Enzymes Flashcards

1
Q

What are enzymes?

A
  • Enzymes are biological catalysts
  • Almost every significant life process is dependent on
    enzyme activity. .
  • Almost all enzymes are protein, except for a class of
    RNA modifying catalysts known as ribozymes.
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2
Q

What is enzyme catalysis?

A
  • In enzyme-catalyzed reactions, substrate
    concentrations are usually greater than the enzyme
    concentration.
  • Enzyme catalysis involves the binding of the
    substrate to a specific site on the enzyme, (active or
    catalytic site
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3
Q

What happens during enzyme catalysis?

A
  • During enzyme catalysis, (ES) complex is first formed
    then; proceeds to a transition state (ES*); before it
    forms enzyme product complex (EP) which
    dissociate to product and free enzyme.
  • The series of events can be shown thus:
    E + S <-> ES <-> ES* <-> EP <-> E + P
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4
Q

What is the enzyme nomenclature?

A

Traditionally, enzymes were simply assigned
names by the investigator who discovered the
enzyme.
* As knowledge expanded, systems of enzyme
classification became complex.

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5
Q

How are enzymes classified currently?

A
  • Currently enzymes are grouped into six
    functional classes by the International Union
    of Biochemists (I.U.B.).
  • I.U.B. gave each enzyme a unique number.
    And specifies a textual name for each enzym
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6
Q

What are the type of enzymes classified by I.U.B?

A

1 Oxidoreductases Add or remove hydrogen atoms.
2 Transferases Transfer functional groups.
3 Hydrolases Add water across a bond, hydrolyzing
it.
4 Lyases Add or remove water, ammonia or
carbon dioxide across double bonds
5 Isomerases Catalyze isomerizations,
6 Ligases Join two chemical groups with the use
of energy from ATP

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7
Q

How is the enzyme name and number composed?

A
  • Each enzyme is given a four digit number
    specifying its class, subclass, substrate and the
    type of the reaction
  • The enzyme’s name is comprised of the names of
    the substrate (S), the product (P) and the enzyme’s
    functional class.
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8
Q

What is another way in which enzymes are classified?

A
  • Enzymes are also classified on the basis of their
    composition.
  • Enzymes composed wholly of protein are known as
    simple enzymes in contrast to complex enzymes,
    which are composed of protein plus a relatively
    small organic molecule.
  • Complex enzymes are also known as holoenzymes.
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9
Q

What are holoenzymes composed of?

A
  • The protein component in the holoenzyme is called
    apoenzyme, while the non-protein part is the
    coenzyme or prosthetic group.
  • The prosthetic group is the small organic molecule
    bound to the apoenzyme by covalent bonds
  • Coenzyme is the small organic molecule noncovalently bound to the apoenzym
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10
Q

What is the non-protien part of enzyme composed as?

A
  • The non-protein component of an enzyme may be as
    simple as a metal ion or as complex as a small nonprotein organic molecule
  • Many prosthetic groups and coenzymes are watersoluble derivatives of vitamins.
  • Enzymes that require a metal in their composition are
    known as metalloenzymes
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11
Q

What do coenzymes do?

A
  • Coenzymes act as transporters of chemical
    groups from one reactant to another.
  • The chemical groups carried can be as simple
    as the hydride ion (H+ + 2e-) carried by NAD
    or the mole of hydrogen carried by FAD; or
    amine (-NH2) carried by pyridoxal phosphate.
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12
Q

How do coenzymes play a role as substrates?

A
  • Coenzymes are chemically changed as a
    consequence of enzyme action, thus can be
    considered as second substrates,
  • Unlike usual substrates the coenzymes are
    recycled to their original form when donate the
    carried chemical grouping to an acceptor
    molecule
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13
Q

How are enzymes specific?

A
  • Enzymes are highly specific for the kind of
    reaction they catalyze,
  • Enzymes are also specific towards the substrate,
  • Some enzymes have broad substrate specificity,
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14
Q

How are enzymes specific about steric configuration of substrates?

A
  • Enzymes also are generally specific for a
    particular steric configuration (D and L
    optical isomer) of a substrate.
  • The racemases are striking exception to
    these generalities; they convert D isomers to
    L isomers and vice versa
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15
Q

What are isozymes?

A
  • Are multiple forms of an enzyme acting on
    the same substrate and produce the same
    product.
  • These are the products of genes that vary
    only slightly.
  • Various isozymes are expressed in different
    tissues of the body.
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16
Q

What is the best studied set of isozymes?

A
  • The best studied set of isozymes is the
    lactate dehydrogenase (LDH).
  • LDH is a tetrameric enzyme composed of all
    possible arrangements of two different
    protein subunits (H) for heart and (M) for
    skeletal muscle.
17
Q

What are the isoforms of lactate dehydrogenase

A
  • HHHH Isoenzyme-1 Heart
  • HHHM Isoenzyme-2
  • HHMM Isoenzyme-3
  • HMMM Isoenzyme-4
  • MMMM Isoenzyme-5 Muscle
18
Q

How are enzyme substrate reactions explained?

A
  • Two models were proposed to explain the
    nature of enzyme substrate binding.
  • The Key and lock model
  • The induced fit model
19
Q

How does the induced fit model explain enzyme substrate interactions?

A

The induced fit model proposes that the
initial interaction between enzyme and
substrate is relatively weak, and not
necessarily complementary but it induces
conformational changes in the enzyme