maltose and glycogen - ANSWER Alpha-1-4-linkages are present in:
chair and boat forms - ANSWER What is an example of a conformational
difference?
acetal - ANSWER The O-glycosidic bond linking two monosaccharide units is
equivalent to the bond found in a/an:
poly isoprenoids - ANSWER Which of the following classes of lipids include
some of the lipid-soluble vitamins?
they are saturated - ANSWER Which of the following is NOT true about trans
fatty acids?
prostaglandin - ANSWER What family of lipids has their synthesis is inhibited
by NSAIDs?
the base component can be degraded to produce energy in catabolic reactions -
ANSWER What is NOT a normal function of nucleic acids and nucleotides?
The bases are covalently bonded to the phosphates. - ANSWER What is not
true about DNA double helix?
hydrogen bonding - ANSWER Base pairing in DNA involves ___________
between purine and pyrimidine bases.
Competitive Inhibitors - ANSWER VMAX not affected,
KM Increased
Noncompetitive - ANSWER VMAX goes down
KM isn't affected
half vmax - ANSWER If the substrate concentration [S] is equal to the Km of
an enzyme, the reaction rate is:
, Transition state intermediate and enzyme - ANSWER Which pair is though to
have the tightest binding/association during enzyme catalysis?
Histidine - ANSWER In the catalytic triad of chymotrypsin, which amino acid
R-group is the closest to the catalytic serine residue?
acyl enzyme intermediate - ANSWER What is the name of the relatively stable
covalent intermediate in the chymotrypsin reaction?
Increase substrate concentration to very high levels - ANSWER How can
Vmax be approached despite the presence of a competitive inhibitor?
The initial reaction velocity nearly doubles - ANSWER 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 - ANSWER If enzyme concentration doubles, how is
Km affected?
Add moderate amount of a competitive inhibitor - ANSWER 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 - ANSWER What is TRUE about competitive and non-
competitive inhibitors?
low affinity for substrate and require high amounts of substrate to reach Vmax -
ANSWER Which of the following is true for an enzyme with a high Km?
Cysteine - ANSWER Iodoacetamide inactivates enzymes by covalently
modifying the R-group of:
Half are active and half are inactive - ANSWER If an enzyme is operating at
very high substrate levels, and an irreversible site specific inhibitor is added, so
that the reaction rate is reduced by 50%, what is TRUE about the resulting
condition of the enzyme and/or substrate?
chair and boat forms - ANSWER What is an example of a conformational
difference?
acetal - ANSWER The O-glycosidic bond linking two monosaccharide units is
equivalent to the bond found in a/an:
poly isoprenoids - ANSWER Which of the following classes of lipids include
some of the lipid-soluble vitamins?
they are saturated - ANSWER Which of the following is NOT true about trans
fatty acids?
prostaglandin - ANSWER What family of lipids has their synthesis is inhibited
by NSAIDs?
the base component can be degraded to produce energy in catabolic reactions -
ANSWER What is NOT a normal function of nucleic acids and nucleotides?
The bases are covalently bonded to the phosphates. - ANSWER What is not
true about DNA double helix?
hydrogen bonding - ANSWER Base pairing in DNA involves ___________
between purine and pyrimidine bases.
Competitive Inhibitors - ANSWER VMAX not affected,
KM Increased
Noncompetitive - ANSWER VMAX goes down
KM isn't affected
half vmax - ANSWER If the substrate concentration [S] is equal to the Km of
an enzyme, the reaction rate is:
, Transition state intermediate and enzyme - ANSWER Which pair is though to
have the tightest binding/association during enzyme catalysis?
Histidine - ANSWER In the catalytic triad of chymotrypsin, which amino acid
R-group is the closest to the catalytic serine residue?
acyl enzyme intermediate - ANSWER What is the name of the relatively stable
covalent intermediate in the chymotrypsin reaction?
Increase substrate concentration to very high levels - ANSWER How can
Vmax be approached despite the presence of a competitive inhibitor?
The initial reaction velocity nearly doubles - ANSWER 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 - ANSWER If enzyme concentration doubles, how is
Km affected?
Add moderate amount of a competitive inhibitor - ANSWER 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 - ANSWER What is TRUE about competitive and non-
competitive inhibitors?
low affinity for substrate and require high amounts of substrate to reach Vmax -
ANSWER Which of the following is true for an enzyme with a high Km?
Cysteine - ANSWER Iodoacetamide inactivates enzymes by covalently
modifying the R-group of:
Half are active and half are inactive - ANSWER If an enzyme is operating at
very high substrate levels, and an irreversible site specific inhibitor is added, so
that the reaction rate is reduced by 50%, what is TRUE about the resulting
condition of the enzyme and/or substrate?
