UNE BIOCHEM UNIT 1
Domains are common structural elements that retain a particular function within
the protein. Give an example fo a protein domain.
An arrangement of Beta-strands connected by a-helices (BaBaBa)
Define what a protein domain is
A section os a protein structure sufficient to perform a particular chemical or physical
task
Chymotrypsin is a protease that cleaves peptide bonds. It is characterized as
which of the following classes of enzymes?
Hydrolases
Hemoglobin bound to heme is termed a holoprotein. The heme or porphyrin ring
is required for oxygen binding and it is defined as which group?
prosthetic group
1. Covalent catalysis is used by many enzymes to cleave peptide bonds. Which
amino acid would not facilitate this type of catalysis? (Think of the structure of
the R-Group of these amino acids)
Valine
How do most enzymes reduce the activation energy needed to move a reaction
forward?
Providing an active site most complementary the transition state
Prosthetic groups are complex non protein molecules that participate in catalysis
by providing functional groups that form a covalent intermediate between the
enzyme and the substrate. Give an example of a coenzyme or cofactor that
participates in the covalent catalysis reaction.
Pyridoxal phosphate
1. Movement of ammonia from an amino acid to an a-keto acid involves a family
of enzymes best categorized as?
Transferases
a. The green line shows enzyme kinetics with the addition of a noncompetitive
inhibitor
In the mage shown the blue line indicates enzyme kinetics with no inhibitor present.
Based on this information which of the following is true?
a. The green line shows enzyme kinetics with the addition of a noncompetitive inhibitor
b. The red line shows enzyme kinetics with the addition of a non competitive inhibitior
c. The green line shows enzyme kinetics with the addition of a competitive inhibitor
d. More information is needed regarding the addition of an inhibitor
c. It reduces the catalytic activity of the enzyme
A 28-year-old male is recently diagnosed with HIV. As part of his treatment he is
prescribed Nevirapine which interfered with retroviral reverse transcriptase enzyme.
Using the graph below, which of the following best describes the impact of this drug on
its target?
a. It increases the Km of its substrate
b. It decreases the Km of its substrate
Domains are common structural elements that retain a particular function within
the protein. Give an example fo a protein domain.
An arrangement of Beta-strands connected by a-helices (BaBaBa)
Define what a protein domain is
A section os a protein structure sufficient to perform a particular chemical or physical
task
Chymotrypsin is a protease that cleaves peptide bonds. It is characterized as
which of the following classes of enzymes?
Hydrolases
Hemoglobin bound to heme is termed a holoprotein. The heme or porphyrin ring
is required for oxygen binding and it is defined as which group?
prosthetic group
1. Covalent catalysis is used by many enzymes to cleave peptide bonds. Which
amino acid would not facilitate this type of catalysis? (Think of the structure of
the R-Group of these amino acids)
Valine
How do most enzymes reduce the activation energy needed to move a reaction
forward?
Providing an active site most complementary the transition state
Prosthetic groups are complex non protein molecules that participate in catalysis
by providing functional groups that form a covalent intermediate between the
enzyme and the substrate. Give an example of a coenzyme or cofactor that
participates in the covalent catalysis reaction.
Pyridoxal phosphate
1. Movement of ammonia from an amino acid to an a-keto acid involves a family
of enzymes best categorized as?
Transferases
a. The green line shows enzyme kinetics with the addition of a noncompetitive
inhibitor
In the mage shown the blue line indicates enzyme kinetics with no inhibitor present.
Based on this information which of the following is true?
a. The green line shows enzyme kinetics with the addition of a noncompetitive inhibitor
b. The red line shows enzyme kinetics with the addition of a non competitive inhibitior
c. The green line shows enzyme kinetics with the addition of a competitive inhibitor
d. More information is needed regarding the addition of an inhibitor
c. It reduces the catalytic activity of the enzyme
A 28-year-old male is recently diagnosed with HIV. As part of his treatment he is
prescribed Nevirapine which interfered with retroviral reverse transcriptase enzyme.
Using the graph below, which of the following best describes the impact of this drug on
its target?
a. It increases the Km of its substrate
b. It decreases the Km of its substrate
