Chapter 14 Biocatalysis Hour2

download Chapter 14 Biocatalysis Hour2

of 4

Transcript of Chapter 14 Biocatalysis Hour2

  • 7/30/2019 Chapter 14 Biocatalysis Hour2

    1/4

    12/26/2011

    1

    Powerpoint@lecture Slides Are Prepared By Biology Lecturer, KMPk

    14.1 : Properties of enzyme and mechanism of actions

    14.2 : Cofactor

    Enzymes?

    Properties of Enzymes.

    Activation Energy?

    Mechanism of Enzyme Action :

    Lock and Key Model

    Induced-Fit Model

    At the end of this subtopic, students should able to :

    a) Explain Factors That Affect The Enzymatic

    Reaction.

    b) Explain The Types and Functions of Cofactors.

    www.themegallery.com

    FACTORS THAT AFFECT THE

    ENZYMATIC REACTION

    The rate of an enzyme-catalyzed reaction is affected

    by :

    Chemical and Physical Factor that alters the enzymes 3-D

    shape :

    Temperature

    pH

    Regulatory molecules

    Concentration ofsubstrate and enzyme.

    Chemicals that specifically influence the enzyme.

    Cofactors

    FACTORS THAT AFFECT THEENZYMATIC REACTION

    mailto:point@lecturemailto:point@lecture
  • 7/30/2019 Chapter 14 Biocatalysis Hour2

    2/4

    12/26/2011

    2

    www.themegallery.com

    Effect of Temperature

    Each enzyme has an optimal

    temperature.

    Optimal temperature: at which

    an enzyme produces the highest

    production rate.

    Optimal conditions favor the

    most active shape for the

    enzyme.

    Effect of Temperature

    Effects the movement of enzyme.

    Increase temperature : The rate ofan enzymatic reactions increase .

    Substrates collide with active sites

    more frequently.

    Fastest conversion of the reactants

    to product molecules.

    Above optimal temperature:

    Enzymes denatured

    Rate of reactions drop sharply

    www.themegallery.c

    EFFECTS OF pH

    Affects the charge of amino

    acids side chains with carboxyl

    or amino groups (active site).

    Maximum rate of reaction

    occurs at optimum pH (most

    enzyme pH 6-8)

    Different enzymes, different

    optimum pH.

    Example :

    Pepsin and Trypsin

    How does pH affect enzyme activity?

    Ionic interactions (+ve andVe) hold enzymes together.

    Deviation from optimal pH range : excess H+ / OH- .

    Alters the acidic/ basic/ functional group/side chain of

    amino acid in enzyme.

    Shifts the balance between positively and negatively

    charged amino acid residues.

    Change in the bonds and tertiary structure breakdown.

    Effect of Substrate Concentration

    Reactionvelocity

    Substrate concentration

    Vmax

    The amount of substrate will

    affect the rate of reaction.

    Substrate concentration

    increases, rate of reaction will

    increase proportionally.

    Then it will level off.

    All the enzyme molecules

    (active sites) are occupied.

    Once all enzymes are

    occupied, increasing

    substrate will no longer

    have an effect on rate

    Constant enzyme concentration

    Graph showing effect of increasing substrateconcentration

    Effect of Enzyme Concentration

    Reactionvelocity

    Enzyme concentration

    2007 Paul Billiet ODWS

    At low enzyme concentration

    and the rate of reaction is low.

    Great competition for the

    active sites.

    As the enzyme concentration

    increases, the reaction can

    proceed at a faster rate.

    more active sites.

    Substrate as a limiting factor. Constant substrate concentration

    http://www.saburchill.com/IBbiology/bio_hp.htmlhttp://www.saburchill.com/IBbiology/bio_hp.html
  • 7/30/2019 Chapter 14 Biocatalysis Hour2

    3/4

    12/26/2011

    3

    www.themegallery.c

    COFACTORS

    One or more nonprotein components

    required by enzymes in order to function

    efficeintly.

    Atom or molecules that are not part of

    the enzymes primary structure.

    3 types :

    Metal Ions/Activator (Inorganic)

    e.g Zn2+ and Mg2+

    Coenzymes (Small organic)

    e.g vitamin (also as precursor )

    Prosthetic groupwww.themegallery.com

    Non-protein inorganic substances.

    Assist in forming ES complex by bind temporarily either

    enzyme or substrate molecule into more suitable shape.

    Eg: Ca2+, Zn2+,Mg2+,Cl-

    E.g : Salivary amylase - chloride (Cl-)

    thrombokinase - calcium (Ca2+)

    www.themegallery.com

    Non-protein organic or organometallicsubstances.

    Tightly or weakly bound to the enzyme.

    Most vitamins act as coenzymes or raw material from which

    coenzymes are made.

    To remove functional group from one substrate and add it to

    another substrate. E.g: Vitamin B6 and B12

    nicotinamide adenine dinucleotide (NAD)

    NAD act to dehydrogenases by acting as hydrogen acceptor.

    www.themegallery.com

    A metal or Coenzymes that are covalently or

    noncovalently bound very tightly to their enzyme.

    E.g:

    prosthetic group of electron carrier cytochrome

    and enzyme catalase.

    FAD (riboflavin) - prosthetic group of the electron

    carrier cytochrome. It take part in oxidation-

    reduction reactions.

    (Boyer. Concepts in Biochemistry. Wiley)

    www.themegallery.com

    Assist in forming the enzyme-substrate complex

    by altering the active site into a more suitable

    shape.

    May function to withdraw electrons from the

    substrate.

    May involve in transfer of electrons / atoms /

    chemical groups in enzyme reactions.

    What is cofactor?

    State THREE types of cofactor.

    Describe the effect of pH, temperature , enzyme

    and substrate concentration .

    How do cofactors work in assisting an enzymatic

    reaction?

  • 7/30/2019 Chapter 14 Biocatalysis Hour2

    4/4

    12/26/2011

    4

    14.3 Inhibition