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Biochemical Engineering > Enzyme > Flashcards

Enzyme Flashcards

1
Q

proteins that are catalysts of biochemical reactions.

A

Enzymes

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2
Q

not consumed during a
chemical reaction.

A

Catalyst

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3
Q

Typically has a
globular shape. It has a complex 3-D structure.

A

Enzymes

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4
Q

First clear recognition of enzyme was made by ?

A

Payen and Persoz (around 1833)

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5
Q

an alcohol precipitate of malt extract contained in a thermolabile substance that converted starch to sugar.

A

Diastase

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6
Q

use of -ase in naming enzyme

A

Duclaux (1898)

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7
Q

first to crystallize enzyme (urease)

A

J.B. Sumner (1924-1930)

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8
Q

modulates an enzyme activity

A

Effectors

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9
Q

found in animal and plant cells

A

Catalase

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10
Q

found in saliva and in the pancreas. It breaks down starch down to
maltose.

A

Amylase

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11
Q

synthesize enzyme (builds up). It builds/combines multiple
Glucose-1-Phosphate molecules into starch

A

Potato Phosphorylase

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12
Q

characteristic of catalyst. High efficiency, 10^3 to 10^17 faster
than the corresponding uncatalyzed reactions.

A

Catalytic efficiency

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13
Q

a characteristic of catalyst. High _________, interacting with one
or a few specific substances and catalyzing only one type of chemical reaction.

A

Specificity

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14
Q

characteristic of catalyst, 37℃, physiological pH, ambient atmospheric pressure.

A

Mild reactions conditions

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15
Q

a part of the enzyme where the reactants bind, where the biochemical reaction occurs.

A

Active Site

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16
Q

The enzyme active site is usually composed of?

A

amino acid side chains interact,
metal ions, various types of polar, non-polar, ionic interactions.

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17
Q

a region within an enzyme that fits the shape of molecules called substrates or reactants.

A

Active Site

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18
Q

The active site contains…

A

amino acid R groups that align and bind the substrate.

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19
Q

The substrates fit like a key in a lock and the active site is the lock itself. If the conditions are satisfied, a chemical reaction will occur to form products. After the reaction, the enzyme is unchanged.

A

β€œLock and Key Model”

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20
Q

additional non-protein molecule that is needed by some enzymes to help the reaction

A

Cofactors

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21
Q

Cofactors that are bound and released easily are called

A

Coenzymes

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22
Q

present in trace amounts within the enzyme.

A

Metal Ions

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23
Q

a cofactor for carboxypeptidase

A

Zn^2+

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24
Q

non-protein or organic, maybe a vitamin

A

Coenzyme

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25
Q

catalyze the same reaction in different tissues in the body

A

Isoenzymes

26
Q

which converts lactate to pyruvate consists of five isoenzymes.

A

Lactate dehydrogenase

27
Q

first created the classifications in enzyme system

A

IUPAC (International Union for Pure and Applied Chemistry)

28
Q

developed the four-integer number system and a name.

A

EC or the Enzyme Commission

29
Q

Enzymes are classified according to the type of reaction they catalyze:

a. Oxidoreductases

A

oxidation-reduction reactions.

30
Q

Enzymes are classified according to the type of reaction they catalyze:

b. Transferases

A

transport/transfer of group of atoms or single atoms

31
Q

Enzymes are classified according to the type of reaction they catalyze:

c. Hydrolases

A

Hydrolysis

32
Q

Enzymes are classified according to the type of reaction they catalyze:

d. Lyases

A

adding or removing atoms to form a double bond.

33
Q

Enzymes are classified according to the type of reaction they catalyze:

e. Isomerases

A

rearranging atoms

34
Q

Enzymes are classified according to the type of reaction they catalyze:

f. Ligases

A

using ATP to combine molecules (substrates).

35
Q

EC first integer:

A

six major classes of enzyme catalyzed reactions.

36
Q

Second integer:

A

a subclass

37
Q

Third integer:

A

sub classification depending on 1st and 2nd integer.

38
Q

Fourth integer:

A

serial number

39
Q

rate of reaction between two molecules is enhanced if
they are abstracted from dilute solution and held in close proximity to each other

A

Facilitation of Proximity

40
Q

This mechanism involves the transient covalent bonding of the substrate to an amino acid residue in the active site.

A

Covalent Catalysis

41
Q

more prone to undergoing covalent catalysis reactions

A

nucleophilic groups

42
Q

many reactions involve the formation of normally unstable, charge intermediates.

A

General Acid-Base Catalysis

43
Q

accounts for the overall lowering of activation
energy for a reaction, and it can also be considered as a catalytic mechanism for a reaction.

A

Binding Energy

44
Q

– various metals, all positively charged including zinc, iron,
magnesium, manganese, and copper are known to form complexes with different
enzymes or substrates.

A

Metal Ion Catalysis

45
Q

The binding of the substrate
results in the distortion of the substrate in a way that makes the chemical reaction easier

A

Strain, Molecular Distortion, and Shape Change

46
Q

Common enzymes used for clinical diagnosis

A

alanine aminotransferase
(ALT, also called glutamate pyruvate transaminase GPT), alkaline phosphatase,
amylase,
aspartate aminotransferase, creatine kinase, and
lactate dehydrogenase.

47
Q

the reaction is in between the reactant consumption and
product formation (peak).

A

Transition State

48
Q

Increasing the temperature make molecules

A

move faster

49
Q

very sensitive to temperature changes

A

Biological systems

50
Q

Enzymes can increase the rate of reactions without?

A

increasing/requiring an increase
in the temperature.

51
Q

they catalyze one type of reaction for a single substrate.

A

Absolute Enzymes

52
Q

they catalyze one type of reaction for similar substrates

A

group enzymes

53
Q

they catalyze one type of reaction for a specific type of bond.

A

linkage enzymes

54
Q

The lock and key hypothesis

A
  1. Temporary structure called the enzyme-substrate complex formed.
  2. Products have a different shape from the substrate.
  3. Once formed, they are released from the active site.
  4. Leaving it free to become attached to another substrate.
55
Q

Induced fit theory

A
  1. Enzyme changes shape with substrate.
  2. The active site is not rigid.
  3. The active site is capable of changing its shape depending upon the substrate.
56
Q

the active site is flexible, not rigid, the shapes of the enzyme, active site, and substrate adjust to maximum the fit which
improves the catalysis, and there is a greater range of substrate specificity

A

induced fit model of enzyme action

57
Q

The induced fit hypothesis:

A
  1. Some proteins can change their shape (conformation).
  2. When a substrate combines with an enzyme, it induces a change in the enzyme’s
    conformation.
  3. The active site is then molded into a precise conformation.
  4. Making the chemical environment suitable for the reaction.
  5. The bonds of the substrate are stretched to make the reaction easier (lowers
    activation energy).
58
Q

When a substrate (S) fits properly in an active site, what is formed?

A

an enzyme-substrate complex
(ES)

𝐸 + 𝑆 β†’ 𝐸𝑆 (π‘Ÿπ‘’π‘£π‘’π‘Ÿπ‘ π‘–π‘π‘™π‘’)

59
Q

Within the active site of the ES complex, what happened?

A

the reaction occurs to convert substrate to product (P):

𝐸𝑆 β†’ 𝐸 + 𝑃 (π‘–π‘Ÿπ‘Ÿπ‘’π‘£π‘’π‘Ÿπ‘ π‘–π‘π‘™π‘’)

60
Q

The overall reaction for the conversion of substrate

A

𝐸 + 𝑆 β†’ 𝐸𝑆(π‘Ÿπ‘’π‘£π‘’π‘Ÿπ‘ π‘–π‘π‘™π‘’) β†’ 𝐸 + 𝑃 (π‘–π‘Ÿπ‘Ÿπ‘’π‘£π‘’π‘Ÿπ‘ π‘–π‘π‘™π‘’)

61
Q

Enzymatic reaction steps

A
  1. Substrate approaches the active site
  2. Enzyme-substrate complex forms
  3. Substrate transformed into products
  4. Products released
  5. Enzyme recycled (depends on the enzyme, not always)
62
Q

The reaction for the sucrase catalyzed hydrolysis of sucrose to glucose and fructose.

A

π‘†π‘’π‘π‘Ÿπ‘Žπ‘ π‘’ + π‘†π‘’π‘π‘Ÿπ‘œπ‘ π‘’ β†’ 𝐸𝑆 π‘π‘œπ‘šπ‘π‘™π‘’π‘₯ (π‘Ÿπ‘’π‘£π‘’π‘Ÿπ‘ π‘–π‘π‘™π‘’) β†’ π‘†π‘’π‘π‘Ÿπ‘Žπ‘ π‘’ + πΊπ‘™π‘’π‘π‘œπ‘ π‘’ + πΉπ‘Ÿπ‘’π‘π‘‘π‘œπ‘ π‘’ (π‘–π‘Ÿπ‘Ÿπ‘’π‘£π‘’π‘Ÿπ‘ π‘–π‘π‘™π‘’)

Biochemical Engineering (3 decks)

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