920 cards
A Michaelis-Menten curve is ____.
____ is the substrate concentration that gives you a reaction rate that is halfway to V max
K m is the ____ that gives you a reaction rate that is halfway to V max
K m is the substrate concentration that gives you ____
____ is the maximum rate at which an enzyme can catalyze a reaction.
V max is the ____ at which an enzyme can catalyze a reaction.
V max is the maximum rate at which ____
The Michaelis–Menten equation is:
The ____ equation is:
Cooperative enzymes display a ____ curve.
____ enzymes display a sigmoidal curve.
____ is when the binding of the first molecule of B to A changes the binding affinity of the second B molecule, making it more or less like…
Cooperative binding is when ____.
The ____ is the site of catalysis .
The active site is the site of ____
The ____ states that the enzyme and substrate are exactly complementary and fit together like a key into a lock.
The ____ states that the enzyme and substrate undergo conformational changes in order to interact fully.
A/an ____ is a metal cation that is required by some enzymes.
A/an cofactor is a ____ that is required by some enzymes.
A/an ____ is an organic molecule that is required by some enzymes.
A/an coenzyme (type of cofactor) is ____ that is required by some enzymes.
____ of an enzyme is when an enzyme is inhibited by high levels of a product from later in the same pathway .
Feedback inhibition of an enzyme is when an enzyme is inhibited by ____ .
A/an ____ binds at the active site and thus prevents the substrate from binding.
A/an competitive inhibitor binds at the ____.
A/an ____ binds only with the enzyme-substrate complex .
A/an uncompetitive inhibitor binds ____ .
A/an ____ binds at the allosteric site , away from the active site.
A/an noncompetitive inhibitor binds at the ____.
In competitive inhibition : V max : ____.
In ____ inhibition : V max : has no change. K m : goes up.
In uncompetitive inhibition : V max : ____.
In ____ inhibition : V max : goes down. K m : goes down.
In noncompetitive inhibition : V max : ____.
In ____ inhibition : V max : goes down. K m : has no change.
Lineweaver-Burk Plot : X-intercept = ____.
This graph shows the activity of a/an ____.
This graph shows the activity of a/an ____.
This graph shows the activity of a/an ____.
Lineweaver-Burk plots are described as double reciprocal plots because the X -intercept is ____; both of them reciprocals.
Lineweaver-Burk plots are described as ____.
Lineweaver-Burk plots are described as double reciprocal plots because the ____ -intercept is 1/V max ; both of them reciprocals.
An irreversible inhibitor is any inhibitor that ____e site of some enzyme, thus eliminating its activity.
____ inhibitor is any inhibitor that covalently binds to the active site of some enzyme, thus eliminating its activity.
____ is an irreversible form of enzyme inhibition that occurs when an enzyme binds a substrate analog and forms an irreversible complex .
Suicide inhibition is ____.
A/an ____ binds at the allosteric site and induces a change in the conformation of the enzyme so the substrate can no longer bind to the ac…
A/an allosteric effector binds at the ____ .
A/an ____ is an allosteric regulator that is also the substrate .
A/an homotropic effector is ____ .
A/an ____ is an allosteric regulator molecule that is different from the substrate .
A/an heterotropic effector is ____ .
____ is the chemical addition of a phosphoryl group (PO 3 - ) to an organic molecule.
Phosphorylation is the chemical addition of a ____ to an organic molecule.
____ is the chemical addition of a carbohydrate .
Glycosylation is the chemical addition of a ____.
____ are precursors to an enzyme .
Zymogens are ____ .
The Michaelis-Menten reaction scheme is:
____ compose the cytoskeleton , anchoring proteins , and much of the extracellular matrix .