1. Substrate Enzyme 1 2 3 Look at the above diagram and understand what is being shown. Explain AND draw a graph depicting how the rate of the reaction depicted here is changing. 2. How will the rate of the reaction change with time after 3? How can we increase the rate of the reaction after 3?
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- Reaction rate 0.35 0.30 0.25 0.20 0.15- 0.10 0.05 0.00 0 1000 2000 Enzyme total is 5mM 3000 4000 1. Substrate concentration 1. The above graph is an enzyme reaction, what is the vMax, KM, and Kcat of this enzymatic reaction? What does vMax, kM and Kcat mean, explain? 2. What are the three forms of regulation that follow the Michaelis Menten kinetics? What are the mechanisms by which these inhibitors can regulate the enzyme?Question #1: Choanoflagelletes are a unicellular ancestor to animals. One observation to support this hypothesis is the appearance of adhesion molecules that are key to the development of multiceullarity. Bulk transport Gap junctions Animals. Adhesion, cell signaling Single-celled :} Insects, mammals, and other animals with bilateral symmetry (~10,000,000) Jellyfish and their relatives (10,000) } Sponges (10,000) Choanoflagellates (150) Despite their simple unicellular lifestyle they express adhesion molecules including cadherins and lectins (King et al., 2003) but don't seem to have molecules that are typically found in the extracellular matrix such as integrins or laminins (Williams et al., 2014). Design a microscopy experiment to test the assertion that choanoflagellates have (some) adhesion molecules and those molecules play a similar role in a closely related animal like sponges.Lysozyme catalyzes a "bi-bi" reaction, which means there are (how many) reactants and (how many) products. List, in order, the reactants that bind and the products that are released during a lysozyme-catalyzed reaction cycle -- be succinct but be specific. 1. First reactant = 2. First product = 3. Second reactant = 4. Second product %3D
- 1 Give the systematic names and the first three digits in the E.C. classifications of the enzymes catalysing the following reactions: (Note: it should be possible to deduce the classification and make a reasonable attempt at the systematic name from the information given in Chapter 1.) (a) R.CO.CH,CH,.Ñ(CH,); + H,0 = R.cO + HOCH,CH,.Ň(CH,)3 acyl choline acid anion choline (b) H,N.ÇOPO + H;N(CH,),.CH.Co, = H,N.C.NH(CH2)3.C CH.CO, +P, * NH3 * NH3 L-ornithine carbamoyl phosphate citrulline H (c) ATP + H,N.CHCO, + H,Ñ.CHCO, H,N.CH.CN.CHCO, + ADP + P, CH3 CH3 H,C Ö CH; D-alanine D-alanine D-alanyl-alanine ÇH,OH (d) Ç=0 + NADH + H* = ÇHOH + NAD ČH,OH glycerol ČH2OH dihydroxyacetone (e) СНОН 2 C=0 + CHOH СНОН CH,OH CH,OPO; ČHOH D-glyceraldehyde-3-phosphate CH,OPO? dihydroxyacetone-phosphate D-frucrose-1,6-bisphosphate (f) NADH + 2 ferricytochrome b, = NAD* +2 ferrocytochrome bs (g) UDP-galactose 2 UDP-glucose (glucose and galactose are aldohexoses differing in configuration at C4)22) answer the following question.. Refer to the kinetic scheme for competitive inhibition and the structures shown below to E+S ES E +P -co- CO- 1 2 EI Compound 1 was determined to act as a competitive inhibitor through standard inhibition studies. Structural studies did not show any resemblance to the transition state. Compound 2 was also determined to act as a competitive inhibitor. Structural studies showed that it does resemble the transition-state. The K, constant is used to assess relative affinity of inhibitors for enzymes. That is, each compound has its own K, value. We can interpret K, the same way we do with Ka values. True or False: K, > Kµ2. Briefly explain your answer.2. Threonine beta-epimerase is a pyridoxyl phosphate-dependent enzyme that catalyzes the reaction below. Provide a mechanism for the PLP-enzyme catalyzed reaction; you need to show the mechanism for the formation of the aldimine and the mechanism for the hydrolysis step that regenerates PLP. -20 PO. OH CO₂ NH3* Threonine beta-epimerase PLP OH NH3 H*N OH Pyridoxyl phosphate (PLP)
- - MULTIPLE CHOICE - Please answer properly QUESTION : 1. Which of the following statements is TRUE in the catabolism of cytidine triphosphate (CTP)? A. the final product will have the same type of nitrogen-containing ring as CTP B. the nitrogen-containing ring will be oxidized C. nitrogen will be released in the form of ammonia (ammonium ion) D. hypoxanthine will be an intermediate 2. Which of the following biomolecules is a lipid? A. all of the above B. triglycerides C. steroids D. fatty acidsA catalyst like lactase that assists in the metabolism od milk is best described as Group of answer choices homogeneous heterogeneous enzymatic non-truseable 7, What graph will demonstrate that experimental concentration data fit a second-order reaction? Group of answer choices ln[reactant] vs. time ln(k) vs. 1/T 1/[reactant] vs. time [reactant] vs. time ln(k) vs. EaReaction Profile 2 Reaction Profile 3 Reaction Profile 1 Reaction Profile 4 Reaction Profile 5 Choices: HO ! Sweet potato tuber extract H. OOH он HO H- H- -OH но. H- OH OH CH,OH OH ÓH ÓH H # Pig liver homogenate CH,OH H- -O- H- -OH H- OH CH,OH
- Vmax [S] Km + [S] Vo = Eadie-Hofstee plot Lineweaver-Burk (L-B) plot v=Vm-Km [S] Km 1 Vm Vm [S] 1 The equations above apply for Michaelis-Menten enzyme kinetics but are presented in three different formats. For uncompetitive inhibition The Michaelis-Menten equation becomes Vo-Vmax(S)/(Km+a'[S)) Put the Minchaelis-Menten equation for uncompetitive inhibition in the Lineweaver-Burk format. The slope of this plot will be5. For a Michaelis-Menten enzyme, k1 = 5.2 ⅹ 108 M-1 s-1, k-1 = 3.1 ⅹ 104 s-1, and k2 = 3.4 ⅹ 105 s-1. a) Write out the reaction, showing k1, k-1, and k2. Calculate Ks and Km. Does substrate binding approach equilibrium or the steady state? Justify your answer. b) What is kcat for this reaction? Justify your answer. c) Calculate Vmax for the enzyme. The total enzyme concentration is 25 pmol L-1, and each enzyme has two active sites. d) What substrate concentration would be required for the reaction in (c) to reach half of Vmax. Justify your answer mathematically. e) A second Michaelis-Menten enzyme has k1 = 4.2 ⅹ 107 M-1 s-1, k-1 = 6.1 ⅹ 104 s-1, and k2 = 5.3 ⅹ 102 s-1. Which enzyme is most efficient? 6. A pharmaceutical company is trying to develop aSubstrate KM (M) N-Acetylvaline ethyl ether 8.8 X 10 -2 N-Acetyltyrosine ethyl ether 6.6 X 10-4 Which substrate has the higher apparent affinity for the enzyme? Explain. Which substrate is likely to give a higher value for Vmax?