Enzymes Flashcards

1
Q

Diverse group of water-insoluble biological molecules; fats – energy stores; phospholipids and sterols – major
components of membrane.

A

Lipids

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2
Q

Polyhydroxy aldehydes and ketones with the
general formula of (CH2O)n.

A

Carbohydrates

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3
Q

Most complex and most abundant
organic molecules containing at least one
carboxyl group and one amino group.

A

Proteins

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4
Q

DNA carries coded information, arranged into genes, that is passed from each cell to its daughter cells and from one generation to the next; RNA instrumental in translating the coded message of DNA into sequences of amino acids during synthesis of protein molecules

A

Nucleic Acid

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5
Q

The process of increasing the rate of reaction with the use of a catalyst.

A

Catalysis

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6
Q

Any substance that increases rate of reaction upon addition to a certain reaction

A

Catalyst

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7
Q

Catalyst of biochemical reactions (biological catalysts). Neither used up in the reaction nor do they appear as reaction products

A

Enzymes

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8
Q

Catalyzes all the synthetic and metabolic
reactions of the cell that allows for a faster speed of reaction. Increases the rate of reaction by means of
lowering the activation energy

A

Enzymes

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9
Q

Measured as the number of calories required to bring all the molecules in a mole of reactant at a given temperature to a reactive (or activated) state.

A

Activation energy

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10
Q

How do enzymes hasten the reaction?

A

Enzyme lowers the activation energy needed

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11
Q

Enzyme (E) binds with a substrate (S) to form an activated:

A

Enzyme-substrate complex (ES)

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12
Q

reactions catalyzed by enzymes are usually __________ to ________ times faster than uncatalyzed reactions.

A

10^3 to 10^17

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13
Q

Trait of an enzyme being specific for a certain substrate:

A

Enzyme Specificity

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14
Q

Specificity of enzymes varies on:

A

Stereoisomerism

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15
Q

Enzyme present in the intestine that hydrolyses any peptide bond where the carbonyl belongs to a phenylalanine, tyrosine, or tryptophan residue.

A

Chymotrypsin

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16
Q

Close and complementary fit between enzymes and substrate in a special portion of the enzyme surface

A

Active Site

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17
Q

Two enzyme-substrate complex models

A

Lock and Key model, Induced Fit model

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18
Q

Catalytic potential of an enzyme

A

Enzyme activity

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19
Q

Number of reactions catalyzed per second by the enzyme

A

Turnover number

20
Q

How enzymes accelerate reactions

A
  1. Hold substrates in close proximity; increasing reaction probability
  2. Presence of proton donors and acceptors in the binding site
  3. Forms an unstable intermediate that readily
    undergoes second reaction
21
Q

Factors affecting Enzyme activity

A

temperature, pH level, cofactors, and coenzymes

22
Q

Increases enzymatic activity by increasing the kinetic energy, thus number of molecular collisions increases, increasing the probability of reaction between molecules

A

Temperature

23
Q

An extreme increase in temperature leads to the __________ of the enzymes

A

denaturation

24
Q

in pH level exposes more positive sites in the enzyme for interactions with negative groups on substrates

A

Drop

25
Q

_____ in pH level facilitates the binding of positive groups in a substrate to negative sites in the enzyme

A

Rise

26
Q

Small organic molecules that act as cofactors

A

coenzymes

27
Q

An enzyme minus its cofactor; cannot function without its cofactor/coenzyme.

A

Apoenzyme

28
Q

Cofactor + apoenzyme

A

Holoenzyme

29
Q

Enzyme that facilitates oxidation-reduction reaction

A

Oxidoreductase

30
Q

Enzyme that catalyzes the transfer of functional groups

A

Transferases

31
Q

Enzymes that facilitate Hydrolysis reactions

A

Hydrolase

32
Q

Enzyme that facilitates the addition or removal of groups to form double bonds

A

Lyase

33
Q

Enzyme that facilitates Isomerization(intramolecular group transfer)

A

Isomerase

34
Q

Enzymes that facilitate ligation of two substrates at the expense of ATP hydrolysis

A

Ligases

35
Q

The rate at which an enzymatic reaction proceeds depends on the concentrations of substrate, product, and active enzymes.

A

Enzyme Kinetics

36
Q

Means of controlling enzymatic reactions used by living cells.

A

Enzyme Inhibition

37
Q

Two types of Enzyme Inhibition

A

Competitive and Non-competitive

38
Q

Inhibition where inhibitor molecules directly reacts with the active site of an enzyme

A

Competitive inhibition

39
Q

Most common type of competitive inhibition

A

Substrate analogs

40
Q

Caused by inhibitor molecules that bind outside the active site.

A

Non-competitive inhibition

41
Q

Regulation of metabolic reactions

A
  1. Control of Enzyme Synthesis
  2. Control of Enzyme Activity
  3. End-product(feedback) inhibition
42
Q

Alters the tertiary structure of an enzyme thus changing the conformation of the active site

A

allosteric site

43
Q

Interactions of the end products in the allosteric site, making the end product an _________________

A

allosteric inhibitor

44
Q

Some cat-ion cofactors acts as allosteric activators for some enzyme

A

Enzyme Activation

45
Q

Two kinds of metabolic pathways in animal tissues

A

Anaerobic and aerobic

46
Q

Metabolic pathway where food molecules are completely oxidized to carbon dioxide and water by molecular oxygen. Greater energy yield

A

Aerobic metabolism

47
Q

Incomplete oxidation of food molecules converting it to lactic acid; due to absence of oxygen

A

Anaerobic metabolism