![Fundamentals of General, Organic, and Biological Chemistry, Books a la Carte Edition; Modified Mastering Chemistry with Pearson eText -- ValuePack ... and Biological Chemistry (4th Edition)](https://www.bartleby.com/isbn_cover_images/9780134465715/9780134465715_largeCoverImage.gif)
Concept explainers
Interpretation:
The structure of arginine which is converted to
Concept Introduction:
Arginine:
Arginine is an essential amino acid which is used to prepare the biosynthesis of proteins.it mainly has amino group and
Ornithine:
Ornithine is an amino acid which plays a role in the urea cycle and which is accumulated abnormally in the body.
Glutamate:
The conjugate base of glutamic acid, which is largely present in the human brain
An important biological compound, which is produced from the deamination of glutamate, it acts as an intermediate in Krebs cycle.
![Check Mark](/static/check-mark.png)
Want to see the full answer?
Check out a sample textbook solution![Blurred answer](/static/blurred-answer.jpg)
Chapter 25 Solutions
Fundamentals of General, Organic, and Biological Chemistry, Books a la Carte Edition; Modified Mastering Chemistry with Pearson eText -- ValuePack ... and Biological Chemistry (4th Edition)
- (a) Write a balanced equation for the conversion of aspartate into glucose through the intermediate oxaloacetate. Which coenzymes participate in this transformation? (b) Write a balanced equation for the conversion of aspartate into oxaloacetate through the intermediate fumaratearrow_forwardThe urea cycle can be summarized through the following reaction: O || H2N-C-OPO3 + COO- | H3N-CHCH₂COO b. O || H2N-C-NH2 1a Write the reactions, using structural formulas that lead to the formation of carbamoyl phosphate and its subsequent incorporation into the urea cycle. Name the enzymes and how they are activated. 1 + OOCCH=CHCOO- Write the rest of the reactions that constitute the urea cycle using structural formulas. Name the enzymes that catalyze each reaction. Indicate which reactions occur in the mitochondrion and which occur in the cytoplasm.arrow_forwardHomocystinuria is caused by a defect in cystathionine beta-synthase (or 13-synthase), which leads to an accumulation of homocysteine in the blood. This accumulation causes symptoms such as a tall, thin frame, flushed cheeks, and osteoporosis (thinning of the bones). These individuals should limit their intake of proteins that contain methionine, such as egg whites. Using your understanding of biochemistry, explain why people with Homocystinuria should not consume egg whites and other such proteins.arrow_forward
- If aspartate is labeled with deuterium D (= H-2 = 12H), answer questions a-c to determine where the label will end up in oxaloacetate after the involvement of aspartate in the urea cycle. Where does the label end up in arginosuccinate? Where is the label in fumarate? Where is the label in oxaloacetate?arrow_forwardIn germ-free mice, which harbor no intestinal bacteria, the O-linked oligosaccharides of intestinal glycoproteins tend to lack a terminal fucose residue (see Fig.). (a) What enzyme is not produced in normal quantities in these mice? (b) What monosaccharides tend to appear at the ends of O-linked oligosaccharides in these animals?arrow_forwardWhat is the end product of catabolism of the pyrimidine base thymine? What circumstances cause excess amounts of this end product, and why doesn’t this molecule (unlike uric acid, the end product of purine catabolism) cause a gout-like illness?arrow_forward
- Assume that all carbon atoms and nitrogen atoms in both alanine and aspartate are labelled with radioisotopes. Then, the radioisotope-labelled alanine and aspartate molecules areallowed to undergo metabolism in the liver. All carbon atoms and nitrogen atoms in both ureaand glutamine are found to be labelled with radioisotopes. Please write down the metabolic reactions that lead to the incorporation of radioisotope-labelled carbon and nitrogen atoms into urea and glutamine.arrow_forwardPhosphoglycerate mutase (PGM) catalyzes the interconversion of 3-phosphoglycerate (3PG) and 2-phosphoglycerate (2PG) in the glycolytic and gluconeogenic pathways. a) To what enzyme class does PGM belong? b) There are two distinct classes of PGM, one which is dependent on 2,3-bisphosphoglycerate (2,3-BPG), dPGM, and one which is not, iPGM. dPGM uses acid base chemistry and a phosphorylated histidine residue to interconvert 3PG and 2PG. The dPGM reaction proceeds with formation of 2,3-BPG as an intermediate. Propose a mechanism for the dPGM-catalyzed conversion of 3PG to 2PG that is consistent with this information. c) What is the purpose of 2,3-BPG (i.e., why does dPGM require it)?arrow_forward(a) How many ATP equivalents are consumed by the reactions of the urea cycle? (b) Operation of the urea cycle actually generates more ATP than it consumes. Explain.arrow_forward
- The sucrose substitute tagatose is produced by hydrolyzing lactose and then chemically converting one of the two resulting aldoses to a ketose. Which residue of lactose gives rise to tagatose?arrow_forwardGiven the following statements, identify which are true and which are not. (1) Two ribose subunits are present in the coenzyme flavin adenine dinucleotide. (2) In the common metabolic pathway, 10 molecules of ATP are produced per acetyl CoA catabolized. (3) The purpose of step 2 in the CAC is to convert a secondary alcohol to a tertiary alcohol.arrow_forwardThe allosterically regulated enzyme ATCase binds aspartic acid as a substrate and acylates the α–amino group. Succinate acts as a competitiveinhibitor of ATCase because it binds the active site but can’t be acylated.The dependence of v0 on [aspartic acid] for ATCase is shown in panel (a)of the accompanying figure. Panel (b) shows the effect of increasing [succinate] on v0 when [Asp] is held at a low concentration (see thick vertical arrow in panel (a)). Note that in panel (b), v0 is not zero when [succinate] = 0 (see thin horizontal arrow). Explain the shape of the curve in panel (b). Why does v0 increase initially, before decreasing at higher [succinate]?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
![Text book image](https://www.bartleby.com/isbn_cover_images/9781319114671/9781319114671_smallCoverImage.jpg)
![Text book image](https://www.bartleby.com/isbn_cover_images/9781464126116/9781464126116_smallCoverImage.gif)
![Text book image](https://www.bartleby.com/isbn_cover_images/9781118918401/9781118918401_smallCoverImage.gif)
![Text book image](https://www.bartleby.com/isbn_cover_images/9781305961135/9781305961135_smallCoverImage.gif)
![Text book image](https://www.bartleby.com/isbn_cover_images/9781305577206/9781305577206_smallCoverImage.gif)
![Text book image](https://www.bartleby.com/isbn_cover_images/9780134015187/9780134015187_smallCoverImage.gif)