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lect16 - Ch395G Fall 2009 Lecture 16 Enzymatic Catalysis...

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Ch395G Fall 2009: Lecture 16 Enzymatic Catalysis And Control
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Enzyme Catalysis Lysozyme as an example – look for how rate is enhanced and the methods used to determine mechanistic information. Biochemical Data Structural Data Phillips Mechanism Recent Developments
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Summary – What “chemical” mechanisms were employed in Lysozyme? What methods provided the data to work out the current mechanism?
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Correction I had noted earlier that procaryotes do not carry out protein glycosylation and that this resulted in problems for making some effective eucaryotic recombinant proteins in bacterial hosts. Recently it was discovered the Campylobacter jejuni can do both N- and O- linked glycosylation. The systems for doing this glycosylation have now been transferred to E.coli .
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Control of Enzymatic Activity Rates of synthesis and degradation (Nobel Prize for the ubiquitination pathway) See Chapter 13 pages 465 - 470 Proenzyme (zymogen) conversion Presence of activators and inhibitors Covalent Modification Allosteric Control
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From the National Museum of Medicine
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Ubiquitin tagging of proteins for degradation Irwin Rose (UCSD) one of the 3 Nobel Prize winners
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