Concept explainers
To determine: The reaction of the IMP
Concept introduction: Synthesis of purine yields inosine monophosphate (IMP). IMP is a precursor of adenosine monophosphate (AMP). The urea cycle is important to remove the amino group from the body.

Explanation of Solution
Explanation:
The reaction in which aspartate is added to the IMP and adenylosuccinate lyase take away fumarate by leaving the amino group. Urea is synthesized in the liver by urea cycle. The urea is secreted into the blood stream and after the filtration in kidney it excretes in the urine. In the urea cycle, after addition of aspartate to the citrulline, argininosuccinase take away fumarate by leaving an amino group. Therefore, the reaction catalyzed by adenylosuccinate lyase in IMP
Want to see more full solutions like this?
Chapter 23 Solutions
FUNDAMENTALS OF BIOCHEM.-NEXTGEN ACCESS
- 1. Conceptual questions a. What dimensionless group describes the relative importance of convection versus diffusion. Explain the physical basis of this group. b. For mass transfer from a flowing fluid to a reactive surface, explain how convection increases the flux of solute to the surface.arrow_forwardAssessment +1501 pts /1600 Resources Solution ? Hint Sub bo Each pictured Lewis structure is invalid. Identify the error in each case. O Macmillan Learning :0▬▬0: Answer Bank wrong electron total :0- :F======F: octet-rule violation N :0:arrow_forward[s] mM V (M/s) Uninhibited 0.333 1.65 x 107 1.05 x 107 V (M/s) x 10' Inhibitor A V (M/s) x 107 Inhibitor B 0.794 x 107 0.40 1.86 x 107 1.21 x 107 0.893 x 107 0.50 2.13 x 107 1.43 x 107 1.02 x 107 0.666 2.49 x 107 1.74 x 107 1.19 x 107 1.0 2.99 x 107 2.22 x 107 1.43 x 107 2.0 3.72 x 107 3.08 x 107 1.79 x 107arrow_forward
- For a Michaelis-Menten reaction, k₁-5 x 10'/M-s, k.-2 x 10%/s, and k₂-4 x 10²/s. a) Calculate the Ks and KM for this reaction. b) Does substrate binding achieve equilibrium or steady state?arrow_forwardAssume that an enzyme-catalyzed reaction follows the scheme shown: E+S SES →E + P k₁ = 1 x 109/M-s k-1=2.5 x 10%/s k₂ = 3.4 x 107/s What is the dissociation constant for the enzyme-substrate, K,? What is the Michaelis constant, Km, for this enzyme? What is the turnover number, Keat, for this enzyme? What is the catalytic efficiency for the enzyme? If the initial Et concentration is 0.25mM, what is Vmax?arrow_forwardAn enzyme lowers the activation energy, (AG) of a reaction from 50.0 kcal/mol to 40.0 kcal/mol. Calulate the catalytic power at 310K. (R-1.987x10 kcal/mol)arrow_forward
- Draw a typical axodendritic synapse, including a specific neurotransmitter of your choice, its associated postsynaptic receptors (indicating whether they are ionotropic or metabotropic), and any associated reuptake transporters or degradation enzymes. Please include a description of what specific steps would occur as an action potential reaches the axonal terminal.arrow_forwardGive a full arrow pushing mechanism of the spontaneous redox reaction between NAD+/NADH and oxaloacetate/malate. Please include diagram drawing of the mechanism! (Thank You!)arrow_forward18. Which one of the compounds below is the major organic product obtained from the following series of reactions? 1. BH3 2. H2O2, NaOH H₂CrO4 CH2N2 oro ororos A B C D Earrow_forward
- 17. Which one of the compounds below is the major organic product obtained from the following series of reactions? CI benzyl alcohol OH PBr3 Mg 1. CO2 SOCl2 ? ether 2. H+, H₂O CI Cl HO OH CI Cl A B C D Earrow_forward14. What is the IUPAC name of this compound? A) 6-hydroxy-4-oxohexanenitrile B) 5-cyano-3-oxo-1-pentanol C) 5-cyano-1-hydroxy-3-pentanone D) 1-cyano-5-hydroxy-3-pentanone E) 5-hydroxy-3-oxopentanenitrile HO. CNarrow_forward13. What is the IUPAC name of this compound? A) 5-hydroxy-3,3-dimethylpentanoic acid B) 3,3-dimethylpentanoic acid C) 3,3-dimethyl-1-oxo-1,5-pentanediol D) 1,5-dihydroxy-3,3-dimethylpentanal E) 4-hydroxy-2,2-dimethylbutanoic acid HO OHarrow_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





