catalytic strategies

Question 1

what is an acid-base catalysis

Answer 1

An enzyme that accepts H + from hydronium and transfers it to an amino group of the substrate.
the result is an increase in the rate of release of the product. T

Question 2

what does carbonic anhydrase use?

Answer 2

acid-base catalysis
catalysis by approximation
metal ion catalysis

Question 3

what does serine proteases use?

Answer 3

acid-base catalysis
catalysis by approximation
covalent catalysis

Question 4

what does serine proteases contain?

Answer 4

a serine residue in their active site

Question 5

what does the catalytic triad of serine proteases contains:

Answer 5

serine, histidine and aspartic acid residues

Question 6

What metabolic type of reaction involves the addition of a functional group across a double bond or the removal of a functional group to form a double bond?

Answer 6

lyase

Question 7

what are the features of equilibrium of this reaction?
CO2 + H2O ⇌ H2CO3

Answer 7

• An increase in the concentration of CO 2 will result in a decrease of pH.
• The H2CO3 dissociates to H+ and bicarbonate ion, HCO3–.
• The majority of CO2 is transported to the lungs in the form of HCO3–.
• This reaction is catalysed by carbonic anhydrase.

Question 8

What is not an internationally accepted class of enzymes?

Answer 8

polymerase

Question 9

What metabolic type of reaction involves the cleavage of bonds by the addition of water?

Answer 9

hydrolysis

Question 10

What is the most predominant form for the transfer of carbon dioxide in the blood?

Answer 10

HCO3-

Question 11

what enzyme does carbonic anhydrase contains in its active site.

Answer 11

Zn2+ ion

Question 12

what does carbonic anhydrase do?

Answer 12

decreases the pKa of water