Complete by circling the correct choice Enzymes are most active at an optimum temperature (usually 37°36°C or 40°C or in humans). show little activity at low or high temperatures. lose activity at low or high temperatures as denaturation occurs. are most active at optimum pH of 7, 8, or 5.5 An increase in enzyme concentration increases /decrease the rate of reaction (at constant substrate concentration). The rate of reaction vs enzyme concentration is linear or non-linear The rate of reaction vs substrate concentration is linear or non-linear

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Chapter20: Enzymes
Section: Chapter Questions
Problem 20.50E
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Complete by circling the correct choice
Enzymes
are most active at an optimum temperature (usually
37°C, 36°C or 40°C or in humans).
show little activity at low or high temperatures.
lose activity at low or high temperatures as
denaturation occurs.
are most active at optimum pH of 7, 8, or 5.5
An increase in enzyme concentration
increases /decrease the rate
of reaction (at
constant substrate concentration).
The rate of reaction vs enzyme concentration is linear
or non-linear
The rate of reaction vs substrate concentration is
linear or non-linear
Sucrase has an optimum temperature of 37°C and an
optimum pH of 6.2.
Determine the effect of the following on its rate of
reaction: 1) no change 2) increase
decrease
3)
A. increasing the concentration of sucrase
B. changing the pH to 4.0
C. running the reaction at 70°C
What are the functions of Allosteric enzymes
What are some factors that affects enzyme activity?
I.
II.
IV.
III. Trypsin catalyzes the removal of dipeptides from
inactive chymotrypsinogen and trypsinogen to
give the active proteases chymotrypsin and
trypsin. T/F
V.
Enzyme activity can be regulated by allosteric
enzymes, feedback control, and covalent
modifications. T/F
VI.
Examples of Zymogens are the proteases
trypsinogen and chymotrypsinogen. T/F?
The removal of a polypeptide chain from
proinsulin produces the active form of insulin.
T/F?
A kinase can activate an inactive enzyme by
phosphorylation, ie adding a phosphate group.
T/F?
A phosphatase can activate an inactive enzyme
by removal of phosphate. T/F?
Identify each description of an inhibitor that is either
competitive or noncompetitive.
A. Increasing substrate reverses inhibition.
B.
It binds to the enzyme's surface
but not to the active site.
C. Its structure is similar to that of
the substrate.
D. Inhibition is not reversed by adding
more substrate.
What are the types of Reversible inhibition?
What are properties of Reversible inhibitors?
For example, they cause a loss of enzyme activity
that can be restored.
Transcribed Image Text:Complete by circling the correct choice Enzymes are most active at an optimum temperature (usually 37°C, 36°C or 40°C or in humans). show little activity at low or high temperatures. lose activity at low or high temperatures as denaturation occurs. are most active at optimum pH of 7, 8, or 5.5 An increase in enzyme concentration increases /decrease the rate of reaction (at constant substrate concentration). The rate of reaction vs enzyme concentration is linear or non-linear The rate of reaction vs substrate concentration is linear or non-linear Sucrase has an optimum temperature of 37°C and an optimum pH of 6.2. Determine the effect of the following on its rate of reaction: 1) no change 2) increase decrease 3) A. increasing the concentration of sucrase B. changing the pH to 4.0 C. running the reaction at 70°C What are the functions of Allosteric enzymes What are some factors that affects enzyme activity? I. II. IV. III. Trypsin catalyzes the removal of dipeptides from inactive chymotrypsinogen and trypsinogen to give the active proteases chymotrypsin and trypsin. T/F V. Enzyme activity can be regulated by allosteric enzymes, feedback control, and covalent modifications. T/F VI. Examples of Zymogens are the proteases trypsinogen and chymotrypsinogen. T/F? The removal of a polypeptide chain from proinsulin produces the active form of insulin. T/F? A kinase can activate an inactive enzyme by phosphorylation, ie adding a phosphate group. T/F? A phosphatase can activate an inactive enzyme by removal of phosphate. T/F? Identify each description of an inhibitor that is either competitive or noncompetitive. A. Increasing substrate reverses inhibition. B. It binds to the enzyme's surface but not to the active site. C. Its structure is similar to that of the substrate. D. Inhibition is not reversed by adding more substrate. What are the types of Reversible inhibition? What are properties of Reversible inhibitors? For example, they cause a loss of enzyme activity that can be restored.
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