Enzymes And Biological Reactions Flashcards

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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
Q

Method: microcapsule

A

encapsulation in alginate beads

26
Q

5 advantages of immobilized enzymes

A

1) reusable- lower costs. 2) not contaminated. 3) microenvironment means more stability at higher temps/ pH. 4) continuous. 5) several enzymes at once

27
Q

5 disadvantages of using immobilized enzymes

A

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
Q

How does a competitive inhibitor work?

A

similar shape to active site- blocks substrate. reversed by increasing substrate conc

29
Q

How does an non-competitive inhibitor work?

A

DO NOT COMPETE FOR ACTIVE SITE. attach to allosteric site and distort shape of active site

30
Q

How are biosensors used?

A

medical diagnosis. detect specific molecule in a mixture (immobilized enzymes) works as enzymes are specific