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Biochem > Enzyme Kinetics > Flashcards

Enzyme Kinetics Flashcards

1
Q

For competitive inhibition, the y-intercept is ____ and the slope is _____.

A

same; different

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2
Q

an enzyme is specialized to catalyze a particular type of biochemical reaction, but it is not highly selective regarding the specific substrate involved.

A

reaction specificity

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3
Q

A low value of Km indicates that the enzyme has ____ affinity with the substrate.

A

high

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4
Q

The net effect of _____ is a reduced value of Vmax while K’m is unaffected

A

non-competitive inhibition

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5
Q

At relatively high substrate concentration, the reaction rate is ____ order.

A

zero

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6
Q

ability of the enzyme to enhance the rate of a chemical reaction

A

catalytic power

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7
Q

ability of an enzyme to select a specific substrate from a range of competing substrates and molecules with similar structures.

A

specificity

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8
Q

an enzyme can bind to different substrate that have similar molecular geometry and size, thus specificity is very low.

A

geometrical specificity

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9
Q

substrate-binding site: ____ subunit
effector-binding site: ____ subunit

A

C-subunit or catalytic subunit; R-subunit or regulatory subunit

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10
Q

In allosteric enzyme, the rate of reaction decreases with the presence of a _____

A

effector

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11
Q

A specific type of enzyme that facilitates the activity of biological pathways whose products may be needed in different amounts at different times

A

regulatory enzyme

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12
Q

In reaction specificity, an enzyme is specific to a particular reaction but not to the ____ and catalyzes only one type of reaction.

A

substrate

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13
Q

Cofactor = ____ ions
Coenzyme = ____ molecules

A

inorganic, organic

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14
Q

The kinetic of allosteric enzymes fit the ____ growth curve.

A

sigmoidal

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15
Q

enzymes act upon a particular functional group present in a range of different substrates, rather than being strictly specific to a particular substrate molecule.

A

group specificity

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16
Q

In the concerted model, when KT is infinite, the factor c is ____

A

zero

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17
Q

enzyme recognizes and interacts on more than one substrate that contain a specific type of chemical bond or linkage

A

bond specificity

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18
Q

defined as the ratio of the concentration of occupied receptor to total receptor concentration

A

Hill constant

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19
Q

type of regulation uses effector does not act as a substrate and often has a different identity to the substrate needed to start the enzyme reaction

A

Heterotropic Regulation

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20
Q

In the quasi-steady state assumption, initial substrate concentration is ___ initial enzyme concentration.

A

greater than

21
Q

enzyme is not only specific to substrate but also to its optical configuration or chirality

A

stereo/optical specificity

22
Q

If n > 1: ____ cooperativity
If n < 1: ____ cooperativity

A

positive, negative

23
Q

The reaction order in the substrate diminishes continuously from _____ to ____ order

A

first; zero

24
Q

It refers to when enzymes can hold substrate such that the reaction substrates are closer to each other.

A

Proximity

25
Q

an enzyme can catalyze one reaction with only one specific substrate, and it cannot recognize or bind to any other substrate, regardless of their structural similarities.

A

absolute substrate specificity

26
Q

In the substrate concentration-rate of reaction graph, a plateau happens because the enzyme is ____

A

saturated

27
Q

Specificity is derived from the formation of many _____ interaction between enzyme substrate molecule.

A

weak

28
Q

as the T and R ratio _____, the growth kinetic curve becomes more sigmoidal in shape

A

increases

29
Q

Uncompetitive inhibition causes a ____ in both Vmax and Km

A

decrease

30
Q

______ inhibitors increase K’m but they do not affect Vmax

A

Competitive inhibitors

31
Q

type of regulation uses an effector that acts as both a substrate and a regulatory molecule

A

Homotropic Regulation

32
Q

enzymes require certain types of co-factors or coenzymes for their catalytic activity

A

cofactor specificity

33
Q

This phenomenon is generally attributed to the
formation of an unproductive enzyme–substrate complexes

A

substrate inhibition

34
Q

Stereo specificity is also called _____ specificity

A

optical

35
Q

The rate of reaction is ____ to the total amount of enzyme present.

A

proportional

36
Q

ratio of the rate of the enzyme-catalyzed reaction to the rate of the uncatalyzed (non-enzymatic) reaction

A

catalytic power

37
Q

enzyme acts on a range of similar substrates, rather
than being strictly specific to one particular substrate.

A

relative substrate specificity

38
Q

Competitive inhibitors bind to ____ but not to ____

A

free enzyme, enzyme-substrate complex

39
Q

As c increases, the difference in the binding affinity between T- and R-states ____, and the growth kinetics resemble more of a hyperbolic curve

A

decreases

40
Q

Two Types of Regulatory Enzymes

A

Covalently-Modulated/Modified Enzymes; allosteric enzymes

41
Q

Binding of inhibitor to one subunit induces a change in the other subunits to a form with _____ affinity for the substrate.

A

lower

42
Q

It is the ability of an enzyme to recognize and work with a particular substrate while ignoring others that
are not its intended targets.

A

Substrate specificity

43
Q

enzymes can interact with and catalyze a wide range
of substrates that are structurally related

A

broad substrate specificity

44
Q

For mixed non-competitive inhibition, KAI is ____ to KCI

A

equal

45
Q

Rapid equilibrium and quasi-steady-state may become identical if k-1 is ____ k2.

A

greater

46
Q

____ equation is primarily used to describe the cooperative binding of ligands

A

Hill

47
Q

The rate of reaction is proportional to the amount of ____ present.

A

enzyme

48
Q

For uncompetitive inhibition, the y-intercept is _____ and the slope is _____

A

different, same

Biochem (4 decks)

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