DAT Bio Flashcards
Gibbs FE Formula
delt G = delt H - t delt S
cell metabolism
the sum of all chemical reactions in a cell
(metabolism= catabolism + anabolism + energy transfer)
Catabolism:
the breakdown of complex molecules into
simpler molecules. Releases energy which can drive
anabolic pathways
Anabolism:
the synthesis of complex molecules from
simpler ones, using energy
3 Laws of thermodynamics:
- Energy cannot be created or destroyed – only
transferred and transformed - Entropy of closed systems tends to increase over
time.
a. Livings organisms are not closed systems, so
they can become more ordered (decreased
entropy) over time by increasing disorder in
their surroundings - Entropy minimizes as a system approaches absolute
0 Kelvin
Substrate:
the molecule that an enzyme acts on
Active site:
the location on the enzyme where the
substrate binds. The shape of the active site
determines the enzyme’s substrate specificity (i.e. what
molecules it can interact with)
Cofactors:
nonprotein structures that assist enzymes in
their function. Can bind permanently or reversibly.
Ribozymes:
RNA molecules with enzymatic function
Vmax:
maximum rate of a reaction
Vmax increases as
the amount of substrate increases.
- Limited by enzyme saturation (increasing enzyme
concentration also increases Vmax)
1/2 vmax
half of the max rate
Km (Michaelis Constant):
the concentration of substrate
at 1⁄2 Vmax. Inversely proportional to substrate binding
affinity (how well the enzyme binds to a substrate)
Small Km:
high binding affinity; less substrate
needed to saturate the enzyme
Large Km:
low binding affinity; more substrate
needed to saturate the enzyme
Competitive Inhibition:
inhibitor reversibly binds to
the active site. Can be overcome by increasing
substrate concentration.
Non-Competitive Inhibition:
the inhibitor binds to the
enzyme at a location other than the active site. Cannot
be overcome by increasing substrate concentration.
- Vmax decreases, Km is unaffected