Week 2 Flashcards
(37 cards)
vi
the initial rate of the reaction at a certain substrate concentration
vmax
the maximal velocity a rxn can achieve at an infinite concentration of substrate
Km
substrate concentration at which the rxn rate is at half-max and is a measure of the substrate’s affinity for the enzyme
Michaelis-Menten Equation
vi = Vmax[S]/(Km+[S])
rate of rxns can be influenced by
temperature
H+ ion centration
competitive inhibitor
binds in the active site
competitive inhibitor impact of Km
increases it - substrate concentration must increase to compete with inhibitor
competitive inhibitor impact on Vmax
remains the same
do competitive inhibitors speed up or slow down the enzyme rxn
slow down
the impact of a competitive inhibitor can be overcome by
increase in substrate concentration
noncompetitive inhibitor
binds in an alternative location to the active site
impact of noncompetitive inhibitor on Vmax
Vmax decreased
impact of noncompetitive inhibitor on Km
remains the same
allosteric effectors
bind to sites that are not the active sites
allosteric activators
positive effectors
enhance enzyme rxn
stabilize a conformation of the protein that increases substrate binding and rxn rate - Rstate
allosteric inhibitors
negative effectors
inhibit enzyme rxn
stabilize a conformation of the protein that decreases binding of substrate and rxn rate
phosphorylation by a kinase on…
the R groups of serine and tyrosine and sometimes threonine
phosphorylations can…
- change protein comformation and activity
- change protein charge
kinases phosphorylate
serine and threonine
tyrosine kinases phosphorylate
tyrosine residues
protein phosphatases
hydrolyze the phosphoester bonds of phosphorseryl and phosphortyrosyl residues
methylation is typical in
c or g nucleotides
increased histone acetylation will result in
decreased histone:DNA interaction allowing for transcriptional accessibility
types of covalent modification
phosphorylation
hydrolyzation
methylation
acetylation