1/Vo 1/[S] with I without I d. with I with 1/vo without I 1/[S] 1/vo without I 1/[S] 3. The above graphs are lineweaver-burk plots that demonstrate how inhibitors affect Michaelis Menten enzymes. For each graph identify the type of inhibition and explain how you determined that this enzyme is kinetically demonstrating this type of inhibition.
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- Describe type I, II, and III L-asparaginases. Mention characteristics and differences between them with respect to enzyme kinetics (rate, km, etc).Match the following Not describe.A schematic representation of the enzyme IspD complexed to inhibitor 3, and a series of inhibitors 3-5 are shown below. Ala202 lle240 mwww NH NH Val263 ОН www HN N- lle177 HN 'N' CI 3 X = N 4 X = C-CN 5 X = C-COO IC50 274 µM IC50 140 nM IC50 35 nM NH2 HN Val266 N -N O-H---- N HN %3D Arg157 HN wwww lle265 Explain why structure 4 is a more potent inhibitor (lower IC50 value) than inhibitor 3 and why structure 5 is a much weaker inhibitor (higher IC50 value) than 3 and 4.
- Latrotoxin identify the species which releases the toxin (if it is man-made then this will be all that is required for this part) identify the step disrupted in the neuromuscular junction pathway Provide any consequences of this disruption. Does the toxin have any applications in biomedicine as a painkiller, disease treatment or analgesic? Provide your source in APA format for each. If this is missing no credit will be awarded.Drag the terms on the left to the appropriate blanks on the right to complete the sentences. Terms can be used once, more than once, or not at all. Submit dCTP GMP AMP GTP dTTP activation inhibition dGTP My Answers Give Up UTP + Gln + ATP → CTP + Glu+ ADP + P₁. Cofactor: dCMP + H₂O →→→→DUMP + NH3. Cofactor: CDP+ [2H] → dCDP+ H₂O. Cofactor: Effect: Effect: Effect: Reset Helpdiagram of the chain of infection for COVID-19
- What step ends the first-half of the chymotrypsin mechanism? Attack of water on the acyl-enzyme intermediate. Selected Collapse of the first tetrahedral intermediate, releasing of the C-terminal peptide fragment and formation of the acyl-enzyme intermediate. Deprotonation of serine by the histidine. Collapse of the second tetrahedral intermediate leading to the final products. REVIEW QUESTION 1/1 CONTINUE MacBook Pro https://virginiacommonwealth.instructure.com/courses/42082/assignments/271397 esc OTBotulinum Toxin identify the species which releases the toxin (if it is man-made then this will be all that is required for this part) identify the step disrupted in the neuromuscular junction pathway Provide any consequences of this disruption. Does the toxin have any applications in biomedicine as a painkiller, disease treatment or analgesic? Provide your source in APA format for each. If this is missing no credit will be awarded.A. 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)
- what possible outcome may be produced when the molecular weight of an alcohol antiseptic is increase to a C20, will it still be effective? Explain your answerThe steps of the chymotrypsin mechanisms are listed below (1-7). Put the steps of chymotrypsin mechanism in the correct order. Figure representing chymotrypsin mechanism is given for reference. a.The portion (N-terminal end) of original substrate with the new C terminus diffuses away b. Substrate binding c. His 57 catalyzes removal of H from Ser 195 hydroxyl; Ser 195’s nucleophilic O attacks carbonyl C of substrate; tetrahedral intermediate is formed d. Water binding; water is deprotonated by His 57; resulting OH nucleophilically attacks carbonyl of remaining substrate; tetrahedral intermediate is formed e. His 57 donates H to N of…The graphs 3 and 4 representing 1/Vo = f(1/[S]o) have been done in the presence of a competitive (CI) and noncompetitive inhibitor (NCI). a- For each figure, determine from the relative position of the straight lines which one is obtained in presence of an inhibitor. b- Indicate which graph corresponds to the competitive inhibition and which one the noncompetitive inhibition. Justify your answer. c- Complete the graphs by indicating which values can be determined from the arrows. 3 1/No 1/[S]⁰ (4) 1/No 1/[S]o