Upgrade to remove ads
BBMB 301 Exam 2/Chapters 7 and 8
Terms in this set (40)
A complex array of enzyme reactions organized in multiple pathways?
The study of rates of chemical reactions?
A reaction that is directly proportional to the concentration of reactant is a?
A reaction with two substrates is considered a _________ reaction?
At _________, there is no net change in the concentration of substrate or product.
The value V0 is called the _______?
The Kcat is often referred to as the?
An enzyme's affinity for its substrate is measured by the ______ constant?
Enzymes that do not obey Michaelis-Lenten kinetics?
Experiments that determine the kinetics of a population of enzyme molecules?
One way to measure the rate of an enzymatic reaction is to measure the loss of _________?
Reactions that have more two reactants or substrates are considered _______ reactions.
The _______ rule states that all subunits in an allosteric enzyme must be in either the T or the R state; there can not be hybrids.
The Michaelis-Menten model assumes that ________ is the rate constant ignored because product has not accumulated.
_______ is directly dependent on enzyme concentration.
near the Km
An enzyme will be most sensitive to changes in cellular concentration when the concentration is ______?
The type of inhibition by a product of one enzyme on another enzyme in an earlier protein in a metabolic pathway is considered a ________ inhibitor.
Allosteric enzymes can be identified because the plot of initial velocity, V0, vs. substrate concentrations, S, is not hyperbolic but _______ shaped.
An allosteric ________ stabilizes the T state of the enzymes.
The y-intercept of a Lineweaver-Burk plot is _______?
An enzyme that temporarily undergoes covalent catalysis as part of its mechanism.
The type of reaction catalyzed by proteases.
A protease enzyme with a low pH optimum.
The type of catalysis in which two substrates are brought into close proximity.
A molecule that is also known as a substrate analog.
The inhibitor which binds only to the ES complex and lowers the Vmax and Km.
The enzyme inhibitor that can be overcome by increasing the concentration of substrate.
Approximation and Orientation
A type of catalysis where the proton donor is not water.
A type of enzyme inhibitor where Km is unaltered.
An enzyme that is part of a pigment formation pathway and has a low optimum temperature.
Metal Ion Catalyst
An enzyme catalyst mechanism that uses a metal cation to stabilize a negative charge in the active site is?
Catalysis by Approximation and Orientation
A _______ catalytic mechanism that forces two substrates into an appropriate 3-D arrangement for the rxn to occur.
The antibiotic penicillin is an example of a ________ inhibitor.
In conducting an experiment with a new drug, you find that regardless of the concentration of substrate, the drug is able to inhibit the enzyme activity. You are likely to not have a ____ type of inhibitor.
An uncompetitive inhibitor will have two _____ lines on a double-reciprocal plot.
A ____ inhibitor binds irreversibly to the active site of an enzyme.
The ______ stabilizes the tetrahedral intermediate of the hydrolysis of a peptide bond by chymotrypsin.
A ______ inhibitor has a structure similar to the substrate and reversibly binds to the active site of the enzyme.
Lineweaver-Burk plot/ double-reciprocal plot
The straight-line kinetic plot a 1/V0 vs. 1/S is called ____.
The mechanism of chymostrypsin involves the formation of an unstable ______- shaped intermediate that is stabilized by the oxyanion hole.
THIS SET IS OFTEN IN FOLDERS WITH...
Biochem exam 2
BIOCHEM QUIZ 3
Biochemistry Quiz Bank (Exam 2)
Biochem Exam 2
YOU MIGHT ALSO LIKE...
Chapter 7: Enzymatic Kinetics & Regulation
7. BBMB 301 Study Questions
Enzyme kinetics ch. 6
OTHER SETS BY THIS CREATOR
MNT 464: Lower GI Tract Terms
what did I get myself into.
FS HN 342 Quiz 1
GRE: Vocab. Group 1