Concept explainers
Interpretation: The function of aspartate transcarbamoylase is to be stated.
Concept introduction: Enzymes being the catalysts increase the
Answer to Problem 1P
The function of aspartate transcarbamoylase is to convert aspartate and carbamoyl phosphate into the compound, N-carbamoylaspartate and inorganic phosphate.
Explanation of Solution
The enzyme, aspartate transcarbamoylase contains two polypeptides which are having different roles. The first polypeptide chain works as a catalytic subunit that helps in carrying the amino acid carbamylation. The second polypeptide chain works as a regulatory subunit. This second polypeptide possesses regulatory sites.
Thus, the enzyme, aspartate transcarbamoylase helps in the condensation of aspartate and carbamoyl phosphate into the compound, N-carbamoylaspartateand also into the inorganic phosphate.
Want to see more full solutions like this?
Chapter 10 Solutions
Biochemistry
- Using a biochemical map and text describe the process by which lactate is recycled from the muscle to liver for gluconeogenesis during high intensity exercise (e.g. a soccer match).arrow_forwardwhat is lactose intolerance ? describe the molecular life cycle for this disease. also describe how it occurs in a molecular level detailed mechanism. what causes this disease and how it develops ? provide detailed biochemical phenomena and life cycle for Lactose Intolerance condition.arrow_forwardSerine protease enzyme mutation To show differences in the effect of the nucleophilic attack of the carbonyl group (C=O) of peptide bond between the catalytic triad of serine, histidine and aspartic acid, and another catalytic triad contains alanine, histidine and aspartic acid Provide/ draw an example of catalytic mechanism with catalytic triad contains alanine, histidine and aspartic Please answer completely will give rating surelyarrow_forward
- elearn.squ.edu.om/mod/qui ystem (Academic) The enzyme asparaginase is used to reduce the level of asparagine in blood in the treatment of leukemia. Which of the following forms of Asparaginase would be most useful if the blood asparagine level is 0.2 mM? Select one: O a. Km = 2.0 mM; Vmax = 0.1 mM/hour O b. Km = 0.1 mM; Vmax = 0.5 mM/hour %3D О с. Кm 0.2 mM; Vmax = 0.1 mM/hour O d. Km = 0.1 mM; Vmax = 0.1 mM/hour O e. Km = 0.2 mM; Vmax = 0.5 mM/hour Clear my choice In a steady state (of ES formation and ES breakdown) Select one: a The rate of formation of ES is equal to the rate of its degradation during the reactionarrow_forwardHelp please. This question is specifically asking for the identification of the biomolecules that are attached to the sphingosine core, then we need to answer what bond causes those biomolecules to be connected to the sphingosine, what reaction created that bond (maybe addition or oxidation etc.), what were the starting materials and lastly what reagents or conditions are needed for the reaction to occur. Thank you!arrow_forwardany biochemistry expect. please help, it's my last attempt..arrow_forward
- Required partner. Aminotransferases require which of the following cofactors: a. NAD+/NADP+NAD+/NADP+ b. Pyridoxal phosphate c. Thiamine pyrophosphate d. Biopterinarrow_forwardENZYME KINETICS ANALYSIS of 6 Xanthine oxidase (XO) is the enzyme that catalyzes the synthesis of uric acid, which in excess causes gouty arthritis. The inhibition of this enzyme is therefore critical in its treatment. A student researcher is investigating the inhibitory effects of kaempferol (Kmp) and chlorogenic acid (Cha) on XO which uses xanthine (Xan) as substrate. Table 1 below shows the enzyme kinetic data. Construct the Lineweaver-Burk plot complete with the linear regression analvsis. Fill in the needed information on Table 2 and paste a copy of your Lineweaver-Burk plot. submit the picture of your output in PNG or JPG format. Table 1. Enzyme Kinetic Data Velocity, mM/s [S], mM Хan Kmp Cha 0.492 0.0678 0.0351 0.0615 0.211 0.0531 0.0261 0.0451 0.087 0.0298 0.0157 0.0211 0.048 0.0195 0.0091 0.0142 0.029 0.0127 0.0067 0.0081 Table 2. Enzyme Kinetic Parameters Xanthine Kaempferol Chlorogenic acid Parameters Vmax Км Type of Inhibition Mode of Binding NA NA Lineweaver-Burk Plotarrow_forwardBIOCHEMISTRY DRAWING. pls accept question only if 100% confident please and thank you. Enalapril is inactive until acted upon by an esterase. Draw the structure of the resulting bioactive derivative. Hintarrow_forward
- Biochemical significance of transamination reactionsarrow_forwardEnteric bacteria .lactic acid, and propionic bacteria have distinctive metabolic traits that can be used to characterized and identify these organisms .Describe the metabolic characteristics of these organisms name a genus that belong to each group, initiated in what way these organisms can be differentiated.arrow_forwardInsulin-dependent diabetes is often accompanied by hypertriglyceridemia, which is an excess blood level of triacylglycerols in the form of very low density lipoproteins. Suggest a biochemical explanation.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