In biological systems, enzymes are used to accelerate the rates of certain bio-logical reactions. Glucoamylase is an enzyme that aids in the conversion of starchto glucose (a sugar that cells use for energy). Experiments show that 1 pg mol ofglucoamylase in a 4% starch solution results in a production rate of glucose of 0.6ug mol/(mL)(min). Determine the production rate of glucose for this system in theunits of Ib mol/(ft³)(day).IbmolAnswer: 0.0639ft dayTrueFalse

Glucoamylase catalyzes the hydrolysis of alpha-glycosidic linkages to form glucose. Production rate…

Answered: In biological systems, enzymes are used…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Interested in studying ethanol fermentation, you prepare two solutions of yeast extract that contains the cytosolic contents of Saccharomyces cerevisiae. You add glucose to both extracts at time zero, but to one (in red) you also add inorganic phosphate (added in two batches). Using a gas sensor, you monitor the CO2 generated by the two solutions over time and obtain the following data:
We want to measure the activity of alanine aminotransferase (ALAT) present in a serum. The reaction catalyzed by the enzyme is: Reaction 1: I- *H₂N- glutamate H - C-COO CH₂ CH₂ COO 0.1 M phosphate buffer pH 7.4 : 550 μL 1.2 M alanine: 100 μL CH3 pyruvate CH3 C time (min) A340 CIO O COO The enzyme reaction is alized in the following conditions: In a 1 cm-cuvette are added: COO™ pyruvate lactate dehydrogenase* (LDH, 300 µμg.mL-¹): 50 μL 1.5 mM NADH : 200 μL 0.04 M a-ketoglutarate: 500 µL serum containing ALAT: 600 μµL ALAT NADH + H+ 0 0.915 a-cétoglutarate COO LDH * Lactate dehydrogenase (LDH) reduces pyruvate into lactate, with the concomitant oxydation of NADH. This allows to indirectly measure the amount of product formed. с=0 CH₂ 1 0.741 Reaction 2: NAD+ CH₂ COO™ H-C CH3 OH COO™ lactate alanine H + *H3N-C The reaction is performed at 25 °C and the absorbance at 340 nm is monitored every minute, for 5 min. The absorbance values are given in the table below: Data: ENADH at 340 nm =…
The Nutrition Facts label on most food products shows % daily values based on a food energy requirement of 8,360 kJ (2,000 kcal) at normal resting state. a) Assuming that the efficiency of converting food energy to ATP is 50%, calculate the mass of ATP (in kg) that is harvested daily by the human body from 8,360 kJ of food energy. A total of 30.5 kJ of energy is needed to synthesize one mole of ATP under standard conditions. The molar mass of ATP is 505 g/mol. b) For an average 68-kg (150 lbs.) human adult, calculate the % mass of extracted ATP (from your answer in 2a) relative to body weight.
Phosphoglycerate-mutase catalyses the isomerization of 3-phospho-glycerate to 2-phospho-glycerate. The enzyme has a molecular weight of 28,556 g/mol. In assays using 1 milligram of enzyme per assay the Km for 3-phosphoglycerate was 1.2 x 10^-3M and the Vmax was 840 μmole min^-1. What would be the Vmax in units of mole s^-1?
Twenty-three milligrams of glucose were eaten by the bacteria Sanacoccus pumasareus. Calculate the hypothetical amount of ATP your patient can generate under aerobic respiration with this amount of glucose. (Note: Glucose MW-180.16 g/mole; 1 mole= 6.02 x 1023 molecules (Avogadro's number)). 2.8 x 10^24 ATPs 02.9 x 10^21 ATPs 028 x 10-21 ATP5 029 x 10 24 ATPS Lacks information, cannot be determined
The process of protein decomposition by pepsin enzymes in stomach is assumed and modeled as a batch reactor. If the protein concentration over time is measured as follows: Write the relationship between time (t), protein concentration (CA). Assuming that the enzyme reaction follows Michaelis-Menten kinetics, write the required constant (Vmax, Km), and the initial concentration of the protein is CA0.
As a result of an experiment following measurements were obtained from a cell: ATP concentration of 0.5 mM, ADP concentration of 0.1 mM, inorganic phosphate (Pi) concentration of 2 mM. Under these conditions calculate the actual free energy (AG) of the reaction of hydrolysis of ATP to ADP and Pi. (The standard energy (AG°) of ATP = -31 kJ/mol; RT = 2,58 kJ/mol) Select one: O a. -28 kJ/mol O b. -33 kJ/mol OC. -19 kJ/mol O d. -42 kJ/mol
what is the Vmax and Km of the enzyme in the reaction asap please.
The lipase substrate emulsion contains 0.500 mg of olive oil per 3 mL Also, the molar mass of the olive oil is 885 g/mol. If all of the olive oil in a 3 mL reaction is "digested" by pancreatic lipase in a reaction, how many molecules of olive oil have been degraded?
Angiotensin Converting Enzyme (ACE) inhibitors cause blood vessels to relax, thereby reducing blood pressure. Although Captopril is part of the group of antihypertensive drugs widely used as ACE inhibitors, new research is constantly being carried out with the aim of selecting compounds that are more kinetically advantageous than Captopril. Therefore, a BioPharma employee selected some prototypes and performed kinetic tests, finding the result shown in the figure below. Based on the statement and the graphic above, mark the incorrect alternative. A) It is a graph for determining kinetic parameters according to Lineweaver-Burk. In that case, the coefficient a B) Comparing the prototypes with the reference drug, Prototype 1 has a higher Vmax value. C) Comparing the prototypes with the reference drug, Prototype 2 has a lower Vmax value. D) Captopril has a Vmax of approximately 0.730 and Km of approximately 0.669. E) The two prototypes have Km values lower than those of Captopril and,…
This is the kcat question. At maximum saturation, 28.3µg of enzyme in 25mL water catalyzes the oxidation of ethanol at a rate of 2.5mM/min. Calculate kcat in units of seconds if the enzyme has a molar mass of 65kg/mol. The more correct work you show, the more credit you will get.

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