Enzymes, intro to cellular respiration Flashcards
There are different forms of some enzymes that…
assist different reactions.
- cytosolic version of enzyme
- mitochondrial version of enzyme (ex slide 5 lecture 12)
Can enzymes work in forward and reverse directions?
Some enzymes can
activity
total amount of reactant converted to product (over time)
number of enzyme molecules
genes
activity of each enzyme molecule
pH, temperature etc.
concentrations of substrates
inhibitors and activators
inhibitors
molecules that interact in some way with the enzyme to prevent it from working in the normal manner
enzyme activator
molecules that bind to enzymes and increase their activity
factors that affect enzyme activity
cofactors
cofactors
nonprotein enzyme helpers coenzyme inorganic (such as a metal ionic form) -ex magnesium needed for hexokinase -forms complex with ATP
Coenzyme
organic cofactor
EX. vitamins
The regeneration of ATP
an organism at work us ATP continuously, but ATP is a renewable resource that can be regenerated by the addition of phosphate to ADP
what happens if the inhibitor attaches to the enzyme by covalent bonds?
inhibition is usually irreversible
Many enzyme inhibitors bind to the enzyme by weak interactions…
in which case inhibitions is reversible.
some reversible inhibitors resemble the normal substrate molecule…
and compete for admission into the active site
Competitive inhibitors
reduce the productivity of enzymes by blocking substrates from entering active sites
How can competitive inhibitors be overcome?
by increasing the concentration of substrate so that as active sites become available, more substrate molecules than inhibitor molecules are around to gain entry to the sites
noncompetitive inhibitors
do not directly compete with the substrate to bind to the enzyme at the active site. Instead they impede enzymatic reactions by binding to another part of the enzyme.
What does the noncompetitive inhibitors interaction cause?
This interaction cause the enzyme moleules to change its shape in such a way that the active site becomes less effective at catalyzing the conversion of substrate to product.
What does regulation of enzyme activity help?
helps control metabolism
Allosteric regulation
protein’s function at one site is affected by the binding of a regulatory molecule to a separate site.
allosteric activator
binds to the allosteric regulatory site
how can a substrate activate the enzyme?
by stabilizing it
feedback inhibition
When ATP allosterically inhibits an enzyme in an ATP generating pathway, the result is feed back inhibition
What happens in feedback inhibition?
a metabolic pathway is switched off by the inhibitory binding of its end product to an enzyme that acts early in the pathway.
certain cells use this five step pathway to synthesize the amino acid isoleucine from threonine…
as isoleucine accumulates, it slows down its own synthesis by allosterically inhibiting the enzyme for the first step of the pathway. feedback inhibition thereby prevents the cell from wasting chemical resources by making more isoleucine than is necessary
If the cell is not using products(isoleucine)….
…product of the pathway builds up
if the cell is using product (isoleucine)…
product of the pathways does not build up
-initial substrate can bind to active site
sites of enzyme activity
- cytoplasm/cytosol
- membranes
- plasma membrane
- endomembranes
- mitochondrial membrane,
- thylakoid membrane
how is sunlight a part of metabolism?
by converting the energy of sunlight to a usable form of chemical energy, photosynthesis is the source of virtually all metabolic energy in biological lsystems
major catabolic pathways- exergonic breakdown of organic molecules
- fermentation
- anaerobic respiration
- aerobic respiration-oxygen
- glycolysis
- Krebs cycle
- oxidative phosphorylation
Aerobic respiration
a form of cellular respiration that requires oxygen in order to generate energy
oxidized
glucose and other substrates are
“burned”