1.What will be the reaction rate at 0.0550 mM [G6P]? (2)
2. If the enzyme concentration is unchanged, at what G6P concentration will the reaction rate equal 1.650 mM/s? (2)
3. What PGI concentration is required to give a reaction rate of 4.000 mM/s at 0.0300 mM [G6P]? (2)
Calculated Vmax=1.440mM/s Km=0.0330 mM
1.What will be the reaction rate at 0.0550 mM [G6P]? (2) 2. If the enzyme concentration...
1.Which step of glycolysis is catalyzed by phosphoglucose isomerase? What is the chemical “reason” for this reaction in glycolysis? (2) 2. Calculate values of Km and Vmax for PGI. (4) 3. How long (in seconds) does a single catalytic event take? (2) The enzyme phosphoglucose isomerase (PGI) catalyzes the following reaction in glycolysis сH,ОРО,?- Phosphoglucose2-03POH2C сH,он н Н isomerase но Н Н он Н он он но но Н он Н Glucose 6-phosphate Fructose 6-phosphate Kinetics experiments were performed on...
10.What type of inhibitor is this? How do you know? (2) 11.For your assigned inhibitor 1, what are the apparent Km & Vmax? (NOTE: apparent Km& Vmax are just the Km & Vmax in presence of inhibitor, at a given concentration.) (2) Kinetics experiments were performed on PGI. Enzyme activity (initial velocity, Vo) was measured at varying concentrations of Glucose-6-phosphate (G6P). The enzyme concentration used in all experiments was 1.5 μM. 12.What will be the reaction rate with 0.500 mM...
54. What is the catalyze reaction rate? Km=2 mM Kcat= 3 s-1 At the enzyme concentration=10 nM and substrate concentration= 3 mM
Biochemistry. Please answer all completely. 13. Identify the electrophilic center and nucleophile in the below image : R 14. Give an example of amino acids with R group shown below which can function as nucleophile during enzyme catalysis. Nucleophiles Negatively charged oxygen (as in an unprotonated hydroxyl group or an ionized carboxylic acid) Negatively charged sulfhydryl Uncharged amine group HN Imidazole 15. Identify the amino acids with the following side chains and also define if they will work as acid...
Question 1 - Linked Reactions (10 marks) The reaction catalysed by pyruvate kinase is: Phosphoenolpyruvate+ ADPpyruvateATP Keg 3.63 x 105 a) Calculate the AG" for this reaction. Show your working. 3 marks b) The hydrolysis of ATP has following equation: AG 30.5 kJ/mol Calculate the AG" for the following reaction: Phosphoenolpyruvate pyruvateP Show your working. 2 marks c) At 37 °C, the steady-state concentrations of phosphoenolpyruvate, ATP, and ADP have been measured to be 23 HM, 1.85 mM and 140...
Consider the data collected for an enzyme-catalyzed reaction. [S] (MM) 2 (MM :5-1) 0.20 0.86 0.33 1.20 2.00 2.42 4.00 2.69 Determine Vmax and Km for this reaction. mMs-1 Km = mM
What is the major product of the following reaction? 1) BD3, THE 2) NaOH, H2O2 он НО. D A B D ОН он OD ОА B EIO 20 What is the major product of the following reaction? Etон only B Eto OET A D C D A What is/are the major product(s) of the following reaction? Br Н,0 д он ОН он А в only с D Ос A What is the major product of the following reaction? HBr ROOR...
1) The rate constant for the reaction 2 N,Os(9) = 4 NO (9) + O2(9) is reported in units of sl. What is the overall order of the reaction? 2) The rate law for a reaction was reported as rate=k[A] [B][C] with molar concentrations in moles per cubic decimetre and time in seconds. What are the units of k? 3) The rate constant for the pseudo first-order acid- catalysed hydrolysis of glucose is 4.07' 10-s. Calculate the half-life for the...
1. According to the paper, what does lactate dehydrogenase (LDH) do and what does it allow to happen within the myofiber? (5 points) 2. According to the paper, what is the major disadvantage of relying on glycolysis during high-intensity exercise? (5 points) 3. Using Figure 1 in the paper, briefly describe the different sources of ATP production at 50% versus 90% AND explain whether you believe this depiction of ATP production applies to a Type IIX myofiber in a human....