Glucosidase I catalyzes hydrolysis of specificglucosidase I is a synthetic trisaccharide, glucose-al-2-glucose-al-3-glucose-a-O(CH₂) #COOCH3. Kinetic measurementsoligosaccharides containing glucose.obtained using this trisaccharide as substrate in thedeoxynorjirimycin at concentrations of 50 μM (), 100 μMabsence (x-x) and presence of the inhibitor 1-A) were used to prepare the(-), and 200 μM (4Lineweaver-Burk plot below:b)Page 312) 7.a)V/V (nmol/hr)-11.S1.0-0.51/Trisaccharide (mM)-!Estimate the values for Vmax and KM for thetrisaccharide substrate in the absence of theinhibitor.0.0-1.00.0One substrate for1.02.0Determine whether inhibition by 1-deoxynorjirimycin iscompetitive, non-competitive or neither.

Parameters such as Km and vmax are used for comparing enzyme activities. If we know the initial rate…

Answered: Page 3 2) 7. J a) Glucosidase I…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter18: Glycolysis

Section: Chapter Questions

Problem 18P: Distinguishing the Mechanisms of Class I and Class I Aldolases Fructose bisphosphate aldolase in...

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Distinguishing the Mechanisms of Class I and Class I Aldolases Fructose bisphosphate aldolase in animal muscle is a class 1 aldolase, which forms a Schiff base intermediate between substrate (for example. fructose-1, 6-bisphosphate or dihydroxyacetone phosphate) and a lysine at the active site (see Figure I8.12). The chemical evidence for this intermediate conies from studies with aldolase and the reducing agent sodium borohydride, NaBH4. Incubation of the enzyme with dihydroxyacetone phosphate and NaBH4 inactivates the enzyme. Interestingly, no inactivation is observed if NabH4 is added to the enzyme in the absence of substrate. Write a mechanism that explains these observations and provides evidence for the formation of a Schiff base intermediate in the aldolase reaction.
Extending the Mechanism of Methylmalonyl-CoA Mutase to Similar Reactions Based on the mechanism for the methylmalonyl-CoA mutase (see problem 14), write reasonable mechanisms for the following reactions shown.
Galactose 1-phosphate: UDP-glucose uridyltransferase (GALT) is an enzyme important for the catabolism of galactose. Patients with GALT deficiency present within days of birth with feeding difficulty, fatigue, jaundice and liver problems, and failure to thrive. In addition, a buildup of galactose and its metabolites are present in the bloodstream. GALT catalyzes the following reaction in galactose catabolism. NOTE that GALT is reversible!! Classify this enzyme and explain why you classified it in this way.
One treatment for hyperuricemia is administration of xanthine oxidase inhibitors like allopurinol. What is the biochemical rationale for this treatment? Discuss the mechanism and show an illustration how this drug able to alleviate symptoms of hyperuricemia?
Phosphoglycerate-mutase catalyses the isomerization of 3-phospho-glycerate to 2-phospho-glycerate. The enzyme has a molecular weight of 28,556 g/mol. In assays using 1 milligram of enzyme per assay the Km for 3-phosphoglycerate was 1.2 x 10^-3M and the Vmax was 840 μmole min^-1 or 14 x 10^-6 moles s^-1. What would be the approximate value of kcat (turnover number or molecular activity) of the enzyme under these conditions?
Phosphoglycerate-mutase catalyses the isomerization of 3-phospho-glycerate to 2-phospho-glycerate. The enzyme has a molecular weight of 28,556 g/mol. In assays using 1 milligram of enzyme per assay the Km for 3-phosphoglycerate was 1.2 x 10^-3M and the Vmax was 840 μmole min^-1. What would be the Vmax in units of mole s^-1?
Phosphoglycerate-mutase catalyses the isomerization of 3-phospho-glycerate to 2-phospho-glycerate. The enzyme has a molecular weight of 28,556 g/mol. In assays using 1 milligram of enzyme per assay the Km for 3-phosphoglycerate was 1.2 x 10^-3M and the Vmax was 840 μmole min^-1. What would be the approximate value of kcat (turnover number or molecular activity) of the enzyme under these conditions?
at what substrate concentration is v= 5.0 mM s^-1 for the enzyme catalyzed hydrolysis of trehalose?
The clinical symptoms of two forms of galactosemia—deficiency of galactokinase or of UDPglucose: galactose 1-phosphate uridylyltransferase—show radically different severity. Although both types produce gastric discomfort after milk ingestion, deficiency of the transferase also leads to liver, kidney, spleen, and brain dysfunction and eventual death. What products accumulate in the blood and tissues with each type of enzyme deficiency? Estimate the relative toxicities of these products from the above information.
An inhibitor that specifically labels chymotrypsin at histidine 57 is N-tosylamido-l-phenylethyl chloromethylketone. How would you modify the structure of this inhibitor tolabel the active site of trypsin?
What are the measures to inhibit the Maillard reaction in undesirable situations. please explain detailed
The reaction catalyzed by phosphorylase is readily reversible in vitro. At pH 6.8, the equilibrium ratio of orthophosphate to glucose 1-phosphate is 3.6. The value of ΔG°’ for this reaction is small because a glycosidic bond is replaced by a phosphoryl ester bond that has a nearly equal transfer potential. However, phosphorolysis proceeds far in the direction of glycogen breakdown in vivo. Suggest one means by which the reaction can be made irreversible in vivo.

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