commercial value associatiatef with glutamate Dehydrogenase? Propose your own ideas!
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- Examine the ActiveModel for alcohol dehydrogenase and describe the structure and function of the catalytic zinc center.Using the acromyn LILHOT give the 6 major families of enzymes found in biological systems. Describe the enzymatic activity of the "I" in LILHOTWhat is the catalytic efficiency of Catalase ? Table. The values of KM and kcat for some Enzymes and Substrates Enzyme Carbonic anhydrase Substrate CO2 HCO3 KM (M) 1.2 x 10-2 2.6 x 10-2 Kcat (s-1) 1.0 x 106 4.0 x 105 Catalase H2O2 2.5 x 10-2 1.0 x 107 Urease Urea 2.5 x 10-2 4.0 x 105 O A. 4 x 108 M-s-1 O B. 4 x 108 M-1.s-1 OC25x 10-9 M-s1 D. 2.5 x 102 M-1.s-1 OE 1.0 x 107 s1
- Write the inhibitors of- · glycolysis . electron transport chainhow much atp is generated from the complete B-oxidation of one molecule of tristearin? Show your solutions neat and organized.2:31 The molecule shown below is? H,C -o HC -o H,C -o O glucose O cholesterol O none is correct O adenine O phospholipid
- Suggest a simple method to determine whether a reaction is being inhibited by a competitive or non-competitive inhibitorGive some options choose the structure of coenzyme that is not derived from a vitamin and provide the name of enzyme to which the coenzyme belongs in the pyruvate dehydrogenase complex? Give explained answerSuggest a simple method to determine whether a reaction is being inhibited bu a competitive or non-competitive inhibitor
- Sketch out the schematic diagram for the enzymatic mechanism of pyruvate dehydrogenase complex Please provide the structure of the functional groups of the substrate and enzyme involved in the reaction at each step (rest of the structure can be indicated as R) Indicate clearly the flow of electrons in the E-1 and E-2 reaction Indicate in short form the cofactor involvedMake tables of reactions of the Glycolysis and Gluconeogenesis with enzyme names and DGo’ values. I provided a template for the table below. With this information, determine the overall free energy of each pathway. Discuss the differences in these values and suggest a reason for this difference. Please answer very soon will give rating surelySuppose that the data below are obtained for an enzyme catalyzed reaction in the presence and absence of inhibitor Y. [S] (mM) V (mmol/mL*min) Without Y With Y 0.2 5.0 2.0 0.4 7.5 3.0 1.8 10.0 4.0 1.0 10.7 4.3 2.0 12.5 5.0 4.0 13.6 5.5 a.) Determine the type of inhibition that has occurred b.) Does inhibitor Y combine with E, with ES or with both? Explain c.) Calculate the inhibitor constant, Ki, for substance Y, assuming that the final concentration of Y in the reaction mixture was 0.3mM