Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
expand_more
expand_more
format_list_bulleted
Question
Chapter 22, Problem 18P
Interpretation Introduction
To determine:
What happened to 2 and 4 carbons of glucose-6-phosphate in pentose phosphate pathway.
Introduction:
2 and 4 carbons of glucose-6-phosphate converts in to 1 and 3 carbons in pyruvate.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
Make an electron-flow-mechanism for this synthetic scheme. This involves predicting major and by-products using electronic and structural effects. The arrow push mechanism must be shown.(from the reaction of α-ketoacids and oxaprolines to proteins that contain native serine residues ) with label
7.
. Pyruvate can be processed under anaerobic conditions to ethanol (in yeast) or to lactate (in
mammals), as shown.
Explain the primary purpose of these reactions.
Describe the major biochemical features of each reaction
Chapter 22 Solutions
Biochemistry
Ch. 22 - Prob. 1PCh. 22 - Prob. 2PCh. 22 - Prob. 3PCh. 22 - Prob. 4PCh. 22 - Prob. 5PCh. 22 - Prob. 6PCh. 22 - Prob. 7PCh. 22 - Prob. 8PCh. 22 - Prob. 9PCh. 22 - Understanding Enzyme Mechanisms Related to...
Ch. 22 - Understanding the Mechanisms of Reactions Related...Ch. 22 - Prob. 12PCh. 22 - Prob. 13PCh. 22 - Prob. 14PCh. 22 - Prob. 15PCh. 22 - Prob. 16PCh. 22 - Prob. 17PCh. 22 - Prob. 18PCh. 22 - Prob. 19PCh. 22 - Prob. 20PCh. 22 - Prob. 21PCh. 22 - Prob. 22PCh. 22 - Using the ActiveModel for aldose reductase,...
Knowledge Booster
Similar questions
- MATHEMATICAL What yield of ATP can be expected from complete oxidation of each of the following substrates by the reactions of glycolysis, the citric acid cycle, and oxidative phosphorylation? (a) Fructose-1,6-bisphosphate (b) Glucose (c) Phosphoenolpyruvate (d) Glyceraldehyde-3-phosphate (e) NADH (f) Pyruvatearrow_forwardUsing the ActiveModel for aldose reductase, describe the structure of the TIM barrel motif and the structure and location of the active site.arrow_forwardRegulation of Glutamine Synthetase by Covalent Modification Suppose at certain specific metabolite concentrations in vivo the cyclic cascade regulating E. coli glutamine synthetase has reached a dynamic equilibrium where the average state of GS adenylylation is poised atn=6. Predict what change in nwill occur if: [ ATP ] increases, PIIA/PIID increases, [ -KG ]/[ Gln ] increases, [ Pi ] decreases.arrow_forward
- Understanding Enzyme Mechanisms Related to Pyruvate Carboxylase Based on the mechanism for pyruvate carboxylase (Figure 22.3), write reasonable mechanisms for the reactions that follow:arrow_forwardChemical labeling of chymotrypsin by the compound tosylphenylalanine chloromethyl ketone (TPCK) modifies the His 57 in the enzyme's active site. The structure of this derivative is shown below. TPCK inactivates the enzyme because the bulky addition prevents it from cleaving nearby covalent bonds. HCI + CH, C-O Chymotrypsin-His 57 TPCK Modified enzyme True O Falsearrow_forwardPlease help!arrow_forward
- H. OH co co2 но H co, 1-isopropylmalate 2-isopropylmalate Biosynthesis of leucine involves conversion of 1-isopropyimalate to 2-isopropylmalate (see above). This proceeds in four steps under basic enzymic catalysis via an isolable compound produced in step 2. Write a detailed mechanism for this conversion. Then, draw the intermediate compound) produced in step 2. • You do not have to consider stereochemistry. • Draw uninvolved carboxyl groups in the anionic state, and enolates as carbanions. When needed, abbreviate CoenzymeA-S- as CH3S- In your drawing. aalearrow_forwardPls help due asaparrow_forwardPredict the effect of each of the following amino acid substitutions on the KM and kcat of the enzyme-catalyzed reactionsarrow_forward
- M-CSA Mechanism and Catalytic Site Atlas (ebi.ac.uk) (ii) Acyl Carrier Protein S-acetyltransferase (EC 2.3.1.38) is a transferase enzyme that catalyzes the first biosynthetic pathway for fatty acid synthase. It transfers the acyl group (CH3CO) first from coenzyme A to a cysteine residue in the active site. This is similar to what happens in Chymotrypsin, however utilizing a sulfur instead of an oxygen. The acyl group is then transferred to the molecule ACP. Provide the enzyme- catalyzed mechanism for the reaction below, making sure to identify the roles of all key amino acids: i H3C SCOA acetyl COA enzyme + HS i H3C SACP acetyl ACParrow_forwardI only need aarrow_forwardThe conversion of glucose-6-phosphate to fructose-6-phosphate in the glycolytic pathway (Choose all that apply) O positions a carbonyl group on carbon 2 of fructose-1-phosphate O positions an amino group NH2 on carbon 3 of fructose-1-phosphate O positions a carbonyl group on carbon 3 of fructose-1-phosphate O is an aldose-keto isomerization O positions a primary alcohol function at carbon C-1 that facilitates phosphorylation of fructose-6-phosphate O is a keto-aldose isomerization O positions an amino group NH2 on carbon 2 of fructose-1-phosphatearrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
- BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage LearningBiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305961135
Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:Cengage Learning