Enzyme Kinetics and Inhibition 10/4 Flashcards
characteristics of enzymes
- cataylze chemical reactions without being consumed 2. very selective 3. products of natural selection
delta G less than 0
spontaneous reaction
delta G greater than 0
non-spontaneous reaction
enzyme catalysis reaction
E+S →[ES]→E+P
active site
has a shape that accomodates and complements the subtrate, including polarity and charge complentarily to the substrate transition state
to be an effective catalyst, should the enzyme bind tighter to the substrate or to the transition state?
the transition state! **this makes TS analogs good inhibitors of enzyme (for drugs)
kcat
the rate at which the ES complex converts to free enzyme and product. units: s-1
Km
the dissociation constant for the enzyme substrate complex. units=M
Vmax
the maximal value for an enzyme reaction
rate saturation equation
[E]0=[E]+{ES]
when [S] is low, the enzyme is mostly ________. how does v increase?
[E]
v increases proportionally to [S]
when [S] is high, the enzyme is mostly _____. how does v increase?
[ES]
v increases slowly in proportion to [S]
steady state enzyme kinetics equation
v=(Vmax[S])/Km+[S]
the upper limit of the forward reaction is
Kcat
carbonic anhydrase
catalyzes interconversion of carbon dioxide and bicarbonate