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Biology > enzymes > Flashcards

enzymes Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

definition of active site

A

indented area on the surface of an enzyme molecule, with a shape that is complementary to the shape of a substrate molecule

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2
Q

catalyst definition

A

chemical that speeds up rate of reaction that remains unchanged and reusable at the end of a reaction

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3
Q

extracellular definition

A

outside the cell

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4
Q

intracellular definition

A

inside the cell

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5
Q

metabolic/metabolism definition

A

chemical reactions that take place inside the cell

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6
Q

product

A

molecule produced from the substrate molecules. from an enzyme-catalysed reaction

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7
Q

substrate

A

molecule that is altered by an enzyme-substrate reaction

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8
Q

What is a cofactor

A

Non protein compound required for enzymes activities to occur. Bind with enzymes and help.

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9
Q

What are the three types of cofactor

A

Coenzymes
Activators
Prosthetic groups

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10
Q

What are coenzymes

A

Organic cofactors
Do not bind permanently
Facilitate binding of substrate to enzyme
Many=vitamin derives

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11
Q

What is an activator

A

Inorganic metal ion
Temporarily bind to enzyme & alter active site

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12
Q

What is a prosthetic group

A

Cofactor
Permanently attached to enzyme
E.g haemoglobin

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13
Q

What is induced fit model

A

Structure of enzyme is altered so that the active site pf the enzyme fits around the substrate

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14
Q

How does enzyme conc affect reaction

A

RoR increases as EC increases bc there are more AS for substrates to bind to. However increasing EC beyond a certain point has no effect on RoR as there are more AS than S so SC becomes limiting factor

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15
Q

Effect of substrate conc on RoR

A

RoR increases as SC increases bc more ES complexes are formed. However beyond a certain point it has no effect on RoR as EC becomes limiting factor

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16
Q

Effect of temp on RoR

A

RoR increases up to the optimum temp. If T too high then they can denature as the hydrogen and ionic bonds break from vibration of atoms. This disrupts hydrophobic and hydrophilic interactions and the tertiary structure.

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17
Q

Enzyme definitiom

A

Biological catalysts that increase RoR by decreasing AE. Large globular proteins consisting of hundreds of amino acids. Have an active site which is specific to a substrate. Remain unchanged at the end of every reaction so can be reused.

18
Q

What is an inhibitor

A

Substance which slows down or stops a reaction by affecting the binding of substrate to be enzymes. Can be reversible or irreversible

19
Q

Describe irreversible inhibitors

A

Cause protein structure to break causing shape of AS to change, affecting protein activity. E.g cyanide

20
Q

Describe reversible inhibitors

A

Bind to AS by hydrogen bonds and weak ionic interactions. Can either be competitive or non competitive

21
Q

Describe competitive inhibitors

A

Reversible
Similar structure to substrate
Bind to AS, decrease activity (compete with substrate)
amount of product formed remains same but RoR decreases

22
Q

Describe non competitive inhibitor

A

Reversible
Does not bind to AS
Binds to another site on enzyme called ALLOSTERIC SITE
This changes shape of AS and prevents binding of substrate

23
Q

Example of inhibitors

A

Drugs e.g penicillin
Fights bacterial infection
Inhibitor of enzyme transpeptidace

24
Q

How do enzymes work

A

Substrate molecules bind with the complementary AS forming an ES complex. Enzyme catalyses the breakdown of the substrate into product forming EP complex

25
Q

Amylase, where found, optimum pH,

A

Saliva
pH 7

26
Q

What would happen to amylase if reacted with stomach acid

A

pH of stomach acid is too lw
Hydrogen bonds break
Disrupt tertiary structure
Change AS shape
Enzyme denatures.

27
Q

EQ relate protein tertiary structure to effect of pH and T on enzyme controlled reactions

A

Tertiary structure determines final 3D shape of proten as a result of bonding between R groups on different amino acids. This bonding is important because in tertiary structure there are different types of additional bonds that can determine resistance to temp and change in pH. Disulphide bond is a strong covalent bond resistant to extreme temperatures so enzymes with these bonds in tertiary structure
will be less effected by change in temp. However these disulphide bonds are uncommon. The most common bond in tertiary structure is the hydrogen bond
and this is weaker. Ionic bind is broken by pH changes.

28
Q

Amylase substrate

A

Starch

29
Q

Amylase product

A

Dextrin

30
Q

Amylase location

A

Saliva

31
Q

Amylase optimum pH

A

6.7-7

32
Q

Pepsin substrate

A

Protein

33
Q

Pepsin products

A

Peptides

34
Q

Pepsin location

A

Stomach

35
Q

Pepsin optimum pH

A

2.5

36
Q

Trypsin substrate

A

Peptide

37
Q

Trypsin product

A

Amino acids

38
Q

Trypsin location

A

Small intestine

39
Q

Trypsin optimum pH

A

7.5-8.5

40
Q

Saturated definition

A

Condition of enzyme AS at a high SC

41
Q

Anabolic vs catabolic

A

A=Synthesise larger molecules
C=breakdown larger molecules

Biology (13 decks)

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