Calculate the reacion Kcat Tor the Control in experiment (1). e. Draw a velocity versus [S] showing Michaelis-Menten curve for the Control. Clearly show Vmax and Ky for the enzyme. [S] (mM) (1) V. (2) V- (3) V- [(µmol/(ml.s)] [(umol/[ml.s)] [[µmol/(ml.s)] 7.6 14.6 26.6 45.8 4.4 8.6 16.4 6.6 11.4 17.8 24.6 8. 16 29.8 40.8 24 60 28.2

Q: An enzyme that follows simple Michaelis–Menten kinetics has an initial reaction velocity of 10…

A: The answer is given in the image given below.

Q: 2. Calculate AG for the exchange of 3 Na* by 2 K* by Na*-K* ATPase (in kJ per mole of ATP) under the…

A: Gibbs free  energy change for the exchange of 3Na and 2 K by Na-K ATPase It is a thermodynamic…

Q: value of AG" for the conversion of 3-phosphoglycerate to 2-phosphoglycerate (2PG) is +4.40 kJ/mol.…

A: dGo = -RTlnKeq T = 25 + 273 = 298 K Keq = [2-phosphoglycerate]/[3phosphoglycerate]

Q: The turnover number for an enzyme that approximates Michaelis-Menten kinetics is known to be 500…

A: Turn over number of an enzyme is the maximum number of substrate molecules that are converted into…

Q: [S] > Km Not true for any of these conditions Almost all active sites are empty. [ES] is much higher…

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

Q: [S] mM 20 50 100 200 300 500 700 Initial Velocity (mM/min) 1.012 1.950 2.823 3.637 4.024 4.398 4.580

A: Enzyme kinetics can  be determined by constructing mm plot or lb plot. With them km and Vmax can be…

Q: Cif only statement A is correct, Hif only statement B is correct, E if both statements are correct,…

A: In the Michaelis- Menton plot, x-axis represents substrate concentration and y-axis represents…

Q: For an enzyme that follows simple Michaelis-Menten kineticS, what is the value of Vmax (in units of…

A:

Q: The energy of activation for the reaction 2 HI - H2 + I2 is 180. kJ-mol-1 at 544 K. Calculate the…

A:

Q: Most of the enzyme reactions followed the mathematical kinetic plots suggested by Michaelis-Menten…

A: Introduction: Those substances that increase the pace of the reactions that occurs within the living…

Q: when saturated with substrate, an enzyme has a maximum initial rate of 110mumoles of substrate…

A: Asked : Reaction rate when substrate concentration is 2x10^-3M

Q: If a michaelis-type enzyme has an apparent Km of 2*10^-8 and apparent Vmax of 1*10^-4 moles/min in…

A: Uncompetitive inhibitors bind only to the enzyme–substrate complex and reduce both kcat and Km (the…

Q: 1. What is the keat of this enzyme? 2. At which concentration of the substrate this enzyme reaches…

A: Given, Km = 200 μM [ETotal] = 10 nm = 0.01  Vmax = 2.5 μM/s

Q: Based on the definition of kcat, substitute a value that can be measured and yet still represents…

A: since this is a multipart question, so I will be answering the first question only, kindly post the…

Q: Lineweaver-Burk plots of enzyme kinetics for the reaction, S P, has the following features: 1/v is…

A:

Q: 7. You obtain the following set of data for two enzymes that follow Michaelis-Menten kinetics:…

A: Michaelis Menton kinetics describes the relation between rate of reaction and substrate…

Q: Qis an analog of substrate A that binds to enzyme X and produces the following kinetics: [A] Vo…

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

Q: Compute for the AST (Aspartate Aminotransferase activity) of 0.10 mL serum sample mixed with 1mL of…

A: Step 1 AST activity: AST or Aspartate Aminotransferase activity is the measurement of AST in blood.…

Q: 1. A Lineweaver-Burk Plot is shown below. 30 25 Curve A y = 3.1207x + 2.4978 20 15 Curve B y =…

A: If an enzyme follows Michaelis-Menten Kinetics, a plot of the reciprocal of the reaction…

Q: L(24 points) Explain How is the Michaelis constant defined. and what does a low or high value for Km…

A: Enzymes acts as the biological catalysts. They regulates the rate at which chemical reactions…

Q: The steady-state kinetics of an enzyme are studied in the absence and presence of an inhibitor…

A: An enzyme inhibitor is a compound that decreases or diminish the rate or velocity of an enzyme…

Q: iven the following information, calculate the catalytic efficiency of the enzyme. Step by step…

A: The substrate binds to the enzyme's active site and is converted to the product. Multiple…

Q: Hi I have this question, can you help me?

A: Michaelis Menton equation relates velocity of enzymatic reaction with substrate concentration.…

Q: The following kinetic data were obtained for an enzyme in the absence of an inhibitor (1) and in the…

A: The determination of Vmax and KM for any enzyme kinetic reaction requires the plotting of the data…

Q: Vmax [S] Km + [S] Vo = Eadie-Hofstee plot V v=Vm-Km [S] Lineweaver-Burk (L-B) plot 1 1 Km 1 Vm Vm…

A: Enzymes increase the rate of a reaction by decreasing the activation energy required for the…

Q: Neutral sphingomyelinase 2 converts sphingomyelin into ceramide and phosphorcholine. What kind of…

A: Neutral sphingomyelinase 2 (nSMase2) helps in breakdown of sphingomyelin to ceramide and…

Q: A bacterial enzyme catalyzes the hydrolysis of maltose as shown in the reaction given below:…

A: We know by Michaelis–Menten kinetics:  V0= Vmax[S]/ Km +[S] V0= velocity of reaction Vmax= maximum…

Q: Iculate the actual, physiological deltaG for the reaction Phosphocreatine + ADP > creatine + ATP at…

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

Q: The maximum saturation, 28.3ug of enzyme in 25ml water catalyzes the oxidation of ethanol at a rate…

A: Introduction Catalytic constant, also known as the turnover number can be given as kcat=v[Et]where v…

Q: Hexokinase in red blood cells has a Km of approximately 50 µM. What concentration of blood glucose…

A:

Q: An enzyme that follows simple Michaelis–Menten kinetics has an initial reaction velocity of 10…

A: GIVEN VALUES: Initial velocity= 10 μmol.min-1 Substrate concentration is 5 time the value of Km .…

Q: 2. A 500ul reaction containing 0.5 pmol of an enzyme following Michaelis –-Menten kineties with…

A: Enzyme increases the rate of the reaction without altering the equilibrium of the reaction. Enzymes…

Q: If the enzyme lactase has a Vo of 0.40 mM per minute when [S] = 1.25 mM, and a Vo of 1.0 mM per…

A: If an enzyme follows Michaelis-Menten Kinetics, a plot of the reciprocal of the reaction velocity…

Q: Estimate KI for a competitive inhibitor when [I] = 5 mM gives an apparentvalue of KM that is three…

A: Enzyme inhibition is the decrease in the rate of enzyme catalyzed reaction by presence of inhibitor…

Q: While furthering your studies of iocane powder you determine that a ceular enzyme, iocase will…

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

Q: (i) a) Construct an empty table with the following column headings: Substrate concentration [S] and…

A: Enzymes are usually protein molecules and catalyzes biochemical reactions without being consumed in…

Q: Two experiments were performed with the enzymeribonuclease. In experiment 1 the effect of…

A: Proteins that catalyze all the biochemical reactions in the body are called enzymes. They decrease…

Q: 3.An enzyme catalyzed reaction is studied and the following kinetic analysis is obtained: (S), mM…

A: Hello. Since your question has multiple sub-parts, we will solve the first three sub-parts for you.…

Q: Calculate AG for the below balanced redox reaction as written. You may find a list of standard…

A: I2 + 2e- gives 2I-1  Standard potential is 0.54 V(E° cathode) Al gives Al3+ + 3e- Standard potential…

Q: For an enzyme that obeys Michaelis-Menten kinetics, k, = 8.0 x 10° M-1 sec1, k.1 = 2.0 × 105 sec,…

A: Given values: K1 = 8×108 M-1sec-1 K-1 = 2×105 sec-1 K2 = 1×102 sec-1

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

A: Vmax km Competitive   remains same increases Non Competitive  Decreases remains same…

Q: Calculate the specific activity and kcat for this enzyme

A: Enzymes are catalyst that speed up the biochemical reaction by lowering the activation energy of the…

Q: The Keq (25C) of the reaction below is 635.67.  Fructose 1,6-biphosphate fructose -6-phosphate +…

A: The Gibbs free energy of a system represents the degree of randomness of the system. It is described…

Q: If the higher value of KM resulting in the new plot ( red curb ) is due to the presence of an enzyme…

A: The concentration of irreversible inhibitor is less than the concentration of enzyme, an…

Q: Consider the following data for an enzyme-catalyzedhydrolysis reaction in the presence and absence…

A: The reciprocal of the given data is as follows: 1/S (Mol-1) 1/V (min/micromol) Uninhibited 1/V…

Q: Calculate the overall ΔG° (report up to two decimal places) for the net reaction (see attached…

A: Standard free energy change is the Gibb's free energy at 273k temperature and 1 atm pressure ∆G°=…

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: 20. The following data are found for the steady state kinetics of a multi- subunit enzyme: [S]…

A: Introduction The study of the rates of enzyme-catalyzed chemical reactions is known as enzyme…

Q: 1.2) If the Km of an enzyme for it's substrate remains constant as the concentration of the…

A: If Km remains unchanged even after increasing the inhibitor concentration it shows that…

Violence

Violence is defined as a physical act that causes or is intended to cause harm. Violence can cause physical, emotional, or both types of harm. Violence is defined by the World Health Organization as the intended use of physical force and power that causes threat or harm against oneself, another person, or against a community or group, and has the potential to cause damage, death, mental distress, maldevelopment, or poverty.