enzymes part ii
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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 - PowerPoint PPT PresentationTRANSCRIPT
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EnzymesPart II
COURSE TITLE: BIOCHEMISTRY 1COURSE CODE: BCHT 201
PLACEMENT/YEAR/LEVEL: 2nd Year/Level 4, 1st Semester
M.F.Ullah, Ph.DShowket H.Bhat, PhD
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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
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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
Enzyme-Substrate Complex Details
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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
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Possible Types of Transition State Changes
1. The enzyme might put “stress” on a bond facilitating bond breakage
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2. The enzyme might bring two reactants into close proximity and maintain proper orientation.
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Chemicals can bind to enzymes and eliminate or drastically reduce catalytic activity
Classify enzyme inhibitors on the basis of reversibility and competition.◦ Irreversible inhibitors bind tightly to the enzyme
and thereby prevent formation of the E-S complex.◦ Reversible competitive inhibitors often
structurally resemble the substrate and bind at the normal active site
◦ Reversible noncompetitive inhibitors usually bind at someplace other than the active site. Binding is weak and thus, inhibition is reversible
Inhibitors of Enzyme Activity
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react with specific type of enzyme functional group (e.g., Ser-OH, or Cys-SH, or His imidazole)
on any enzyme/protein Irreversible 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
Irreversible Inhibitors
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Mechanism of Nerve gas- A potent neurotoxin
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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, Competitive Inhibitors
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Reversible, Competitive Inhibitors
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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
Reversible, Noncompetitive Inhibitors