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Enzyme Inhibition
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Irreversible and Reversible Inhibition

Ashish Kr Dwivedi
Follow me on my Youtube: Triyambak Life Sciences Former Scientist (IIT Kanpur), Authored 10+ Peer Reviewed International Publications, PhD (

Unacademy user
very useful topic are very much clear with nice and clear voice thank you so much mam
thankyou so much sir
  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