(a)
To determine: The equilibrium constant for the reaction for formation of glucose 6-phosphate at 37°C and whether this reaction is a reasonable
Introduction:
The glycolysis is a series of reactions converting the glucose molecules into two molecules of pyruvate in the presence of oxygen. The pyruvate undergoes series of reactions in the citric acid cycle and converts into acetyl CoA (acetyl coenzyme A).
(a)

Explanation of Solution
The reaction for the formation of glucose-6-phosphate by reaction of inorganic phosphate and glucose is as follows:
The value of gas constant R is 0.0083 kJ/ mole K. The equilibrium constant at the given temperature 37°C (310 K) is calculated as follows-
The value of equilibrium constant of glucose-6-phosphate is determined as follows:
The given reaction will not be favorable based on the levels of glucose in a cell, as it will exceed the concentration of
(b)
To determine: Whether the route is physiologically reasonable when the maximum solubility of glucose is less than 1M.
Introduction:
The glycolysis is a series of reactions converting the glucose molecules into two molecules of pyruvate in the presence of oxygen. The pyruvate undergoes series of reactions in the citric acid cycle and converts into acetyl CoA (acetyl coenzyme A).
(b)

Explanation of Solution
The value of equilibrium constant is also determined as follows:
This route will be unfavorable because the given concentration of glucose exceeds the permissible limit of 1M. The concentration of glucose at given conditions is 11 M and the reaction will not be physiologically feasible because the maximum limit is exceeded by given concentration of glucose.
(c1)
To determine: The
Introduction:
The glycolysis is a series of reactions converting the glucose molecules into two molecules of pyruvate in the presence of oxygen. The pyruvate undergoes series of reactions in the citric acid cycle and converts into acetyl CoA (acetyl coenzyme A).
(c1)

Explanation of Solution
The two given
The value of gas constant R is 0.0083 kJ/ mole K. The equilibrium constant at the given temperature 37°C (310 K) is calculated as follows-
The
(c2)
To determine: The concentration of glucose needed to achieve 250 mM intracellular concentration of glucose-6-phosphate when the concentrations of ATP and ADP are 3.3 mM and 1.32 mM.
Introduction:
The glycolysis is the process of series of reactions converting the glucose molecules into two molecules of pyruvate in the presence of oxygen. The pyruvate undergoes series of reactions in the citric acid cycle and converts into Acetyl CoA (acetyl coenzyme A).
(c2)

Explanation of Solution
The value of equilibrium constant is determined as follows:
The concentration of glucose needed is
(c3)
To discuss: Whether this coupling process provides feasible route at least in principle for phosphorylation of glucose in the cell.
Introduction:
The glycolysis is the process of series of reactions converting the glucose molecules into two molecules of pyruvate in the presence of oxygen. The pyruvate undergoes series of reactions in the citric acid cycle and converts into Acetyl CoA (acetyl coenzyme A).
(c3)

Explanation of Solution
This route will be favorable because the given concentration of glucose does not exceed the permissible limit of 1 M. The coupling process will be feasible for given route for phosphorylation of glucose in the cell.
(d)
To determine: Whether the route is reasonable given that the coupling requires a common intermediate, the route uses ATP hydrolysis to raise the intracellular concentration of Pi.
Introduction:
The glycolysis is a series of reactions converting the glucose molecules into two molecules of pyruvate in the presence of oxygen. The pyruvate undergoes series of reactions in the citric acid cycle and converts into acetyl CoA (acetyl coenzyme A).
(d)

Explanation of Solution
The high levels of phosphates are needed for the precipitation of divalent cations of phosphate salts under normal physiological conditions, and thus, the condition will not be possible. Therefore, the given route is not reasonable for the requirement of common intermediate in coupling.
(e)
To determine: The advantages of route of transfer of phosphate group by ATP to glucose by enzyme glucokinase.
Introduction:
The glycolysis is a series of reactions converting the glucose molecules into two molecules of pyruvate in the presence of oxygen. The pyruvate undergoes series of reactions in the citric acid cycle and converts into acetyl CoA (acetyl coenzyme A).
(e)

Explanation of Solution
This reaction of transfer of phosphate group to glucose by ATP is catalyzed by glucokinase. The phosphate group is transferred and the potential of ATP is used and generation of high levels of intermediate molecules is not required. The reaction is catalyzed by glucokinase and no intermediates are formed by utilization of potential of ATP.
Want to see more full solutions like this?
Chapter 13 Solutions
Lehninger Principles of Biochemistry (Instructor's)
- Sodium fluoroacetate (FCH 2CO2Na) is a very toxic molecule that is used as rodentpoison. It is converted enzymatically to fluoroacetyl-CoA and is utilized by citratesynthase to generate (2R,3S)-fluorocitrate. The release of this product is a potentinhibitor of the next enzyme in the TCA cycle. Show the mechanism for theproduction of fluorocitrate and explain how this molecule acts as a competitiveinhibitor. Predict the effect on the concentrations of TCA intermediates.arrow_forwardIndicate for the reactions below which type of enzyme and cofactor(s) (if any) wouldbe required to catalyze each reaction shown. 1) Fru-6-P + Ery-4-P <--> GAP + Sed-7-P2) Fru-6-P + Pi <--> Fru-1,6-BP + H2O3) GTP + ADP <--> GDP + ATP4) Sed-7-P + GAP <--> Rib-5-P + Xyl-5-P5) Oxaloacetate + GTP ---> PEP + GDP + CO 26) DHAP + Ery-4-P <--> Sed-1,7-BP + H 2O7) Pyruvate + ATP + HCO3- ---> Oxaloacetate + ADP + Piarrow_forwardTPP is also utilized in transketolase reactions in the PPP. Give a mechanism for theTPP-dependent reaction between Xylulose-5-phosphate and Ribose-5-Phosphate toyield Glyceraldehyde-3-phosphate and Sedoheptulose-7-Phosphate.arrow_forward
- What is the difference between a ‘synthetase’ and a ‘synthase’?arrow_forwardIn three separate experiments, pyruvate labeled with 13C at C-1, C-2, or C-3 is introduced to cells undergoing active metabolism. Trace the fate of each carbon through the TCA cycle and show when each of these carbons produces 13CO2.a. Glucose is similarly labeled at C-2 with 13C. During which reaction will this labeled carbon be released as 13CO2?arrow_forwardDraw the Krebs Cycle and show the entry points for the amino acids Alanine,Glutamic Acid, Asparagine, and Valine into the Krebs Cycle. How many rounds of Krebs will be required to waste all Carbons of Glutamic Acidas CO2?arrow_forward
- Suppose the data below are obtained for an enzyme catalyzed reaction with and without the inhibitor I. (s)( mM) 0.2 0.4 0.8 1.0 2.0 4.0 V without i (mM/min) 5.0 7.5 10.0 10.7 12.5 13.6 V with I (mM/min) 3.0 5.0 7.5 8.3 10.7 12.5 Make a Lineweaver Burke plot for this data using graph paper or a spreadsheet Calculate KM and Vmax without inhibitor. What type of inhibition is observed? show graph and work 2. Give the Lineweaver Burk equation and define all the parameters. 3. When substrate concentration is much greater than Km, the rate of catalysis is almost equal to a. kcat b. none of these c. all of these d. Kd e. Vmaxarrow_forwardPlease explain the process of how an axon degenerates in the central nervous system following injury and how it affects the neuron/cell body, as well as presynaptic and postsynaptic neurons. Explain processes such as chromatolysis and how neurotrophin signaling works.arrow_forwardPlease help determine the Relative Response Ratio of my GC-MS laboratory: Laboratory: Alcohol Content in Hand Sanditizers Internal Standard: Butanol Standards of Alcohols: Methanol, Ethanol, Isopropyl, n-Propanol, Butanol Recorded Retention Times: 0.645, 0.692, 0.737, 0.853, 0.977 Formula: [ (Aanalyte / Canalyte) / (AIS / CIS) ]arrow_forward
- Please help determine the Relative Response Ratio of my GC-MS laboratory: Laboratory: Alcohol Content in Hand Sanditizers Internal Standard: Butanol Standards of Alcohols: Methanol, Ethanol, Isopropyl, n-Propanol, Butanol Recorded Retention Times: 0.645, 0.692, 0.737, 0.853, 0.977 Formula: [ (Aanalyte / Canalyte) / (AIS / CIS) ]arrow_forwardplease draw it for me and tell me where i need to modify the structurearrow_forwardPlease help determine the standard curve for my Kinase Activity in Excel Spreadsheet. Link: https://mnscu-my.sharepoint.com/personal/vi2163ss_go_minnstate_edu/_layouts/15/Doc.aspx?sourcedoc=%7B958f5aee-aabd-45d7-9f7e-380002892ee0%7D&action=default&slrid=9b178ea1-b025-8000-6e3f-1cbfb0aaef90&originalPath=aHR0cHM6Ly9tbnNjdS1teS5zaGFyZXBvaW50LmNvbS86eDovZy9wZXJzb25hbC92aTIxNjNzc19nb19taW5uc3RhdGVfZWR1L0VlNWFqNVc5cXRkRm4zNDRBQUtKTHVBQldtcEtWSUdNVmtJMkoxQzl3dmtPVlE_cnRpbWU9eEE2X291ZHIzVWc&CID=e2126631-9922-4cc5-b5d3-54c7007a756f&_SRM=0:G:93 Determine the amount of VRK1 is present 1. Average the data and calculate the mean absorbance for each concentration/dilution (Please over look for Corrections) 2. Blank Correction à Subtract 0 ug/mL blank absorbance from all readings (Please over look for Corrections) 3. Plot the Standard Curve (Please over look for Corrections) 4. Convert VRK1 concentration from ug/mL to g/L 5. Use the molar mass of VRK1 to convert to M and uM…arrow_forward
- BiochemistryBiochemistryISBN:9781319114671Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.Publisher:W. H. FreemanLehninger Principles of BiochemistryBiochemistryISBN:9781464126116Author:David L. Nelson, Michael M. CoxPublisher:W. H. FreemanFundamentals of Biochemistry: Life at the Molecul...BiochemistryISBN:9781118918401Author:Donald Voet, Judith G. Voet, Charlotte W. PrattPublisher:WILEY
- BiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage LearningBiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage LearningFundamentals of General, Organic, and Biological ...BiochemistryISBN:9780134015187Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. PetersonPublisher:PEARSON





