biology- cell & molec Flashcards
(178 cards)
catabolism
break down
anabolism
build up
oxidation
loss of electrons
more bonds to oxygen
reduction
gain of electrons
more bonds to hydrogens
enzymes
protein catalysts
Vmax
enzymes processing substrate as fast as they can
active site
site where enzyme binds
inhibitors
bind to wrong active sites that slow down reactions
competitive inhibition
inhibitor and substrate compete for the enzyme doesn't change vmax (rate) new Km (concentration) value increases
non-competitive inhibition
- inhibitor can bind to the enzyme at the binding site at the same time as the substrate but not to the active site
- doesn’t bind to active site but somewhere else
- binding happens but reaction doesnt
- vmax decreases
- km unchanged
- EI and EIS complexes enzymatically inactive
uncompetitive inhibition
inhibitor cannot bind to the free enzyme, only to the ES complex
the complex formed is enzymatically inactive
rare kind of inhibition
may happen in multimeric enzymes
mixed inhibition
like noncompetitive
EIS complex has residual enzymatic activity
does not follow the MIchaelis-Menten Equation
enzymes work by lowering the _____
activation energy and increase the rate of reaction
enzymatic catalyzed reactions form products faster, making reactions reach their ______ more rapidly
equilibrium
T/F enzymes are not conumed by the reactions they catalyze
true
how do enzymes differ from other catalysts
they are highly specific for their substrates due to their complementary shape, charge, and hydrophilic/hydrophobic characteristics
michaelis-menten equation
v=(vmax [S])/(km + [S])
cooperativity
when a substrate binds to one enzymatic sub-unit/binding site, which induces the rest of the subunits to be stimulated and become active
example of cooperativity
hemoglobin shows positive cooperativity for oxygen because it is more accepting to oxygen after one oxygen molecule binds
-transports 4 oxygen subunits while myoglobin only transports 1 subunit
what demonstrates cooperativity?
ligands
negative cooperativity
as ligands bind to the protein, the protein’s affinity for the ligand decreases
types of enzyme regulation
- allosteric
- phosphorylation
- zymogens
- cofactors
- association with other peptides
allosteric regulation
other molecules bind to enzyme in places other than active site
-ex: feedback inhibition
phosphorylation
adding a phosphate group
- covalent modification (make covalent bond)
- ser, thr, tyr residues can be phosphorylated by kinases (using ATP hydrolysis) or phophorylases
- phosphatases pull phosphate off
- phosphorylation can either activate or inhibit an enzyme depending upon the enzyme