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Lecture 7

Lecture 7 inhibition.docx

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Department
Biochemistry
Course Code
BCH210H1
Professor
Stavroula Andreopoulos

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Description
Lecture 7 Inhibition - enzymes can be inhibited reversibly or irreversibly - reversible inhibitors – interact with the enzyme through noncovalent association/dissociation reactions - irreversible inhibitors – usually form covalent bonds with side chains or prosthetic groups in the enzyme - decrease in concentration of active enzyme with irreversible inhibitors Reversible Inhibition - bind at active site or some other site - three categories of reversible inhibitors – competitive, noncompetitive, uncompetitive - competitive inhibitors – substrate and inhibitor compete for the same binding site on the enzyme – on the active site/substrate-binding site - increasing the concentration of substrate favours S binding to the enzyme instead of inhibitor, I – high concentration S can overcome the effects of I - other types of inhibition cannot be overcome by increase in S concentration Competitive Inhibition - binding of I and S are mutually exclusive and competitive - formation of the complex IES is impossible – only one can be bound to the enzyme - deduction that I and S share structural similarity – bind at the same site on the enzyme Noncompetitive Inhibition - interact with both E and ES, and rarely, with S and ES - inhibitor does not bind to the same site as S - inhibition cannot
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