Exam 2 Flashcards
An enzyme that temporarily undergoes covalent catalysis as part of its mechanism
Chymotrypsin
The type of reaction catalyzed by proteases
Protein Breakdown
The inhibitor which binds only to the ES complex and lowers the Vmax and Km
Uncompetitive
The enzyme inhibition that can be overcome by increasing concentration of substrate
Competitive
The shape of the kinetic plot of an enzyme that exhibits cooperative binding
Sigmodial
An enzyme catalyst mechanism that uses anther molecule other than water to accept or donate a proton is what kind of catalytic strategy
General Acid-Base
The sulfa drug, sulfanilamide, is what kind of inhibitor
Competitive
What kind of inhibitor would you NOT have if you find out drug inhibition decreases when substrate concentration increased
Uncompetitive or Noncompetitive
An uncompetitive inhibitor will have two_______ lines on a double reciprocal plot
Parallel
Inhibitor which binds irreversible to the active site of an enzyme
Suicide
Stabilizes the intermediate of the hydrolysis of a peptide bond to chymotrypsin
NH groups
A ____________ inhibitor has a structure similar to the substrate and reversibly binds to the active site of the enzyme
Competitive
Which three amino acids in chymotrypsin are found in the active site and play the most critical role in catalysis
Ser
His
Asp
The mechanism of chymotrypsin involves the formation of an unstable _______-shaped intermediate that is stabilized by the oxyanion hole
Tetrahedral
This is the organic portion of the heme group in hemoglobin
Protoporphyrin
This type of hemoglobin is composed of two alpha chains and two y chains
Fetal
This type of binding is indicated by a sigmoidal-shaped binding curve
Cooperative
This condition is a result of a single point mutation in the beta chain of hemoglobin
Sickle cell anemia
Under normal conditions, the heme iron in myoglobin and hemoglobin is in the_________ oxidation state
Ferrous
Fe2+
The ability of myoglobin to bind oxygen depends on the presence of a bound prosthetic group called
Heme
In hemoglobin, the iron of the heme is bonded to the four nitrogens of porphyrin and to the proximal_______ residue of the global chain
Histidine
The binding of 2-3-bisphosphogycerate to hemoglobin___________ its affinity of oxygen binding
decreases
The effects of pH on oxyge-binding of hemoglobin is referred to as the
Bohr effect
Carbon dioxide reacts with the amino terminal groups of hemoglobin to form carbamate groups which carry a _______ charge
Negative
The T-state of hemoglobin is stabilized by a salt bridge between beta1 Asp 94 and the C-terminal __________ of the beta1 chain
Histidine
In normal adult hemoglobin, HbA, the beta6 position is a glutamate residue, whereas in sickle cell hemoglobin, HbS, it is a ________ residue
Valine
As the pressure of carbon increases, the affinity of oxygen binding to hemoglobin ________
Decreases
2,3-Bisphosphoglcerate binds only to the ________ form of hemoglobin
Deoxy
This is the chemical form in which most of the carbon dioxide is transported in the blood
Bicarbonate
HCO3-