Exam 2 Flashcards Preview

BIO 600 > Exam 2 > Flashcards

Flashcards in Exam 2 Deck (74)
Loading flashcards...
1

An enzyme that temporarily undergoes covalent catalysis as part of its mechanism

Chymotrypsin

2

The type of reaction catalyzed by proteases

Protein Breakdown

3

The inhibitor which binds only to the ES complex and lowers the Vmax and Km

Uncompetitive

4

The enzyme inhibition that can be overcome by increasing concentration of substrate

Competitive

5

The shape of the kinetic plot of an enzyme that exhibits cooperative binding

Sigmodial

6

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

7

The sulfa drug, sulfanilamide, is what kind of inhibitor

Competitive

8

What kind of inhibitor would you NOT have if you find out drug inhibition decreases when substrate concentration increased

Uncompetitive or Noncompetitive

9

An uncompetitive inhibitor will have two_______ lines on a double reciprocal plot

Parallel

10

Inhibitor which binds irreversible to the active site of an enzyme

Suicide

11

Stabilizes the intermediate of the hydrolysis of a peptide bond to chymotrypsin

NH groups

12

A ____________ inhibitor has a structure similar to the substrate and reversibly binds to the active site of the enzyme

Competitive

13

Which three amino acids in chymotrypsin are found in the active site and play the most critical role in catalysis

Ser
His
Asp

14

The mechanism of chymotrypsin involves the formation of an unstable _______-shaped intermediate that is stabilized by the oxyanion hole

Tetrahedral

15

This is the organic portion of the heme group in hemoglobin

Protoporphyrin

16

This type of hemoglobin is composed of two alpha chains and two y chains

Fetal

17

This type of binding is indicated by a sigmoidal-shaped binding curve

Cooperative

18

This condition is a result of a single point mutation in the beta chain of hemoglobin

Sickle cell anemia

19

Under normal conditions, the heme iron in myoglobin and hemoglobin is in the_________ oxidation state

Ferrous
Fe2+

20

The ability of myoglobin to bind oxygen depends on the presence of a bound prosthetic group called

Heme

21

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

22

The binding of 2-3-bisphosphogycerate to hemoglobin___________ its affinity of oxygen binding

decreases

23

The effects of pH on oxyge-binding of hemoglobin is referred to as the

Bohr effect

24

Carbon dioxide reacts with the amino terminal groups of hemoglobin to form carbamate groups which carry a _______ charge

Negative

25

The T-state of hemoglobin is stabilized by a salt bridge between beta1 Asp 94 and the C-terminal __________ of the beta1 chain

Histidine

26

In normal adult hemoglobin, HbA, the beta6 position is a glutamate residue, whereas in sickle cell hemoglobin, HbS, it is a ________ residue

Valine

27

As the pressure of carbon increases, the affinity of oxygen binding to hemoglobin ________

Decreases

28

2,3-Bisphosphoglcerate binds only to the ________ form of hemoglobin

Deoxy

29

This is the chemical form in which most of the carbon dioxide is transported in the blood

Bicarbonate
HCO3-

30

The HIV envelope is coated with what class of biomolecules

Carbohydrates