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Note for BCHS 3304 with Professor Briggs at UH


Note for BCHS 3304 with Professor Briggs at UH

Marketplace > University of Houston > Note for BCHS 3304 with Professor Briggs at UH

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This 2 page Class Notes was uploaded by an elite notetaker on Friday February 6, 2015. The Class Notes belongs to a course at University of Houston taught by a professor in Fall. Since its upload, it has received 16 views.

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Date Created: 02/06/15
Glycogen 01 14 linked Dglucose with 01 16 linked branches every 814 residues Glycogen granules also contain the enzymes that catalyze glycogen synthesis and degradation as well as regulatory proteins Highly branched structure permits rapid glucose mobilization through the simultaneous release of the endbranch glucose units Glycogenolysis Requires three enzymes 1 Glycogen phosphorylase catalyzes glycogen phosphorolysis bond cleavage by the substitution of a phosphate to yield GlP releases a glucose unit only if it is at least five units away from a branch point 2 Glycogen debranching enzyme breaks glycogen s branches making other glucose residues accessible to glycogen phosphorylase 3 Phosphoglucomutase converts GlP to G6P Glycogen phosphorylase degrades Glycogen to G1P Glycogen phosphorylase is a dimer of identical 842 residue subunits that catalyzes the rate controlling step in glycogen breakdown Allosterically inhibited by ATP G6P and glucose Allosertically activated by AMP A 30A long crevice on the surface of the phosphorylase monomer connects the glycogen storage site to the active site Since this crevice can accommodate a four or five sugar residues chain but cannot admit branched oligosaccharides it provides a clear physical rationale for the inability of phosphorylase to cleave glycosyl residues closer than five units from branch points Phosphorylase binds the cofactor Pyridoxal5 phosphate a vitamin BG derivative covalently linked to the enzyme via a Schiff base formed between its aldehyde group and the 8 amino group of Lys 680 In phosphorylase only the phosphate group participates in catalysis Phosphorolysis of glycogen proceeds by a random mechanism Glycogen phosphorylase undergoes conformational changes between the active R and inactive T conformations The Tstate enzyme has a buried active site and hence a low affinity for its substrates whereas the Rstate enzyme has an accessible catalytic site and a high affinity phosphate binding site AMP promotes phosphorylase s T 9 R shift by binding to the R state of the enzyme at its allosteric effector site increasing access to the active site by disordering a loop of residues that otherwise block it The conformational change also causes the Arg 569 side chain which is located in the active site to rotate in a way that increases the enzyme s binding affinity ATP also binds to the allosteric effector site but in the T state so that it inhibits not promotes the T R conformational shift Glycogen Debranching Enzyme AC1 as a Glucosyltransferase Phosphorolysis proceeds along a glycogen branch until it approaches to within four or five residues of an 01 16 branch point Glycogen debranching enzyme acts as an 01 14 transglycosylase by transferring an 01 14 linked trisaccharide unit from a limit branch of glycogen to the nonreducing end of another branch This reaction forms a new 01 14 linkage with three more units available for phosphorylase catalyzed phosphorolysis Debranching enzyme has separate active sites for the transferase and the Cl6 glucosidase reactions The maximal rate of the glycogen phosphorylase reaction is much greater than that ofthe glycogen debranching reaction Glycogen degradation beyond this point requires debranching and hence occurs more slowly Phosphoglucomutase interconverls G1P and G6P Phosphorylase converts the glucosyl units of glycogen to GlP which is converted by phosphoglucomutase to GGP Similar to the reaction in glycolysis catalyzed by phosphoglycerate mutase A phosphoryl group is transferred from the active phosphoenzyme to GlP forming Gl6P which then rephosphorylates the enzyme to yield GGP An important difference between this enzyme and PGM is that the phosphoryl group in PGM is covalently bound to a Ser hydroxyl group rather than to a His imidazole nitrogen The GGP produced by glycogen breakdown can continue along the glycolytic pathway or the pentose phosphate pathway Since the glucose is already phosphorylated the ATPconsuming hexokinase step can be bypassed In the liver this GGP is also made available for use by other tissues Because GGP cannot pass through the cell membrane it is first hydrolyzed by GGPase Although GGP is produced in the cytosol GGPase resides in the endoplasmic reticulum membrane Consequently GGP must be imported into the ER by a GGP translocase before it can be hydrolyzed The resulting glucose and phosphate are then returned to the cytosol via specific transport proteins A defect in any of the components of this GGP hydrolysis results in type glycogen storage disease Glycose leaves the liver via a specific glucose transporter named GLUTZ and is carried by the blood to ther tissues GGPase and therefore retain their GGP Muscles and other tissues lack GGPase and therefore retain their GGP


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