: 23, The following is correct regarding metabolism a, Catabolism = chemical reactions where organic…
A: Metabolism is process which ply vital role in the body by releasing and gaining of energy in form of…
Q: Predict or describe the absorbance or enzyme activity at: pH = 2 pH = 14 Explain your…
A: The single most crucial asset of enzymes is the ability to increase the rates of reactions going on…
Q: A. Briefly explain the factors that could affect enzyme activity B. How can these factors influence…
A: Enzymes are biological catalysts that are generally made up of proteins. They aid in the catalysis…
Q: Enumerate and discuss three disorders that could result from the absence of enzymes
A: Enzymes are highly specialized proteins that have extraordinary catalytic power, greater than that…
Q: aw materials: 2 kg p-aminophenol and 3 kgs acetic anhydride
A: Acetaminophen, also known as paracetamol, is the most commonly used analgesic and antipyretic…
Enzyme kinetics
In biochemistry, enzymes are proteins that act as biological catalysts. Catalysis is the addition of a catalyst to a chemical reaction to speed up the pace of the reaction. Catalysis can be categorized as either homogeneous or heterogeneous, depending on whether the catalysts are distributed in the same phase as that of the reactants. Enzymes are an essential part of the cell because, without them, many organic processes would slow down and thus will affect the processes that are important for cell survival and sustenance.
Regulation of Enzymes
A substance that acts as a catalyst to regulate the reaction rate in the living organism's metabolic pathways without itself getting altered is an enzyme. Most of the biological reactions and metabolic pathways in the living systems are carried out by enzymes. They are specific for their works and work in particular conditions. It maintains the best possible rate of reaction in the most stable state. The enzymes have distinct properties as they can proceed with the reaction in any direction, their particular binding sites, pH specificity, temperature specificity required in very few amounts.
Step by step
Solved in 2 steps with 1 images
- 1. The optimal conditions for salivary lysozyme (hydrolyzing glycoproteins ofbacterial wall) are 37 C- temperature and pH is 5.2. Explain the decrease in this enzyme activity if the temperature will rise up to 60 °C and pH will be changed to 8.0. To answer the question: a) draw the graph of the velocity dependency on temperature and pH; b) calculate the relative enzyme activity if 10 mg of lysozyme catalyzes the formation of 5 uM of the product per 2 minutes. 2 Consider the matic reaction schee: Asnaragine + H20 Aspartate+ NH3:Which substrate is the best substrate for chymotrypsin? O N-acetylphenylalanine ethyl ester with Km of 8.2 x 102 M and keat of 2.1 x 102 sec 1. O N-acetylmethionine ethyl ester with Km of 12.3 x 102 M and keat of 2.1 x 1o sec1. O N-acetylleucine ethyl ester with Km of 8.2 x 10o2 M and kcat of 4.1 x 102 sec1. O N-acetylalanine ethyl ester with Km of 4.1 x 101 M and kcat of 4.1 x 101 sec.Staphylococcal nuclease has a ΔΔG‡ of -84.1 kJ mol-1 at 25.0 °C. If the uncatalyzed rate is 0.630x10-13 µmol s-1, calculate the enzyme-catalyzed rate in µmol s-1. (Use R = 8.3145 J mol-1 K-1)
- 1. Suppose the following kinetic data was collected for an enzymatic reaction For each substrate concentration, calculate and show the average initial rate and its standard deviation. [substrate), mM initial rate, min¹ Average initial rate, min¹ 150 62 150 60 150 63 40 44 40 41 40 43 222 12 11 15 Calculation of rates (min) for acid phosphatase reaction General Procedure for the End Point Assay of What Germ Acid Phosphate The general procedure used for each assay except the concentration of p-nitrophenyl phosphate was varied. The concentration of acid phosphatase was 7.2 μM) and each assay involve a 5-minute incubations with enzyme. Using this information along with the extinction coefficient of the p- nitrophenol product of the reaction allows for the initial rate to be expressed in terms of min¹. Vo [E] = absorbance at 410 nm 0.677 = initial rate in min-1i) Re-arrange the Michaelis Menten equation so it involves the ratio [S]. Show all steps beginning Km noting any assumptions or required conditions. Km ii) Calculate the ratio [lo for the case when the rate of product formation is 68% of Vmax and the substrate is in great excess. d[P] dt : k₂ with = [E],[S] Km+[S]' [S]o Km iii) Explain, in a few sentences, why the ratio determines the ratio V Vmax V Vmax Begin by explaining the meaning of stating simply "it's the ratio...." is not sufficient. Include in your explanation the factors that effect v and Vmax. Consider what factors make v different from or equal to Vmax. Consider what Km represents concerning processes involving ES. " iv) Calculate KM at 310K at given the following rate constant information: k₁ = 17 s-¹M-1 at 300K with A = 7300 s-¹M-1 K-1₁ 6 s¹ at 300K with A = 14500 s -1 k₂ = 31 s¹ at 300K with A = 600 s-¹Given this research scenarios kindly construct a research framework. A researcher is interested to test the antibacterial activity of a Philippine Plant crude extracts against Beta-lactamase producing Klebsiella pneumonia isolated in a hospital setting. He will use the following concentrations of crude extract, 500mg/ml, 250mg/ml and 100mg/ml. Positive control: Tetracycline 10mg/ml and DMSO as the negative control.
- roblem 1An aerobic biochemical process uses a CSTR w/o recycle. The feed characteristics are asfollows: Influent substrate concentration, So = 200 mg/L; half- velocity coefficient, Ks = 50mg/L; maximum, specific substrate utilization rate, k = 5 g/g- day; yield coefficient, Y = 0.5g Xa/g substrate consumed; microorganism decay coefficient, b = 0.10 day-1.1. The process goal is the production of active biomass. Determine the hydraulicretention time that the reactor should be operated in order to maximize the reactoractive biomass concentration (Xa). How does this retention time compare with theminimum solids retention time that the system can theoretically be operated?Calculate the solids retention time safety factor.2. Based on the solids retention time for maximum Xa calculated above, estimate theactive biomass concentration (Xa) and the substrate removal efficiency (E, %)CHEM151/251 Biochemistry 1 a. Determine Km 1. The following data were obtained for a competitive inhibition study in which the [I] = 3 µM for each determination of vo in the presence of inhibitor. The Vmax = 200 μM P/min for both data sets. 200 Vo (UM P/min) 8 8 8 8 8 8 8 8 8 180 160 140 120 100 40 Name (Print)/ID #: the absence of inhibitor. Participation Question # 10 No Inhibitor 50 +Inhibitor 100 [Substrate] (UM) 150 b. Determine Km, app for the data obtained in presence of inhibitor. 200 c. Calculate the value for Ki. Note: a = 1 + [I]/Ki and a¹ = 1 + [I]/Ki*. for the data obtained inIncubating 10µl of an LDH sample for 5 min in the presence of 60mM of lactate and 100mM NAD+ resulted in an OD = 1.2. Total volume is 1ml. The protein 340nm concentration of the LDH sample was 2000µg/ml. Calculate specific activity in U/µg of protein (1 Unit of enzyme catalyzes the conversion of 1 µmole of substrate to product.
- 3. Below is a Michaelis-Menten plot for a wild-type (WT) and mutant (V105A) enzyme isolated from the bacterium Staphylococcus aureus. The enzyme is involved in carbohydrate metabolism and is a potential biocatalyst for the large-scale production of rare sugars. -1 v, μmol s¹ mg-¹ 1.50- 1.25- 1.00- 0.75- 0.50- 0.25- 0.00+ 0 100 → WT 200 300 [s], mM 400 500 → V105A (a) Estimate the Km and Vmax for the wild-type and mutant enzyme from the graph. (b) Calculate the Keat and Keat/Km for the wild-type and mutant enzyme based on your estimated values in (a) if the total enzyme concentration is 0.5 µmol/mg. (c) Is the mutant enzyme a more or less efficient catalyst than the wild-type enzyme? Briefly explain.Enzyme hydrolysis of glucose-6-sulfate occurs in a marine microorganism. The activity test is based on the rate at which glucose is metabolized. Its KM is 6.7 x 10-9 M and its Vmax is 300 nM min-1 in cell-free extract. Galactose-6-sulfate competes with the enzyme to inhibit it. When glucose-6-sulfate and galactose-6-sulfate are present at 2 x 10-5 M, the starting speed is 1.5 nM min-1. Take a look at the Ki for galactose-6-sulfate and figure out what it is.PTP1B Substrate kcat Km kcat/Km UM 10-7 x (s-1 M) DADEPYLIPQQG DADAPYLIPQQG DAAEPYLIPQQG AAAAPYLIPQQG 44.6 + 1.8 39.8 + 0.32 3.9 + 0.9 13.7 + 0.46 1.1 + 0.25 0.29 + 0.01 35.3 + 0.22 6.6 ± 0.22 0.53 + 0.02 34.7 + 0.25 52.7 ± 0.7 0.066 + 0.001 (d) (. ) The units for kcat/KM in the above are given according to standard scientific notation. On this basis what is the value of this kinetic parameter for the DADEPYLIPQQG substrate?