6-Enzymes

Shafie Abdulkadir Hassan

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Terms should be learn
• allosteric enzyme; a regulatory enzyme whose affinity
for its substrate is affected by the presence or absence of
other molecules
• Apoenzyme; protein portion of an enzyme (i.e., lacking a
coenzyme)
• Enzyme; protein which catalyzes a biochemical reaction,
an enzyme name ends in -ase (e.g., amylase and carbonic
anhydrase)
• Holoenzyme; complete active enzyme (i.e.,
protein + coenzyme)

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• enzyme classificationl; assignment of an enzyme to one of six groups, depending
on the type of chemical reaction which the enzyme catalyzes
• first order kinetics; rate of reaction is directly proportional to the concentration
of starting materials (i.e., substrate)
• Inhibition; alteration in an enzyme’s activity, usually caused by modification of
the enzyme active site, so that substrate cannot bind to the enzyme, or substrate
can bind but cannot be converted to product, or product cannot be released
• Michaelis-Menten kinetics; simple mathematical description of a first-order
enzyme reaction [Leonor Michaelis was British and Maud Menten was Canadian ]
• Catalyst; chemical substance that facilitates (or slows) a chemical process, but is unchanged
by the process
• Coenzyme; small, nonprotein group attached to an enzyme; the site on the enzyme where
catalysis occurs
• Cofactor; organic molecule that acts as a coenzyme
• Michaelis constant ( Km ) represent the concentration of a substrate that is found in an
occurring reaction when the reaction is at one half its maximum velocity

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 Enzymes
• macromolecular components composed of protein
They are known as biological catalysts responsible
for supporting almost all of the chemical reactions
that maintain life processes
• Enzymes are found in all tissues and fluids of the
body.
• Enzymes have a high degree of specify for types of
reaction catalized and for their substrate
• Enzymes are also stereospecific catalysts for
specific stereoisomers (L & D)
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• All enzymes are proteins except ribozymes;
• ribozymes are certain RNA molecules act as
catalysts

• ribozymes catalyzing the cleavage and

synthesis of phosphodiester bond in RNA at
specific sites in RNA

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Localization of enzymes

• 1-Enzymes of the intracellular

• Lysosome; enzyme required for the degradation
of complex macromolecules
• Nucleous; enzymes of DNA and RNA synthesis
• Cytosol; enzyme of glycolysis, fatty acid
synthesis, urea cycle, gluconeogenesis, heam
synthesis
• Mitochondria; enzymes of TCA cycle, fatty acid
oxidation, oxidative phosphorylation
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• 2-extracellular enzymes
• Are secreted and function out from the cell
• Mainly digestive enzymes
• Alfa amylase secreted by salivary glands
• Pepsin and renin secreted by gastric glands
• Lipase, trypsin, chymotrypsin, amylase secreted by
pancreas
• Aminopeptidase, dipeptidase, lactase, sucrase,
maltase, isomaltase secreted from intestinal glands
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 Proenzyme or zymogen (precursor enzyme)

• Some proteolytic enzymes found in the blood

or digestive tract are present in an inactive
form (precursor) known as zymogen or
proenzymes
• Some examples; prothrombin, proelastase,
chymotrypsinogen, trypsinogen, pepsinogen
which produced and stored as inactive
proenzyme or zymogen

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 Composition classification of enzymes

• Simple enzymes composed completely of

protein
• complex enzymes, are composed of protein
plus a relatively small organic molecule.
• Complex enzymes are also known as
holoenzymes.
• protein component is known as the
apoenzyme,
• Apoenzymes becomes active enzymes on
addition of a cofacter. Shafici Cqadir 10
• Cofactors can be either inorganic (e.g., metal
ions or organic compounds, (e.g.,favin and
heme) or organic
• Organic cofactors can be either prothetic
groups, which are tightly bound to an enzyme,
or coenzymes, which are released from the
enzyme's active site during the reaction
• Coenzymes binds apoenzyme protein molecule
to produce active holoenzyme
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Cofactors can be either inorganic (e.g., metal ions or organic compounds,
(e.g.,favin and heme)
Organic cofactors can be either prothetic groups, which are tightly bound to an
enzyme, or coenzymes, which are released from the enzyme's active site during
the reaction. when the binding between the apoenzyme and non-protein
components is non-covalent, the small organic molecule is called a coenzyme

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Apoenzyme, cofactor and holoenzyme

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 classification and nomenclature of Enzyme
Reference; Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (NC-IUBMB) Enzyme Nomenclature

'

• Functional classification
• enzymes are grouped into six functional
classes by the International Union of
Biochemists (I.U.B.).

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• Class 1.Oxidoreductases- this class belong to all
enzymes of catalysing oxidoreduction reactions.
• The substrate that is oxidized is regarded as
hydrogen donor.
• Act on many chemical groupings to add or remove
hydrogen atoms
• The common name will be dehydrogenase,
reductase can be used.
• Oxidase is only used in cases where O2 is the
acceptor.
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• Class 2. Transferases- transfer chemical groups
from one molecule to another or to another
part of the same molecule (ATP).

• Kinases are specialized transferases that

regulate metabolism by transferring phosphate
from ATP to other molecules (glucokinase,
Phosphofructokinase)

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• Class 3. Hydrolases-
• Add water across a bond, hydrolyzing it
• These enzymes catalyse the hydrolytic
cleavage of C-O, C-N, C-C and some other
bonds,
• Although the systematic name always includes
hydrolase, such as digestive enzymes

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• Class 4. Lyases- remove a group from or add a
group to double bonds.
• Add water, ammonia or carbon dioxide across
double bonds, or remove these elements to
produce double bonds
• In the common names, expressions like
decarboxylase, aldolase, dehydratase (in case of
elimination of CO2, aldehyde, or water) are used

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• Class 5. Isomerases-.
• These enzymes catalyse geometric or structural
changes within one molecule. According to the
type of isomerism (interconvert isomeric
structures by molecular rearrangements),
• they may be called, cis-trans-isomerases,
phosphohexose-isomerases, tautomerases,
mutases and L to D isomerase,

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• Class 6. Ligases –
• Ligases are enzymes catalysing the joining together
of two molecules coupled with the hydrolysis of a
diphosphate bond in ATP or a similar triphosphate
• Catalyze reactions in which two chemical groups are
joined (or ligated) with the use of energy from ATP

• pyruvate oxaloacetate
• enzyme = pyruvate carboxylase

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 The Catalytic Activity of Enzymes

• enzymes are characterized by two fundamental

properties.
• 1- First, they increase the rate of chemical reactions
without themselves being consumed or permanently
altered by the reaction.
• 2-Second, they increase reaction rates without altering
the chemical equilibrium between reactants and products,
• a molecule acted upon by an enzyme is called substrate
[S]
• substrate [S] is converted to a product (P)

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• The functional activities depend on
• 1-protein portion of enzyme
• 2-non-protein prothetic group or co-enzyme
• Usually prothetic group is inorganic (metal ions, Mg,
Zn, Cu, Mn, Fe
• Enzyme activity system may affected by;-
• Negative modifiers
• Change on pH
• Change in enzyme concentration
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 Factors affecting the Velocity of Enzyme
reaction
• Any substrate that affects the configuration of an
enzyme affects its activity
• Various factors that affect enzyme activity are;-
• 1-substrate concentration
• 2-Enzyme concentration
• 3- Ph (H ions concentration)
• 4-temperature
• 5-product concentration
• 6-inhibitors
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glossary
• Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (NC-IUBMB)
Enzyme Nomenclature
• Michael W King, PhD | © 1996–2012 themedicalbiochemistrypage.org, LLC | info @
themedicalbiochemistrypage.org
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• Sareen Gropper, Jack Smith and James Groff, Advanced Nutrition and Human Metabolism, fifth ed.
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• Koppenol, W. H. (2002). "Naming of New Elements (IUPAC Recommendations 2002)" (PDF). Pure and
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• Guyton, C. Arthur. 1985. Textbook of Medical Physiology. 6th edition, W.B. Company

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• Murry K. Robert, Granner K. daryl, Mayes A. peter, Rodwell W. Victor (1999). Harpers Biochemistry.
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• Cooper GM 2000. The Central Role of Enzymes as Biological CatalystsThe Cell: A Molecular Approach. 2nd
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