ENZYME Flashcards

1
Q

It is a non protein entities

A

Cofactors

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2
Q

Example of a cofactor

A

Inorganic substances like non metals and minerals

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3
Q

Release after catalysis is called

A

Coenzymes

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4
Q

Alters spatial configuration of the enzyme for proper substrate binding

A

Activators

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5
Q

Example of coenzyme

A

Vitamins

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6
Q

Example of Activators

A

Calcium Ion

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7
Q

Interferes with the enzymatic reactions

A

Inhibitors

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8
Q

Binds to the active site of an enzyme

A

Competitive inhibitor

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9
Q

Binds to the allosteric site (Cofactor site)

A

Noncompetitive inhibitor

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10
Q

Binds to the enzyme-substrate complex

A

Uncompetitive inhibitor

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11
Q

Without _______ protein will not be activated and enzyme cannot function without factors.

A

Cofactors

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12
Q

Optimum temperature of enzyme activity

A

37 degree Celsius

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13
Q

Denaturation of enzymes

A

40-50 degrees Celsius

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14
Q

Inactivation of enzymes

A

60-65 degrees Celsius

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15
Q

For every 10 C increase in temperature, there will be a two-fold increase in enzyme activity.

A

Temperature coefficient (Q10)

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16
Q

At what range does most physiologic reactions occur in pH?

A

7-8

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17
Q

Storage for enzyme

A

-20 C

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18
Q

Storage for substrate and coenzymes

A

2-8 C

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19
Q

Storage for LD 4 and 5

A

Room Temperature

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20
Q

Increases enzyme concentration

A

Hemolysis

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21
Q

Decreases enzyme concentration

A

Latescence or milky specimen

22
Q

Enzyme nomenclature

A

1st digit: Classification
2nd and 3rd digits: subclass
4th digits: serial number

23
Q

Enzyme classification

A

a. Oxidoreductases
b. Transferases
c. Hydrolases
d. Lyases
e. Isomerases
f. Ligases

24
Q

Transfer of a chemical group other than hydrogen from 1 substrate to another

A

Transferases

25
splitting by addition of water - Hydrolysis
Hydrolases
26
removal of groups without hydrolysis
Lyases
27
Redox reduction
Oxidoreductases
28
Intramolecular arrangements
Isomerases
29
Joining of 2 substrate molecules synthases
Ligases
30
Where the substrate interacts
Active site
31
May bind regulatory molecules
Allosteric site
32
coenzyme that bound tightly to the enzyme
Prosthetic group
33
an enzyme along with its cofactor is called
Haloenzyme
34
Inactive form of enzyme
zymogen/proenzyme
35
shape of the key must fit into the lock
Lock and key theory
36
Based on the substrate binding to the active site of the enzyme
Induced fit theory
37
Enzyme combines with only 1 substrate and catalyzes only 1 reaction
Absolutely specificity
38
Enzyme combines with all the substrates in a chemical group.
Group specificity
39
Enzymes reacting with specific chemical bonds
Bond specificity
40
Reaction rate depends only on enzyme concentration
Zero-order reaction
41
Reaction rate is directly proportional to substrate concentration
First-order reaction
42
International unit for enzyme
1 micromole of substrate /minute
43
Katal unit
1 mole of substrate/second
44
Absorbance is made at 10-second intervals for 100 seconds
Nonkinetic assay
45
Electrophoresis:
(+) Liver - Bone (Regan) - Placenta- Intestine (-)
46
Heat fractionation:
(Stable) Regan - Placenta - Intestine - Liver- Bone (Labile)
47
Inhibits Regan, placental and intestinal ALP
Phenylalanine
48
Inhibits Nago ALP
L-Leucine
49
Inhibits live and bone ALP
Levamisole
50
Inhibits bone ALP
3M urea