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Enzymes Part II. M.F.Ullah , Ph.D Showket H.Bhat , PhD. COURSE TITLE : BIOCHEMISTRY 1 COURSE CODE : BCHT 201. PLACEMENT/YEAR/LEVEL: 2nd Year/Level 4, 1st Semester. The Enzyme-Substrate Complex. These reversible reaction steps represent the steps in an enzyme catalyzed reaction

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Enzymes

Part II

M.F.Ullah, Ph.D

ShowketH.Bhat, PhD

COURSE TITLE: BIOCHEMISTRY 1

COURSE CODE: BCHT 201

PLACEMENT/YEAR/LEVEL: 2nd Year/Level 4, 1st Semester

the enzyme substrate complex
The Enzyme-Substrate Complex
  • These reversible reaction steps represent the steps in an enzyme catalyzed reaction
    • The first step involves formation of an enzyme-substrate complex, E-S
    • E-S* is the transition state
    • E-P is the enzyme-product complex
enzyme substrate complex details
Enzyme-Substrate Complex Details
  • The part of the enzyme combining with the substrate is the active site
  • Active sites characteristics include:
    • Pockets or clefts in the surface of the enzyme
      • R groups at active site are called catalytic groups
    • Shape of active site is complimentary to the shape of the substrate
    • The enzyme attracts and holds the enzyme using weak noncovalent interactions
    • Conformation of the active site determines the specificity of the enzyme
the transition state and product formation
The Transition State and Product Formation

How does the enzyme promote a faster chemical reaction?

  • As the substrate interacts with the enzyme, its shape changes and this new shape is less energetically stable
  • This transition state has features of both substrate and product and falls apart to yield product, which dissociates from the enzyme
possible types of transition state changes
Possible Types of Transition State Changes
  • The enzyme might put “stress” on a bond facilitating bond breakage
inhibitors of enzyme activity
Inhibitors of Enzyme Activity
  • Chemicals can bind to enzymes and eliminate or drastically reduce catalytic activity
  • Classify enzyme inhibitors on the basis of reversibility and competition.
    • Irreversible inhibitorsbind tightly to the enzyme and thereby prevent formation of the E-S complex.
    • Reversible competitive inhibitorsoften structurally resemble the substrate and bind at the normal active site
    • Reversible noncompetitiveinhibitors usually bind at someplace other than the active site.
      • Binding is weak and thus, inhibition is reversible
irreversible inhibitors
Irreversible Inhibitors
  • react with specific type of enzyme functional group (e.g., Ser-OH, or Cys-SH, or His imidazole)

on any enzyme/proteinIrreversible enzyme inhibitors bind very tightly to the enzyme

    • Binding of the inhibitor to one of the R groups of a amino acid in the active site
      • This binding may block the active site binding groups so that the enzyme-substrate complex cannot form
      • Alternatively, an inhibitor may interfere with the catalytic group of the active site eliminating catalysis
    • Irreversible inhibitors include:
      • Arsenic
      • Snake venom
      • Nerve gas
reversible competitive inhibitors
Reversible, Competitive Inhibitors
  • Reversible, competitive enzyme inhibitors are also called structural analogs
    • Molecules that resemble the structure and charge distribution of a natural substance for an enzyme
    • Resemblance permits the inhibitor to occupy the enzyme active site
    • Once inhibitor is at the active site, no reaction can occur and the enzyme activity is inhibited
  • Inhibition is competitive because the inhibitor and the substrate compete for binding to the active site
    • Degree of inhibition depends on the relative concentrations of enzyme and inhibitor
reversible noncompetitive inhibitors
Reversible, Noncompetitive Inhibitors
  • Reversible, noncompetitive enzyme inhibitors bind to R groups of amino acids or to the metal ion cofactors
    • This binding is weak
    • Enzyme activity is restored when the inhibitor dissociates from the enzyme-inhibitor complex
    • These inhibitors:
      • Do not bind to the active site
      • Do modify the shape of the active site once bound elsewhere in the structure