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Enzyme

Enzymes help break down nutrients into smaller molecules during digestion. They are proteins that catalyze biochemical reactions without being used up in the process. Each enzyme has a specific 3D structure and active site that allows only certain substrates to fit and undergo reaction. The rate of enzymatic reactions is affected by factors like temperature, pH, cofactors, and inhibitors. Enzymes work together in metabolic pathways to transform initial substrates into final products through a series of reaction steps.
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0% found this document useful (0 votes)
8 views

Enzyme

Enzymes help break down nutrients into smaller molecules during digestion. They are proteins that catalyze biochemical reactions without being used up in the process. Each enzyme has a specific 3D structure and active site that allows only certain substrates to fit and undergo reaction. The rate of enzymatic reactions is affected by factors like temperature, pH, cofactors, and inhibitors. Enzymes work together in metabolic pathways to transform initial substrates into final products through a series of reaction steps.
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ENZYME

METABOLISM
Enzyme Metabolism
• enzymes help to break down large nutrient molecules, such as
proteins, fats, and carbohydrates, into smaller molecules.
• This process occurs during the digestion of foodstuffs in the
stomach and intestines of animals. Other enzymes guide the
smaller, broken-down molecules through the intestinal wall
into the bloodstream.
• Enzymes are specific biological protein that catalyze
biochemical reactions without altering the equilibrium point
of the reaction or changed in composition.
• The catalyzed reactions are frequently specific and essential
to physiologic functions.
General Properties of Enzymes
• Enzymes catalyze many specific physiologic reactions. These
reactions are facilitated by the enzyme structure and several
other factors. As a protein, each enzyme contains a specific
amino acid sequence.

I. Primary structure
- The resultant polypeptide chains twisting

II. Secondary structure


- Refers to the coiling or folding of the peptide chain
III. Tertiary structure
- Results in structural Cavities

IV. Quaternary structure


- Refers to the spatial relationship between the sub units.
- Each enzyme contains an active site – often a water-free cavity,
where the substance on which the enzyme acts or interacts with
particular charged amino acid residues.

- Even though a particular enzyme maintains the same catalytic


function throughout the body, that enzyme may exist in different
forms within the same individual.
Physical Properties of Enzyme
I. Isoform
- contribute to heterogeneity in properties and function of
enzymes.
II. Cofactor
- a non-protein molecule, that may be necessary for
enzyme activity.
III. Heloenzyme
- forms a complete and active system.
IV. Zymogen
- originally secreted from the organ of production and an
inactive form.
Mechanism of Enzyme action
• Ability of enzymes to lower activation energy
due to structure.
• Each type of enzyme has a highly-ordered,
characteristic 3-dimensional shape (conformation).

Substrates
- the chemical species being observed in a chemical reaction,
which reacts with a reagent to generate a product.
In synthetic and organic chemistry, the substrate is the chemical
of interest that is being modified.
Substrates have specific shapes to fit into the active sites:

– Substrate fits into active sites in enzyme.


– Perfect fit may be induced:
• Enzyme undergoes structural change.
– Enzyme-substrate complex formed, then dissociates.
– Products formed and enzyme is unaltered.
Factors that affects Enzymatic Reaction
Temperature
- Slightly above body temperature (37o C), as temperature
increases reaction rate also increases.

pH
- Each enzyme exhibits peak activity at narrow pH range (pH
optimum).
- pH optimum reflects the pH of the body fluid in which the
enzyme is found.
Cofactors
- Attachment of cofactor causes a conformational change of active site.

Inhibitors
- Competitive Inhibitors:
Shape at least partially fits in the enzymes active site
“ blocks substrate from binding.”
• Allosteric “different shape” Inhibitors:
Bind to a different location of the enzyme protein— the allosteric site
“active site no longer fits substrates”
Metabolic Pathway
• Sequence of enzymatic reactions that begins
with initial substrate, progresses through
intermediates and ends with a final product.

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