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

25
_____ in pH level facilitates the binding of positive groups in a substrate to negative sites in the enzyme
Rise
26
Small organic molecules that act as cofactors
coenzymes
27
An enzyme minus its cofactor; cannot function without its cofactor/coenzyme.
Apoenzyme
28
Cofactor + apoenzyme
Holoenzyme
29
Enzyme that facilitates oxidation-reduction reaction
Oxidoreductase
30
Enzyme that catalyzes the transfer of functional groups
Transferases
31
Enzymes that facilitate Hydrolysis reactions
Hydrolase
32
Enzyme that facilitates the addition or removal of groups to form double bonds
Lyase
33
Enzyme that facilitates Isomerization(intramolecular group transfer)
Isomerase
34
Enzymes that facilitate ligation of two substrates at the expense of ATP hydrolysis
Ligases
35
The rate at which an enzymatic reaction proceeds depends on the concentrations of substrate, product, and active enzymes.
Enzyme Kinetics
36
Means of controlling enzymatic reactions used by living cells.
Enzyme Inhibition
37
Two types of Enzyme Inhibition
Competitive and Non-competitive
38
Inhibition where inhibitor molecules directly reacts with the active site of an enzyme
Competitive inhibition
39
Most common type of competitive inhibition
Substrate analogs
40
Caused by inhibitor molecules that bind outside the active site.
Non-competitive inhibition
41
Regulation of metabolic reactions
1. Control of Enzyme Synthesis 2. Control of Enzyme Activity 3. End-product(feedback) inhibition
42
Alters the tertiary structure of an enzyme thus changing the conformation of the active site
allosteric site
43
Interactions of the end products in the allosteric site, making the end product an _________________
allosteric inhibitor
44
Some cat-ion cofactors acts as allosteric activators for some enzyme
Enzyme Activation
45
Two kinds of metabolic pathways in animal tissues
Anaerobic and aerobic
46
Metabolic pathway where food molecules are completely oxidized to carbon dioxide and water by molecular oxygen. Greater energy yield
Aerobic metabolism
47
Incomplete oxidation of food molecules converting it to lactic acid; due to absence of oxygen
Anaerobic metabolism