AOS2 Flashcards
what are biomechanical reactions
reactions occurring in cells that lead to the formation of a product from a reactant.
what are reactants
substances (molecules/elements) that are changed from a chemical reaction
what are products
a compound produced from the reactants reacting (from the chemical reaction)
what are biomechanical pathways
a series of linked biomechanical reactions
what is metabolism
The total activity of the reactions of all biochemical pathways in a living organism
what are substrates
a compound on which an enzyme acts
what are the types of biomechanical pathways
- anabolic pathways
- catabolic pathways
what are anabolic pathways (anabolism)
These pathways turn simple molecules into more complex ones
what happens to the energy levels in the anabolic pathways
anabolic pathways are energy-requiring or endergonic
what are catabolic pathways (catabolism)
These pathways break down complex molecules into more simple ones
what happens to the energy levels in catabolic pathways
Catabolic pathways are energy-releasing or exergonic
example of anabolic pathway
Photosynthesis, where glucose molecules are synthesised from carbon dioxide and water using radiant energy from the Sun
example of catabolic pathway
Aerobic cellular respiration, where glucose molecules are broken down into carbon dioxide and water molecules
are enzymes proteins
yes most enzymes are proteins
what are catalysts
factors that increase rate of reaction
are all catalysts enzymes?
no, enzymes are all catalysts but not all catalysts are enzymes
are enzymes specific to reaction?
yes, each different reaction will be catalysed by a specific enzyme
what is activation energy
minimum amount of energy required to initiate a chemical reaction
what is the active site
region of an enzyme that binds temporarily with the specific substrate of the enzyme
what do enzymes do to speed up a reaction
lower activation levels
how do enzymes lower activation levels (2)
- Influence the stability of bonds in the reactants
- Providing an alternative reaction pathway;
how do enzymes bind to substrates (2 steps)
- the enzyme and substrate with join to form the E-S complex (when it binds to the active site)
- the substrate forms weak bonds with particular amino acid residues (in the protein) at the active site.
what are the 3 types of enzyme activity (ways they can bind to substrates)
- substrate specificity
- bond specificity
- group specificity
what is substrate specificity (enzyme activities)
they catalyse one particular substrate only
what is bond specificity (enzyme activities)
they act only on one kind of chemical bond (only peptide bonds)
what is group specificity (enzyme activities)
they act only on particular functional groups present as part of the substrate molecule (-COOH, or -OH)
what are coenzymes
an organic molecule that acts with an enzyme to alter the rate of a reaction
what are cofactors
a non-protein molecule or ion that is essential for the normal functioning of some enzymes
are cofactors and coenzymes the same
no, coenzymes are cofactors but not all cofactors and coenzymes
what are inorganic cofactors
cofactors that do not contain carbon and include metal ions such as magnesium or copper
what are organic cofactors
small non-protein organic molecules that are essential for the function of particular enzymes
what are the 2 types of organic cofactors
- prosthetic groups
- coenzymes
prosthetic groups are ……
cofactors that are tightly bound to an enzyme and are essential for it to function as a catalyst.
what is the difference between prosthetic groups and coenzymes
prosthetic groups are tightly bound to an enzyme, whereas, coenzymes are loosely bound
what are the 5 main coenzymes we focus on
- NAD
- NADP
- FAD
- ATP
- CoA (coenzyme A)
what are the 2 roles of coenzymes to assist enzymes
- transfers of atoms or groups of atoms, such as hydrogens, phosphate groups and acetyl groups
- energy transfers
what are the 2 forms coenzymes can be in (interconvertible forms)
- loaded and
- unloaded
loaded coenzymes main info
they are high in energy and have a group that can be transferred. In simple they are electron donors
unloaded coenzymes main info
they have low energy, and accept groups. In simple they are electron acceptors
what are the 3 factors that impact enzyme activity
- temperature
- pH
- substrate concentration
summary of what happens with varied temperatures for enzyme activity (rate of reaction)
when temperature first increases, the reaction rate also increases. This is because the reactants absorb heat energy and move faster, allowing them to collide and overcome the activation energy.
However, in enzyme-catalysed reactions, this increase only occurs up to the optimum temperature, after which the rate decreases, due to denaturation and the change in enzyme structure.
summary of what happen with varied pH for enzyme activity (rate of reaction)
As pH increases or decreases from optimum pH, the rate of reaction and the activity of an enzyme decreases.
do each enzyme have different optimum pH
yes, each with have different so different graphs with rate of reaction
summary of what happen with varied substrate concentration for enzyme activity (rate of reaction)
the rate of reaction increases with increasing substrate concentration — but only up to a point. Beyond this, any further increase in substrate concentration produces no significant change in reaction rate (active sites are all occupied)
what are enzyme inhibitors
substances that prevent the normal action of an enzyme and therefore slow the rate of enzymes-controlled reactions
what are the 2 types of inhibition
reversible inhibition
irreversible inhibition
what are the 2 types of reversible inhibition
- competitive inhibition
- non-competitive inhibition
what is competitive inhibition
inhibition in which a molecule binds to the active site of a molecule instead of the usual substrate
why does competitive inhibition slow down reaction rate
inhibitor molecules prevent the formation of the E–S complexes (as active site is partially occupied)
what is non-competitive inhibition
inhibition in which a molecule binds to the allosteric site of an enzyme causing a conformation change in the active site
is the active site and an allosteric site the same?
no, allosteric site is somewhere on the enzyme but not the active site itself
why does non-competitive inhibition slow down reaction rate
as the binding of the inhibitor to the allosteric site changes the shape of the enzyme’s active site the E-S complex cannot form
what is irreversible inhibition
occurs when a specific molecule can form a strong covalent bond with an enzyme at its active site, so that the normal substrate is permanently blocked from accessing the active site
what are common irreversible inhibitors?
Heavy metals
what are 3 things that the regulation of rates of reaction does
- prevent waste, such as would occur if pathway products were made in excess of cell requirements
- prevent the build-up in cells of products to potentially harmful levels
- prevent depletion of substrates
what are the 2 types of regulation
- allosteric regulation
- feedback regulation
what is allosteric regulation
control of the reaction rate of enzymes through conformational changes in enzymes. This occurs when a regulator molecule binds to the allosteric site
what can the regulator molecules be (allosteric regulation)
- allosteric inhibitors
- allosteric activators
what does allosteric inhibitors do
their binding produces a change of shape in the enzyme that stops enzyme activity; they act like an OFF switch
what does allosteric activators do
the shape change resulting from the binding produces an increase in enzyme activity; they act like an ON switch
what is feedback regulation
the end product of a metabolic pathway acts as an inhibitor of the key enzyme that catalyses the first step in a pathway.
what is photosynthesis
the process by which plants use the radiant energy of sunlight trapped by chlorophyll to build carbohydrates (glucose) from carbon dioxide and water.
what is the photosynthesis equation
6 carbon dioxide + 6 water = glucose + 6 oxygen (gas)
what are the 2 stages of photosynthesis
- light-dependent stage
- light-independent stage
what is the function of the light dependent stage
to transform sunlight energy that is captured by chlorophyll into the chemical energy of loaded coenzymes
what is the function of the light independent stage
to assemble simple inorganic carbon dioxide molecules into more complex organic glucose molecules
what is another name for the light independent stage
Calvin cycle
where does photosynthesis occur
chloroplasts, in the chlorophyll pigment inside (in the cytosol of plants)