Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
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Textbook Question
Chapter 22, Problem 23P
Using the ActiveModel for aldose reductase, describe the structure of the TIM barrel motif and the structure and location of the active site.
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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,...
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- 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 labelarrow_forwardAmino acid alaninearrow_forwardExplain the biochemical defect that leads to Lesch-Nyhan syndrome and suggest how the defect might cause the behavioral symptoms characteristic of the disorder.arrow_forward
- Examination of the cleavage of the amide substrate, A, by chymotrypsin with the use of stopped-flow kinetic methods reveals no burst. The reaction is monitored by noting the color produced by the release of the amino part of the substrate (highlighted in orange). Why is no burst observed?arrow_forwardConsider the complete oxidation of a mixed TAG containing the following fatty acid residues:At carbon 1: cerotic acidAt carbon 2: heptadecanoic acidAt carbon 3: palmitoleic acid Draw the structure of the mixed TAG.arrow_forwardPhosphopentose isomerase interconverts the aldose ribose 5-phosphate and the ketose ribulose 5-phosphate. Propose a mechanism.arrow_forward
- Glucosidase I catalyzes hydrolysis of specific glucosidase I is a synthetic trisaccharide, glucose-al-2- glucose-al-3-glucose-a-O(CH₂) #COOCH3. Kinetic measurements oligosaccharides containing glucose. obtained using this trisaccharide as substrate in the deoxynorjirimycin at concentrations of 50 μM (), 100 μM absence (x-x) and presence of the inhibitor 1- A) were used to prepare the (-), and 200 μM (4 Lineweaver-Burk plot below: b) Page 3 12) 7. a) V/V (nmol/hr)-1 1.S 1.0- 0.5 1/Trisaccharide (mM)-! Estimate the values for Vmax and KM for the trisaccharide substrate in the absence of the inhibitor. 0.0 -1.0 0.0 One substrate for 1.0 2.0 Determine whether inhibition by 1-deoxynorjirimycin is competitive, non-competitive or neither.arrow_forwardHigh blood levels of triacylglycerides are associated with heart attacks and strokes. Clofibrate, a drug that increases the activity of peroxisomes, is sometimes used to treat patients with such a condition. What is the biochemical basis for this treatment?arrow_forwardThe sedimentation value of aspartate transcarbamoylase decreases when the enzyme switches to the R state. On the basis of the allosteric properties of the enzyme, explain why the sedimentation value decreases.arrow_forward
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