Enzyme Regulation - simply be the reverse of each other...

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Enzyme Regulation Understand the different mechanisms by which enzyme activity can be regulated, and know some examples of each Understand how the MWC model explains cooperativity in substrate binding and allosteric regulation Understand how the KNF model explains cooperativity in substrate binding and allosteric regulation Know the quaternary structures of hemoglobin and myoglobin Understand how oxygen binds and how binding causes conformational changes Binding causes small changes in tertiary structure and large changes in quaternary structure of Hb, cooperativity shows features of both models 2,3-bisphosphoglycerate is an allosteric effector of Hb Metabolism Understand how the redox transformations of NADH/NAD + are coupled to the redox reactions of organic metabolites Catabolic and anabolic pathways that inter-convert the same metabolites cannot
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Unformatted text preview: simply be the reverse of each other Understand how such pathways can be reciprocally regulated Carbohydrates Starch is a polymer of amylose and amylopectin containing both 1,4 and 1,6 glycosidic bonds Plant starch phosphorylase releases glucose-1-phosphate from starch (following isomerization to glucose-6-phosphate this can enter glycolysis) In animals, salivary amylase and (1,6) glucosidase participate in starch catabolism Glycogen is identical to starch except for the degree of branching Cellulose is (1,4) linked glucose units The different nature of the glycosidic bond in amylose and cellulose has a profound effect on properties Peptidoglycan (structural polysaccharide in bacteria) contains N-acetyl sugars with cross-linked peptide side chains...
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This note was uploaded on 02/08/2012 for the course CHEM 3361 taught by Professor Marsh during the Spring '11 term at University of Texas at Dallas, Richardson.

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