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Enzyme Inhibition
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Irreversible and Reversible Inhibition

Ashish Kr Dwivedi
Former Scientist (IIT Kanpur), Authored 10+ Peer Reviewed International Publications, PhD (IITK) Chief Mentor Triyambak Life Sciences

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Unacademy user
  1. Basics of Biochemistry Enzyme Inhibition Ashish Kr Dwivedi, PhD


  2. Irreversible inhibitor is specific for a particular type of protease, for example serine proteases, thiol proteases, aspartic proteases and metalloproteases. Common examples of inhibitors include: di-isopropylphosphofluoridate (DFP), phenylmethyl sulphonylfluoride (PMSF) and tosylphenylalanyl-chloromethylketone (TPCK) (all serine protease inhibitors) iodoacetate and cystatin (thiol protease inhibitors) pepstatin (aspartic protease inhibitor) EDTA and 1,10-phenanthroline (metalloprotease inhibitors)


  3. Reversible inhibiton Inhibitor type None Competitive Uncompetitive Mixed Apparent K K, Apparent V max max max max max


  4. Competitive inhibition E+ P EI Competitive inhibitors bind to the enzyme's active site; K is the equilibrium constant for inhibitor binding to E.


  5. max / [S] V max 1 No inhibitor Slope V Tm maX max S mM


  6. Uncompetitive inhibition lo ESI Uncompetitive inhibitors bind at a separate site, but bind only to the ES complex; Ki is the equilibrium constant for inhibitor binding to ES.


  7. Km , = 2 '=1.5 , 1 maX [S] mM


  8. Mixed inhibition ESI Mixed inhibitors bind at a separate site, but may bind to either E or ES.


  9. , maX maX No inhibitor maX [S] mM