365 S2011 L25 - carbon 10 How does lysozyme do this 1...

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1 What do enzymes do? Use a variety of mechanisms to provide a reaction pathway with a lower energy of activation Free energy released upon binding of a substrate to the enzyme is used to lower the activation energy Supplying functional groups that initiate the reaction Increase the reaction rate
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Enzymes allow reactions to proceed under mild conditions 2
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3 Enzymes mediate coupling of biochemical reactions
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4 Enzymes can be regulated
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Enzymes are specific (binding site) 5
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6 Lysozyme Discovered twice 1909 by P. Laschtchenko in egg white 1922 by Alexander Flemming – Found that nasal mucus inhibited bacterial growth – Proceeded working on this enzyme that he isolated from the tears of volunteers
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7 Lysozyme cleaves bacterial cell walls Peptidoglycans 1. Linear polysaccharide 2. Crosslinked by short peptides
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8 Peptidoglycan
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9 Lysozyme cleaves the β glycosidic bond between the NAM 1 carbon and the NAG 4
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Unformatted text preview: carbon 10 How does lysozyme do this? 1. Specifcity substrate binding site – ( H-bonds and van der Waals interactions) 2. NAM in the D position is distorted – (preFerential binding oF the transition state) 3. Glu 35 donates a proton – (general acid catalysis) 4. Asp 52 stabilizes the carbocation by Forming a covalent bond – (covalent catalysis) 5. Glu 35 activates H 2 O – (general base) 11 Polypeptide backbone 12 Space flling model 13 Structure of Lysozyme bound to (NAG) 3 14 Modeled of the substrate into its binding site 1. Space for 6 sugar units (A-F) 2. C and E do not accommodate NAM 3. NAM must occupy site B, D, and F 4. NAM in site D has to be distorted 15 16 • Interactions that stabilize sustrate binding • NAM D is distorted • Glu 35 and Asp 52 are present close to the glycosidic bond that is cleaved...
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