BIOC 3021 EXAM 2 QUESTIONS AND ANSWERS 2024/2025 | VERIFIED
maltose and glycogen - Alpha-1-4-linkages are present in:
chair and boat forms - What is an example of a conformational difference?
acetal - The O-glycosidic bond linking two monosaccharide units is the equivalent to the bond
found in a/an:
polyisoprenoids - Which of the following classes of lipids include some of the lipid soluble
vitamins?
they are saturated - Which of the following is NOT true about trans fatty acids?
prostaglandin - What family of lipids has their synthesis is inhibited by NSAIDS?
the base component can be degraded to produce energy in catabolic reactions - What is NOT a
normal function of nucleic acids and nucleotides?
The bases are covalently bonded to the phosphates. - What is not true about DNA double helix?
hydrogen bonding - Base pairing in DNA involves ___________ between purine and pyrimidine
bases.
Competitive Inhibitors - VMAX not affected,
KM Increased
Noncompetitive - VMAX goes down
KM isn't affected
, half vmax - If the substrate concentration [S] is equal to the Km of an enzyme, the reaction rate is:
Transition state intermediate and enzyme - Which pair is though to have the tightest
binding/association during enzyme catalysis?
Histidine - In the catalytic triad of chymotrypsin, which amino acid R-group is the closest to the
catalytic serine residue?
acyl enzyme intermediate - What is the name of the relatively stable covalent intermediate in the
chymotrypsin reaction?
Increase substrate concentration to very high levels - How can Vmax be approached despite the
presence of a competitive inhibitor?
The initial reaction velocity nearly doubles - For an enzyme with a Km of 10 uM, how does the
initial reaction velocity change if the substrate level is raised from 1 uM to 2 uM?
Km remains the same - If enzyme concentration doubles, how is Km affected?
Add moderate amount of a competitive inhibitor - If an enzyme reaction rate is approaching the
Vmax, with a large excess of substrate present, what would have the least effect on the rate of reaction?
Both can be reversible - What is TRUE about competitive and non-competitive inhibitors?
low affinity for substrate and require high amounts of substrate to reach Vmax - Which of the
following is true for an enzyme with a high Km?
Cysteine - Iodoacetamide inactivates enzymes by covalently modifying the R-group of:
maltose and glycogen - Alpha-1-4-linkages are present in:
chair and boat forms - What is an example of a conformational difference?
acetal - The O-glycosidic bond linking two monosaccharide units is the equivalent to the bond
found in a/an:
polyisoprenoids - Which of the following classes of lipids include some of the lipid soluble
vitamins?
they are saturated - Which of the following is NOT true about trans fatty acids?
prostaglandin - What family of lipids has their synthesis is inhibited by NSAIDS?
the base component can be degraded to produce energy in catabolic reactions - What is NOT a
normal function of nucleic acids and nucleotides?
The bases are covalently bonded to the phosphates. - What is not true about DNA double helix?
hydrogen bonding - Base pairing in DNA involves ___________ between purine and pyrimidine
bases.
Competitive Inhibitors - VMAX not affected,
KM Increased
Noncompetitive - VMAX goes down
KM isn't affected
, half vmax - If the substrate concentration [S] is equal to the Km of an enzyme, the reaction rate is:
Transition state intermediate and enzyme - Which pair is though to have the tightest
binding/association during enzyme catalysis?
Histidine - In the catalytic triad of chymotrypsin, which amino acid R-group is the closest to the
catalytic serine residue?
acyl enzyme intermediate - What is the name of the relatively stable covalent intermediate in the
chymotrypsin reaction?
Increase substrate concentration to very high levels - How can Vmax be approached despite the
presence of a competitive inhibitor?
The initial reaction velocity nearly doubles - For an enzyme with a Km of 10 uM, how does the
initial reaction velocity change if the substrate level is raised from 1 uM to 2 uM?
Km remains the same - If enzyme concentration doubles, how is Km affected?
Add moderate amount of a competitive inhibitor - If an enzyme reaction rate is approaching the
Vmax, with a large excess of substrate present, what would have the least effect on the rate of reaction?
Both can be reversible - What is TRUE about competitive and non-competitive inhibitors?
low affinity for substrate and require high amounts of substrate to reach Vmax - Which of the
following is true for an enzyme with a high Km?
Cysteine - Iodoacetamide inactivates enzymes by covalently modifying the R-group of:
