Enzymes Flashcards

(64 cards)

1
Q

are proteins that increase the rate of reaction by lowering the energy of activation

A

enzymes

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

They catalyze nearly all the chemical reactions taking place in the cells of the body

A

enzymes

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

they have unique three-dimensional shapes that fit the shapes of reactants (substrates)

A

Enzymes

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

shape of enzymes

A

globular

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

complex structure of enzyme

A

3D

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

The substrate of an enzyme are the ______ that are activated by the enzyme

A

reactants

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

Enzymes are _______ to their substrates

A

specific

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

The specificity of enzyme is determined by the?

A

active site

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

The name of an enzyme identifies the reacting substance
- usually ends in?

A

-ase

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

Enzymes are classified according to the?

A

type of reaction they catalyze

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

Oxidation-reduction is classified as?

A

Oxidoreductases

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

Transfer groups of atoms is classified as?

A

transferases

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

hydrolysis is classified as?

A

hydrolases

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

addition and removal of atoms from a double bond is classified as?

A

lyases

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

rearranging atoms is classified as?

A

isomerases

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

using atp to combine molecules is classified as?

A

ligases

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 substrate molecules

A

active site

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

Amino acid side-chains align to bind the _____ through H-bonding, salt-bridges, hydrophobic interactions, etc.

A

substrate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

are released when the reaction is complete (they no longer fit well in the active site)

A

Products

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

Enzymes have varying degrees of ______ for substrates

A

specificity

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

Enzymes may recognize and catalyze:

A
  • a single substrate
    • a group of similar substrates
    • a particular type of bond
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

types of enzyme specificity

A
  1. absolute
  2. group
  3. linkage
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

Catalyze one type of reaction for a
single substrate
ex: Urease catalyzes only the
hydrolysis of urea

A

absolute

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

Catalyze one type of reaction for
similar substrates
ex: Hexokinase adds a phosphate
group to hexoses

A

group

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Catalyze one type of reaction for a specific type of bond ex: Chymotrypsin catalyzes the hydrolysis of peptide bonds
linkage
26
In the ________ of enzyme action: - the active site has a rigid shape - only substrates with the matching shape can fit - the substrate is a key that fits the lock of the active site
lock-and-key model
27
This is an older model, however, and does not work for all enzymes
Lock-and-Key Model
28
In the __________ of enzyme action: - the active site is flexible, not rigid - the shapes of the enzyme, active site, and substrate adjust to maximize the fit, which improves catalysis - there is a greater range of substrate specificity
induced-fit model
29
This model is more consistent with a wider range of enzymes
induced-fit model
30
When a substrate (S) fits properly in an active site, an __________ is formed
enzyme-substrate (ES) complex
31
Within the active site of the ES complex, the reaction occurs to convert substrate to?
product (P)
32
The products are then released, allowing another ________ to bind the enzyme - this cycle can be repeated millions (or even more) times per minute
substrate molecule
33
are different forms of an enzyme that catalyze the same reaction in different tissues in the body
isoenzymes
34
they have slight variations in the amino acid sequences of the subunits of their quaternary structure •For example, lactate dehydrogenase (LDH), which converts lactate to pyruvate, consists of five isoenzymes
isoenzymes
35
An additional non-protein molecule that is needed by some enzymes to help the reaction
cofactors
36
Tightly bound cofactors are called?
prosthetic groups
37
Cofactors that are bound and released easily are called?
coenzymes
38
Many vitamins are?
coenzymes
39
The levels of ______ in the blood can be used to determine the amount of damage in specific tissues
diagnostic enzymes
40
Enzymes are most active at an optimum temperature
usually 37°C in humans
41
enzyme show little activity at?
low temperatures
42
Activity is lost at high temperatures as _________ occurs
denaturation
43
Enzymes are most active at?
optimum pH
44
Amino acids with _________ have the proper charges when the pH is optimum
acidic or basic side-chains
45
Activity is lost at low or high pH as _________ is disrupted
tertiary structure
46
Most enzymes of the body have an optimum pH of about? However, in certain organs, enzymes operate at lower and higher optimum pH values
7.4
47
The rate of reaction increases as _______ increases (at constant substrate concentration)
enzyme concentration
48
At higher enzyme concentrations, more enzymes are available to _____ the reaction (more reactions at once)
catalyze
49
There is a ______ between reaction rate and enzyme concentration (at constant substrate concentration)
linear relationship
50
The rate of reaction increases as _______ increases (at constant enzyme concentration)
substrate concentration
51
__________ occurs when the enzyme is saturated (when all enzymes are binding substrate)
Maximum activity
52
The relationship between reaction rate and substrate concentration is? (levels off) when the enzyme is saturated
exponential, and asymptotes
53
are molecules that cause a **loss of enzyme activity**
inhibitors
54
They prevent substrates from fitting into the active site of the enzyme
inhibitors
55
goes on and off, allowing the enzyme to regain activity when the inhibitor leaves
reversible inhibitor
56
reversible and has a structure like the substrate
competitive inhibitor
57
it competes with the substrate for the active site
competitive inhibitor
58
its effect is reversed by increasing substrate concentration
competitive inhibitor
59
is a competitive inhibitor of succinate dehydrogenase - it has a structure that is similar to succinate - inhibition can be reversed by adding succinate
malonate
60
has a structure that is different than that of the substrate
noncompetitive inhibitor
61
noncompetitive inhibitor it binds to an? rather than to the active site
allosteric site
62
it distorts the shape of the enzyme, which alters the shape of the active site and prevents the binding of the substrate
noncompetitive inhibitor
63
The effect can not be reversed by adding more substrate
noncompetitive inhibitor
64
destroys enzyme activity, usually by bonding with side-chain groups in the active site
irreversible inhibitor