General Biology
Second Grading
Biological Molecules
ENZYMES
erminology
‘catalyst -a substance that speeds up a chemical reaction without
being changed
(enzyme-a biological catalyst (usually a protein)
(Substrate - the reactant mole that an enzyme works on
(Active'site -part of the enzyme where the substrate binds
-formed when the substrate molecule
collides with the active site of its site
transition staté -the intermediate stage in a reaction in which the old
bonds break and new bonds are formed
activation energy) -the minimum energy required to start a chemical
reaction
Enzymes are protein macromolecules.
They have a defined amino acid sequence and are typically 100 - 500
amino acids long.
They have a defined three-dimensional structure.
They act as a catalyst to a chemical or biochemical reaction, with a
defined mechanism.
They increase the speed of the reaction, typically by 106/= 1014 timesfaster than the rate of the uncatalyzed reaction.
They are selective for a single substrate.
They are stereospecific, the reaction produces a single product.
Enzymes are not reactants and are not used up during the reaction.
Once an enzyme binds to a substrate and catalyzes the reaction, the
enzyme is released, unchanged, and can be used for another
reaction.
For each reaction, there does not need to be G 11 ratio between the
enzyme and substrate molecules.
Nomenclature
-typically add "-ase" to the name of the substrate
e.g. lactase breaks down lactose (disaccharides of glucose and
galactose)
Processes that Involves Enzymes
Anabolism) -requires energy to build
*synthesis of macromolecules
ismy-uses energy to breakdown
*digestion of food particles
Apoenzyme
-an inactive enzyme, activation of the enzyme occurs upon binding of
an organic or inorganic cofactor-enzymes that lack their necessary cofactor(s) for proper functioning
-protein
-active forms of apoenzymes (apoenzyme plus cofactor)
*DNA polymerase and RNA polymerase
-mostly metal ions or small organic molecules are organic and
inorganic chemicals that assist enzymes during the catalyst of
reactions
-nonprotein component
e.g. magnesium, zinc
-nonprotein organic molecules that re mostly derivatives of vitamins
soluble in water by phosphorylation
-organic cofactor
e.g. NADH, FADH
-part of the enzyme to which substrates binds and where a reaction is
catalyzed
-a reactant in a chemical reaction
- called substrate when acted upon by an enzyme-since enzymes are proteins, this site is composed of a unique
combination of amino acid residues (side chains or R groups)
-each amino acid residue can be large or small; weakly acidic or
basic; hydrophilic or hydrophobic; and positively-charged,
negatively charged, or neutral
-a specific chemical substrate matches this site like a jigsaw puzzle
Pieceond mokes the enzymesspecitic fois substrate)
~proposes that the initial interaction aind substrate is relatively Weak,
but that these weak interactions rapidly induce a conformational
-when an enzyme binds its substrate, it forms an enzyme-substrate
complex
-this complexilowers the activation energy of the reaction and
[promotes its rapid progression by providing certain ions or chemical
i Is @ necessary step
of the reaction process
Enzymes based upon the class of organic chemical reaction
catalyzed:
catalyze redox reactions; dehydrogenases, oxidases,
eroxidases, reductases
falcata catalyze group transfer reactions; often require
coenzymes
(Hydrolases\- catalyze hydrolysis reactionsLyases - lysis of substrate; produce contains a double bond.
Isomerases - catalyze structural changes; isomerization.
Ligases - ligation or joining of two substrates with the input of energy,
usually from ATP hydrolysis; often called synthetases or synthesis
The enzyme's active site binds to the substrate.
The induced-fit model states a substrate binds to an active site and
both change shape slightly, creating an ideal fit for catalysis.
-when an enzyme binds its substrate, it forms an enzyme-substrate
“complex
renzymies (aint by bringing Saar
(injanjoptimaljorientation) thus creating an ideal chemical
environment for the reaction to occurOxidation-Reduction Reaction
Redox React ior
-addition of oxygen/electronegative element to a substance
-removal of hydrogen/electropositive element from a substance
-removal of oxygen/electronegative element from a substance
-addition of hydrogen/electropositive element to a substance
Enzymatic browning is a natural phenomenon that occurs widely in
many fruits and vegetables. When fruits and vegetables are bruised,
cut, peeled, diseased, or exposed to any abnormal conditions, they
darken rapidly on
brown melanins from the oxidation of phenolic
compounds. Polyphenol oxidase (PPO) present in most fruits and
vegetables, and some seafood, is responsible for enzymatic browning.
In addition to PPO, the presence of peroxidase, a similar oxidative -
“enzyme, may initiate enzymatic browning of fruits and vegetables. Ths
article presents an overview of the current understanding of
the browning reaction about biochemical characteristics and
potential physiological roles of PPO in fresh fruits and vegetables andprovides the latest information on the control of enzymatic browning
in foods.
7 Factors that Affect Enzyme Activity
‘Temperature
Raising temperature will generall ion, and a
lowering temperature will in. However, the q
oe cause an enzyme to denature and to stop.
Most enzymes have an optimum temperature, near-normal u
body temperature, at which they catalyze a reaction most rapidly.
Each enzyme has an optimum pH range, changing pH level outside
this range will slow down enzyme activity. Such extreme pH values can
cause an enzyme to denature, even small changes can alter the
in enzymes, therefore
Increasing enzyme concentration wil speed up the reaction as long
. Once all the substrates are
as
bound to an enzyme, the reaction will no longer speed up.
“Substrate Concentration
Increasing substrate concentration wl jon up too
certain point. A
on the reaction as all the enzymes are bound, the available enzymes
will saturate and work at their maximum rate. At saturation point, the-photosynthesis
-decay
-respiration
-biological respiration
-corrosion/rustingATP (adenosine triphosphate)
What is ATP?
Adenosine triphosphate, or ATP, is a small, relatively simple molecule.
It can be thought of as the main energy currency of cells, much as
money is the main economic currency of human societies. The energy
released by hydrolysis (breakdown) of ATP is used to power many
energy-requiring cellular reactions.
Structurally, ATP is an RNA nucleotide that bears a chain of three
phosphates. At the center of the molecule lies a five-carbon sugar,
ribose, which is attached to the nitrogenous base adenine and the
chain of three phosphates.
The three phosphate groups, in order of closest to furthest from the
ribose sugar, are labeled alpha, beta, and gamma. ATP is made
unstable by the three adjacent negative charges in its phosphate tail,
which "want" very badly to get further away from each other. The
bonds between the phosphate groups are called phosphoanhydride
bonds, and you may hear them referred to as "high-energy" bonds.
Hydrolysis of ATP
Why are the phosphoanhydride bonds considered high-energy? All
this means is that an appreciable amount of energy is released when
one of these bonds is broken in a hydrolysis (water-mediated
breakdown) reaction, ATP is hydrolyzed to ADP in the following
reaction:ATP+H20%ADP+Pi+energy
Note: Pi just stands for an inorganic phosphate group.
These three phosphate groups are linked to one another by two high-
energy bonds called phosphoanhydride bonds. When one phosphate _
group is removed by breaking a phosphoanhydride bond in a process
called hydrolysis, energy is released, and ATP is converted to
_ adenosine diphosphate (ADP).
Reactions can also be classified by the overall increase or decrease in
Generoy|frofnithelrpaction.
Less energy is required to break original bonds than is released when
new one forms.
_EnergeticReactions
Chemical reaction that requires more energy to go in (break reactant
bond) than is feleased when new bonds are formed (create product).
How is the energy released by ATP hydrolysis used to power other
reactions in a cell?
In most cases, cells use a strategy called reaction coupling, in which