Topic 3: Enzyme Flashcards

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1
Q

Activation Energy

A

The energy that must be provided to make a reaction take place; enzymes reduce the activation energy required for a substrate to change into a product.

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2
Q

Active Site

A

An area on an enzyme molecule where the substrate can bind.

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3
Q

Allosteric

A

Other site.

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4
Q

ATPase

A

.

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5
Q

Buffer Solution

A

An aqueous solution consisting a mixture of weak acid and its conjugate base, or vice versa, which has a fixed pH value.

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6
Q

Cofactor

A

Other factor

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7
Q

Competitive Inhibition

A

When a substance reduces the rate of activity of an enzyme by competing with the substrate molecules for the enzyme’s active site; increasing the concentration of the substrate reduces the degree of inhibition.

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8
Q

Denaturation

A

Above a certain temperature, the structure of enzyme molecule vibrate so energetically that some of the bonds holding the enzyme molecule in its precise shape begin to break and the enzyme molecules begin to lose its shape and activity.

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9
Q

End-Product Inhibition

A

End products accumulate within the cell and stop the reaction when the sufficient product is made

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10
Q

Enzyme

A

a protein produced by a living organism that act as a biological catalyst in a specific reaction by reducing activation energy but remains unchanged at the end of the reaction.

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11
Q

Enzyme-Substrate Complex

A

The combined structure in which the substrate is held in place by temporary bonds which form between the substrate and some of the E groups of the enzyme’s amino acids

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12
Q

Extracellular

A

Enzymes that are secreted by cells and catalyse reaction outside the cell.

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13
Q

Feedback Mechanism

A

.

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14
Q

Immobilised Enzyme

A

Enzymes that have been fixed to a surface or within a bead of agar gel

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15
Q

Induced Fit Hypothesis

A

The substrate is complementary shape to the active site of the enzyme but the substrate is not an exact fit.
Enzyme or sometimes the substrate can change its shape in order to ensure a perfect fit for catalysis to occur.

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16
Q

Inhibitor

A

A substance that decrease or stop enzyme activity.

17
Q

Intracellular

A

Enzymes that operate within cells

18
Q

Irreversible Inhibitor

A

Inhibitors that damage the enzyme irreversibly leaving them permanently damaged.

19
Q

Lactose

A

Disaccharides that are found in milk

20
Q

Lock and Key Hypothesis

A

Enzyme has a particular fixed shape into which the substrate fits perfectly analogous to a key fitting into a lock.

21
Q

Lysozyme

A

An enzyme that damage the cell wall (made of polysaccharide chains) of bacterias by catalyse the hydrolysis

22
Q

Metabolic Reaction

A

All the reactions that take place in a living organism

23
Q

Michaelis-Menten constant, km

A

The substrate concentration at which an enzyme work at half it maximum rate (1/2 Vmax), used as a measure of the efficiency of an enzyme; the lower value of km, the more efficient the enzyme.

24
Q

Non-Competitive Inhibitor

A

A substance reduce the rate of activity of an enzyme by binding to another site of the enzyme rather than the active site.

25
Q

Optimum

A

The best possible result; the ideal result

The temperature at which an enzyme catalyse the reaction at the maximum rate

26
Q

pH

A

A measure of concentration of hydrogen ion in the solution

27
Q

Reversible Inhibitor

A

Enzyme inhibitors that do not damage the enzyme permanently and do not break the disulphide bond.

28
Q

Saturation

A

All the active site are bound to substrate to form an enzyme-substrate complex

29
Q

Substrate

A

Molecules that react in the enzyme catalysis reaction

30
Q

Theoretical Maximum Rate (Velocity), Vmax

A

The theoretical maximum rate of an enzyme controlled reaction, obtained when all of the active sites are occupied.

31
Q

Turnover Rate of Enzyme

A

The speed at which an enzyme can convert substrate into a product. A typical enzyme can convert around one thousand substrate molecules into product per second.