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PRINCIPLES > Biochemistry - Enzymes as Biological Catalysts > Flashcards

Biochemistry - Enzymes as Biological Catalysts Flashcards

1
Q

What is the function of an enzyme?

A

Enzymes CATALYSE specific reactions which make up a metabolic process. Impact on health and disease.

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2
Q

What does an enzyme do with regard to Equilibrium?

A

An enzyme speeds up the rate at which equilibrium is achieved.

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3
Q

What do enzymes NOT affect?

A

The POSITION of EQUILIBRIUM in a reaction.

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4
Q

Enzymes are … to to their substrates.

A

SPECIFIC.

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5
Q

What are enzymes? MESP

A

Mostly Protein
Efficient
Specific
Potent

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6
Q

Enzymes - M

A

Mostly Protein

e.g. RNA - ribozymes

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7
Q

Enzymes - E

A

Efficient
Can increase rate by a factor of 1020.
Can work at various temperatures.

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8
Q

At what temperatures can enzymes work at?

A

Enzymes can work at:

Body Temperature
Neutral pH
Acidic Conditions
Aqueous Solutions

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9
Q

Enzymes - S

A

Specific
They have a limited substrate range.
Can distinguish between STEREOISOMERISM.

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10
Q

Enzymes - P

A

Potent

Enzymes can convert many substrate molecules into product per second.

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11
Q

What is the Activation Energy?

Ea

A

The activation energy is the minimum energy required for a reaction to take place.

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12
Q

What intermediate product is produced in a reaction going from Substrate to Products?

A

TRANSITION STATE.

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13
Q

What is the Transition State?

A

An intermediate compound with the GREATEST FREE ENERGY in a reaction.

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14
Q

Explain the ‘Cocktail Party’ Analogy.

A

You are in a room full of people with the intention to meet the ‘right’ person. The greater the number of people, the greater the likelihood of meeting the person you’re looking for.

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15
Q

What effect do enzymes have on the Activation Energy?

A

Enzymes LOWER the Activation Energy.

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16
Q

How do enzymes lower the Activation Energy?

A

Enzymes lower the activation energy by providing alternative pathways for reactions.

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17
Q

What is Glycogen Storage Disease?

A

Enzyme Deficiency
Failure for Glycogen to enter “phosphorylated state”.
Can’t part-take in Glycolytic pathway.

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18
Q

Catalytic activity of enzymes depends on what?

A

Catalytic activity of enzymes depends on the presence of CO-ENZYMES and COFACTORS.

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19
Q

What are COFACTORS?

A

Cofactors are METAL IONS (inorganic).

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20
Q

What are CO-ENZYMES?

A

Co-enzymes are ORGANIC MOLECULES (organic organ).

21
Q

What is a METALLOPROTEIN?

A

A co-factor with a metal co-ordination centre in an enzyme.

22
Q

The association between an enzyme and a coenzyme is…

A

TRANSIENT

not permanent

23
Q

What happens to Co-Enzymes during the course of a reaction?

A

They may change shape/structure/charge but are regenerated.

24
Q

What is a PROSTHETIC GROUP?

A

A prosthetic group is a TIGHTLY BOUND CO-ENZYME.

25
Q

Name an example of PROSTHETIC GROUP.

A

Haem in Haemoglobin and Cytochromes.

26
Q

What is a APOENZYME?

A

An enzyme WITHOUT a COFACTOR.

27
Q

What is a HALOENZYME?

A

An enzyme WITH a COFACTOR.

Halo - circle - centre - with metal centre

28
Q

APOENZYME + COFACTOR =

A

HALOENZYME

29
Q

Examples of Cofactors include…

A

Zinc
Iron
Copper

30
Q

What is the function of metal ions? (2)

A

Stabilise Transition States

Involved in Redox Processes

31
Q

What are the functions of Co-enzymes?

A

Involved in Redox Processes (NAD+, FAD)

Involved in Group Transfer (CoA, ATP transfers PO3-)

32
Q

Where are many Co-enzymes derived from?

A

Vitamins.

33
Q

What do the symptoms of vitamin deficiencies reflect?

A

They reflect the loss of ENZYME ACTIVITIES.

34
Q

What is NAD?

A

Nicotinamide Adenine Dinucleotide (NAD)

35
Q

What does NAD+ go to?

A

NADH

36
Q

What do NAD and NADH do?

A

They donate and receive electrons.

Easily regenerated.

37
Q

Where does the substrate bind in an enzyme?

A

Substrate binds to the ACTIVE SITE.

38
Q

What is the INDUCED FIT?

A

The induced fit occurs when an active site changes conformation to bind more tightly to a substrate to increase likelihood of a reaction.

39
Q

Describe the Lock-and-Key Model.

A

The model illustrates that an enzyme’s active site is COMPLEMENTARY to the shape of the substrate.

40
Q

What is an Active Site?

A

A cleft/crevice.

41
Q

The Active Site contains …?

A

AMINO ACIDS

42
Q

What are the Amino Acids in an active site essential for? (2)

A

Catalytic Activity

Specific Interactions

43
Q

What two factors affect enzyme activity?

A

Temperature

pH

44
Q

What is an ISOZYME?

A

Isoforms of enzymes

Catalyse same reaction but have a different sequence of amino acids and different structure.

45
Q

What are ISOFORMS?

A

Several different forms of a protein.

Similar function to another protein but differing genes (slightly).

46
Q

What are examples of Active Sites?

A

Three pancreatic serine protases:
Chemotrypsin
Trypsin
Elastase

47
Q

When can different isozymes be synthesised?

A

Different isozymes can be synthesised during FOETAL and EMBRYONIC development.

48
Q

Where are isozymes present?

A

Isozymes are present in different TISSUES and CELLULAR LOCATIONS.

49
Q

Name an example of a tissue specific isoform.

A

Lactate Dehydrogenase

PRINCIPLES (8 decks)

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