BIOCHEM-ACHIEVE(FIRST DAY DISCOUNTED)
9th Edition
ISBN: 2818000069358
Author: BERG
Publisher: MAC HIGHER
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Question
Chapter 10, Problem 9P
Interpretation Introduction
Interpretation:
The molecule that can enhance the ATCase inhibition other than CTP needs to be suggested.
Concept introduction:
ATCase is Aspartate Transcarbamoylase enzyme which is an allosteric enzyme. This function is the catalysis of the first step of synthesis of pyrimidines. It is composed of both regulatory and catalytic subunits.
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1H. please help me in detail. For molecular Mechanism of ATP versus GTP selectivity of adenylate kinase
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Write an expression for the reaction velocity.
Chapter 10 Solutions
BIOCHEM-ACHIEVE(FIRST DAY DISCOUNTED)
Ch. 10 - Prob. 1PCh. 10 - Prob. 2PCh. 10 - Prob. 3PCh. 10 - Prob. 4PCh. 10 - Prob. 5PCh. 10 - Prob. 6PCh. 10 - Prob. 7PCh. 10 - Prob. 8PCh. 10 - Prob. 9PCh. 10 - Prob. 10P
Ch. 10 - Prob. 11PCh. 10 - Prob. 12PCh. 10 - Prob. 13PCh. 10 - Prob. 14PCh. 10 - Prob. 15PCh. 10 - Prob. 16PCh. 10 - Prob. 17PCh. 10 - Prob. 18PCh. 10 - Prob. 19PCh. 10 - Prob. 20PCh. 10 - Prob. 21PCh. 10 - Prob. 22PCh. 10 - Prob. 23PCh. 10 - Prob. 24PCh. 10 - Prob. 25PCh. 10 - Prob. 26PCh. 10 - Prob. 27PCh. 10 - Prob. 28PCh. 10 - Prob. 29PCh. 10 - Prob. 30PCh. 10 - Prob. 31PCh. 10 - Prob. 32PCh. 10 - Prob. 33PCh. 10 - Prob. 34PCh. 10 - Prob. 35PCh. 10 - Prob. 36PCh. 10 - Prob. 37PCh. 10 - Prob. 38PCh. 10 - Prob. 39PCh. 10 - Prob. 40PCh. 10 - Prob. 41PCh. 10 - Prob. 42PCh. 10 - Prob. 43P
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- Fill in the blanks.: Write Cif only statement A is correct, Hif only statement B is correct, E if both statements are correct, M if both statements are incorrect. A. An enzyme catalyzes a reaction by providing an alternative reaction pathway that has a lower energy of activation. B. The enthalpy of the enzyme-catalyzed reaction decreases significantly as compared to the uncatalyzed reaction.arrow_forwardI. Active site analysis. Below is a diagram of a putative active site for Monoamine oxidase. As we learned, the purpose of tertiary structure is to form a scaffold so you can orient just a few amino acids in the right orientation to promote binding and/or catalysis. The position where this occurs is the active site. The amino acid architecture of an active site is designed to bind substrates. Amino acid side chains are capable of hydrogen bonding, ionic and hydrophobic interactions. Fill in each amino acid that you think is suitable for interacting with the part of the substrate it is closest to. Assume the pH will be at 7.0 a.a.#1 a.a.#2 a.a.#6 HO Lond NH₂ НО a.a.#5 OH a.a.#3 a.a.#4arrow_forwardCTP inhibits ATCase; however, the inhibition is not complete. Can you suggest another molecule that might enhance the inhibition of ATCase?arrow_forward
- distribution of Benzene in a 4-compartment PBK model after an exposure of 6h. Convert Berkeley Madonna code to Matlab. Note: The parameters in the table below are for a mouse model. 1a) What are the two type of products containing Benzene consumers were recently concerned about. Which of these two different type of products is likely more harmful? (hint: check news/reports and social media channels) 1b) Plot Jresp along with the concentrations of Benzene in blood, fat, non-fat and liver in a 24h window (pdf). Why is Jresp slightly decreasing within 6h of exposure? Here is the Berkeley Madonna code: {Top model} METHOD RK4 STARTTIME = 0 STOPTIME = 24 DT = 0.02 {Reservoirs Blood, Fat, NonFat and Liver} d/dt (NF) = + Jnf INIT NF = 0 d/dt (F) = + Jf INIT F = 0 d/dt (B) = - Jnf - Jf - Jl + Jresp INIT B = 0 d/dt (L) = + Jl - Jmetab INIT L = 0 {Flows} Jnf = Qnf*(Cb-Cnf) Jf = Qf*(Cb-Cfv) Jl = Ql*(Cb - Clv) Jmetab = vmax*Cl/(Km +…arrow_forwardA. Lineweaver-Burk plot of the enzyme with increasing amounts of substrate in the absence or the presence of the inhibitor is shown below. Graph A : x-intercept Graph B : x-intercept = - 0.012, y-intercept = 0.8 Graph C : x-intercept = - 0.027, y-intercept = 0.8 Graph D : x-intercept = - 0.039, y-intercept = 0.8 - 0.007, y-intercept = 0.8 Graph A 4 Graph B Graph C Graph D 1 -0,04 -0,02 0,00 0,02 0,04 1/[Substrate] (uM) (i) Which graph indicates an enzymatic reaction without inhibitor? (ii) Which type of inhibitor is it? Briefly explain. (iii) Which graph indicates the highest concentration of inhibitor? (iv) Calculate the Vmax and Km of the graph showing an enzymatic reaction with the lowest concentration of inhibitor. Show the steps of calculation and unit in your answers. Keep 2 decimal places in your answers. 1/Rate (umol/min)arrow_forward1J. Please help me in detail. for molecular Mechanism of ATP versus GTP selectivity of adenylate kinasearrow_forward
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