Bio enzyme Flashcards
more complex
increases in G (free energy), more likely to fall apart
enzymes has ATP attached to it
the phosphate attaches to the substrate,
entropy
describes level of disorder
energy coupling
transfer of energy catabolism to anabolism
energy released in an reaction
is stored in bonds
38 ADP + 38P
38ATP
exergenic
catabolic
spontaneous
down
endergonic
anabolic
non-spontanous
up
cofactor
molecules that activate enzymes, at the active site with the substrate
ex. iron
increase enzyme concentration
increase rxn rate
increase of substrate
increase rxn rate until leveling out
max velocity, highest point
competitive enzyme inhibitor
block active site, not permanent
noncompetitive enzyme inhibitor
changes of shape of active sites, nonpermanent. binds at allosteric site
how to overcome activation energy
heat
enzyme
How does enzyme facilitate rxn to fall apart
- increase in complexity
- apply breaker
enzyme decrease energy input
add phosphate group to increase complexity and break it down faster
exogonic ex.
atp break down
endergonic ex.
protein synthesis
DNA replication
how enzyme lower Ea in endergonic
- align molecule
- stretch molecule (separation
enzyme specificity
enzyme only interact with specific substrate that has complimentary (opposite) charge and shape
induced fit model
decribes how enzyme binds/surrounds a substrate
allosteric regulation
only in quaternary
metabolic pathway
unnecessary molecules are made (3) until the 4th (needed) molecule is produced. 3 enzyme used.
Feedback inhibition
increase in 4th molecule, needs to lowe. stop production by using it to competive inhibit the first enzyme
