Enzyme Flashcards

1
Q

proteins that are catalysts of biochemical reactions.

A

Enzymes

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

not consumed during a
chemical reaction.

A

Catalyst

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

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

A

Enzymes

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

First clear recognition of enzyme was made by ?

A

Payen and Persoz (around 1833)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

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

A

Diastase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

use of -ase in naming enzyme

A

Duclaux (1898)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

first to crystallize enzyme (urease)

A

J.B. Sumner (1924-1930)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

modulates an enzyme activity

A

Effectors

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

found in animal and plant cells

A

Catalase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

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

A

Amylase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

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

A

Potato Phosphorylase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

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

A

Catalytic efficiency

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

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

A

Mild reactions conditions

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

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

A

Active Site

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

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

A

Active Site

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

The active site contains…

A

amino acid R groups that align and bind the substrate.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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

“Lock and Key Model”

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

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

A

Cofactors

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

Cofactors that are bound and released easily are called

A

Coenzymes

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

present in trace amounts within the enzyme.

A

Metal Ions

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

a cofactor for carboxypeptidase

A

Zn^2+

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

non-protein or organic, maybe a vitamin

A

Coenzyme

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
catalyze the same reaction in different tissues in the body
Isoenzymes
26
which converts lactate to pyruvate consists of five isoenzymes.
Lactate dehydrogenase
27
first created the classifications in enzyme system
IUPAC (International Union for Pure and Applied Chemistry)
28
developed the four-integer number system and a name.
EC or the Enzyme Commission
29
Enzymes are classified according to the type of reaction they catalyze: a. Oxidoreductases
oxidation-reduction reactions.
30
Enzymes are classified according to the type of reaction they catalyze: b. Transferases
transport/transfer of group of atoms or single atoms
31
Enzymes are classified according to the type of reaction they catalyze: c. Hydrolases
Hydrolysis
32
Enzymes are classified according to the type of reaction they catalyze: d. Lyases
adding or removing atoms to form a double bond.
33
Enzymes are classified according to the type of reaction they catalyze: e. Isomerases
rearranging atoms
34
Enzymes are classified according to the type of reaction they catalyze: f. Ligases
using ATP to combine molecules (substrates).
35
EC first integer:
six major classes of enzyme catalyzed reactions.
36
Second integer:
a subclass
37
Third integer:
sub classification depending on 1st and 2nd integer.
38
Fourth integer:
serial number
39
rate of reaction between two molecules is enhanced if they are abstracted from dilute solution and held in close proximity to each other
Facilitation of Proximity
40
This mechanism involves the transient covalent bonding of the substrate to an amino acid residue in the active site.
Covalent Catalysis
41
more prone to undergoing covalent catalysis reactions
nucleophilic groups
42
many reactions involve the formation of normally unstable, charge intermediates.
General Acid-Base Catalysis
43
accounts for the overall lowering of activation energy for a reaction, and it can also be considered as a catalytic mechanism for a reaction.
Binding Energy
44
– various metals, all positively charged including zinc, iron, magnesium, manganese, and copper are known to form complexes with different enzymes or substrates.
Metal Ion Catalysis
45
The binding of the substrate results in the distortion of the substrate in a way that makes the chemical reaction easier
Strain, Molecular Distortion, and Shape Change
46
Common enzymes used for clinical diagnosis
alanine aminotransferase (ALT, also called glutamate pyruvate transaminase GPT), alkaline phosphatase, amylase, aspartate aminotransferase, creatine kinase, and lactate dehydrogenase.
47
the reaction is in between the reactant consumption and product formation (peak).
Transition State
48
Increasing the temperature make molecules
move faster
49
very sensitive to temperature changes
Biological systems
50
Enzymes can increase the rate of reactions without?
increasing/requiring an increase in the temperature.
51
they catalyze one type of reaction for a single substrate.
Absolute Enzymes
52
they catalyze one type of reaction for similar substrates
group enzymes
53
they catalyze one type of reaction for a specific type of bond.
linkage enzymes
54
The lock and key hypothesis
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
Induced fit theory
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
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
induced fit model of enzyme action
57
The induced fit hypothesis:
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
When a substrate (S) fits properly in an active site, what is formed?
an enzyme-substrate complex (ES) 𝐸 + 𝑆 → 𝐸𝑆 (𝑟𝑒𝑣𝑒𝑟𝑠𝑖𝑏𝑙𝑒)
59
Within the active site of the ES complex, what happened?
the reaction occurs to convert substrate to product (P): 𝐸𝑆 → 𝐸 + 𝑃 (𝑖𝑟𝑟𝑒𝑣𝑒𝑟𝑠𝑖𝑏𝑙𝑒)
60
The overall reaction for the conversion of substrate
𝐸 + 𝑆 → 𝐸𝑆(𝑟𝑒𝑣𝑒𝑟𝑠𝑖𝑏𝑙𝑒) → 𝐸 + 𝑃 (𝑖𝑟𝑟𝑒𝑣𝑒𝑟𝑠𝑖𝑏𝑙𝑒)
61
Enzymatic reaction steps
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
The reaction for the sucrase catalyzed hydrolysis of sucrose to glucose and fructose.
𝑆𝑢𝑐𝑟𝑎𝑠𝑒 + 𝑆𝑢𝑐𝑟𝑜𝑠𝑒 → 𝐸𝑆 𝑐𝑜𝑚𝑝𝑙𝑒𝑥 (𝑟𝑒𝑣𝑒𝑟𝑠𝑖𝑏𝑙𝑒) → 𝑆𝑢𝑐𝑟𝑎𝑠𝑒 + 𝐺𝑙𝑢𝑐𝑜𝑠𝑒 + 𝐹𝑟𝑢𝑐𝑡𝑜𝑠𝑒 (𝑖𝑟𝑟𝑒𝑣𝑒𝑟𝑠𝑖𝑏𝑙𝑒)