Enzymes And Biological Reactions Flashcards

(30 cards)

1
Q

Enzymes structure

A

Globular proteins, tertiary structure

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2
Q

Structure bonds in enzymes

A

Hydrogen, Ionic, Disulphide

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3
Q

Functions of enzymes

A

Biological catalysts- speed up rate of reaction. Reusable (unchanged). Specific

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4
Q

Name the model where the substrate is complementary to the active site

A

Lock and key model

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5
Q

Name the model where the substrate doesn’t fit the active site

A

Induced fit model. Enzymes slightly alters shape of active site putting strain on the bonds wearing and lowering the EA of the reaction

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6
Q

What is activation energy? How do enzymes affect it?

A

Energy needed for a reaction to take place. Enzymes lower the AE- less energy needed to react.

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7
Q

What is the turnover number?

A

The max. number of molecules of substrate that can be converted to product per unit time

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8
Q

5 factors that affect enzyme activity

A

1) pH 2) temperature 3) substrate conc. 4) enzyme conc. 5) presence of inhibitors

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9
Q

What is an anabolic reaction?

A

small+small=large molecule (condensation reactions- producing larger molecules)

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10
Q

What is a Catabolic reaction?

A

Breaking down of larger molecules to smaller ones

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11
Q

What are intracellular enzymes?

A

Inside the cell (e.g. breakdown of glucose to ATP)

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12
Q

What are extracellular enzymes?

A

Released to work outside the cell (e.g. digestive enzymes)

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13
Q

3 ways to measure enzyme activity

A

1) time taken for reaction. 2) rate of reaction (1/time). 3) concentration of products formed

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14
Q

How do you plot a graph (axis)?

A

x axis= whatever you CHANGED. y axis= whatever you MEASURED

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15
Q

How does temperature effect enzyme conc?

A

Increased temp= more KE= more successful collision= more ESC. Above optimum= denatured (bonds broken, shape altered)

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16
Q

How does pH effect enzyme conc?

A

Optimum= charge of active site complimentary to charge of substrate. Small change= R groups repel= less ESC (can be reversed). Extreme change= denatured. pH buffers neutralise pH

17
Q

How does changing substrate conc. effect enzyme conc?

A

No. of ESC increases with substrate conc. More KE= more collisions. Levels off as active sites fill (enzyme conc= limiting)

18
Q

How does changing enzyme conc. effect enzyme conc?

A

Increased enzyme conc= increased RoR- excess of substrate so always collisions and ESC

19
Q

Source of industrial enzymes

A

Obtained from microorganisms e.g. fungi & bacteria. Grown in fermenters, reproduce rapidly, produce enzymes as part of usual metabolic activity

20
Q

What is an immobilized enzyme?

A

When an enzyme us fixed to an inert, insoluble matrix

21
Q

Four methods of immobilization

A

1) enzyme inclusion 2) cross linked enzyme 3) carrier bound enzyme 4) microcapsule

22
Q

Method: enzyme inclusion

A

entrapment in a cellulose mesh

23
Q

Method: cross linked enzyme

A

chemically bonded cross linked by glutaraldehyde

24
Q

Method: carrier bound enzyme

A

Adsorption onto inert material e.g. glass beads/ clay particles

25
Method: microcapsule
encapsulation in alginate beads
26
5 advantages of immobilized enzymes
1) reusable- lower costs. 2) not contaminated. 3) microenvironment means more stability at higher temps/ pH. 4) continuous. 5) several enzymes at once
27
5 disadvantages of using immobilized enzymes
1) enzyme can detach and contaminate. 2) takes time to diffuse through gel. 3) gel can alter active site shape. 4) expensive and complex. 5) contamination is expensive
28
How does a competitive inhibitor work?
similar shape to active site- blocks substrate. reversed by increasing substrate conc
29
How does an non-competitive inhibitor work?
DO NOT COMPETE FOR ACTIVE SITE. attach to allosteric site and distort shape of active site
30
How are biosensors used?
medical diagnosis. detect specific molecule in a mixture (immobilized enzymes) works as enzymes are specific