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Lecture

10 - Enzymes.docx

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Department
Biology (Sci)
Course
BIOL 112
Professor
Frieder Schoeck
Semester
Winter

Description
Enzymes Enzymes bind to specific molecules called substratesSubstrates bind to specific site on the enzymes surface called the active site where catalysis occursHIGHLY specific 3 Possibilities1 Bind in a correct orientation to speed uppromote reaction 2 Cause strain slightly change conformation making reaction more likely3 Charge transfer molecule is given charge to induce reaction and charge is returnedCofactorsSome enzymes require them to function examplesMetal Ions Zn Cu Small organic molecules that are permanently or temporarily bound to help catalysisEnzymes are saturated when all active sites have a substrate thus theres a maximal reaction rate Maximum Rateturnover from 1 moleculesec for lysosome all the way to 40 million moleculessec for catalaseEnzyme Regulation and Catalysis Regulation of Metabolic Pathway Feedback inhibitionstops formation of final product so that it is not created in excess Multiple Feedbackallows cells to adjust ratio of different compounds such as amino acids Can be inhibited Artificial and natural binders Naturally occurring inhibitors regulate metabolismIrreversible inhibition occurs when inhibitor destroys enzymes ability to interact with its normal substratesuch as covalently bonding to active site Reversible Inhibition 1 Competitive Inhibition another substrate competes and when there is enough more of it will block the enzyme from catalyzing its normal substrate2 Noncompetitive Allosteric Inh ibitionAn allosteric regulator can come in and change the conformation of the enzyme and not allow any substrate to bind Must more efficient than competitive since less inhibitors are required large about of substrate less enzymes less inhibitors In contrast competitive you need competitivesubstrate There can also be POSITIVE regulation activate enzyme NOTE Cooperative allosteric transition
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