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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
Q

splitting by addition of water - Hydrolysis

A

Hydrolases

26
Q

removal of groups without hydrolysis

27
Q

Redox reduction

A

Oxidoreductases

28
Q

Intramolecular arrangements

A

Isomerases

29
Q

Joining of 2 substrate molecules synthases

30
Q

Where the substrate interacts

A

Active site

31
Q

May bind regulatory molecules

A

Allosteric site

32
Q

coenzyme that bound tightly to the enzyme

A

Prosthetic group

33
Q

an enzyme along with its cofactor is called

A

Haloenzyme

34
Q

Inactive form of enzyme

A

zymogen/proenzyme

35
Q

shape of the key must fit into the lock

A

Lock and key theory

36
Q

Based on the substrate binding to the active site of the enzyme

A

Induced fit theory

37
Q

Enzyme combines with only 1 substrate and catalyzes only 1 reaction

A

Absolutely specificity

38
Q

Enzyme combines with all the substrates in a chemical group.

A

Group specificity

39
Q

Enzymes reacting with specific chemical bonds

A

Bond specificity

40
Q

Reaction rate depends only on enzyme concentration

A

Zero-order reaction

41
Q

Reaction rate is directly proportional to substrate concentration

A

First-order reaction

42
Q

International unit for enzyme

A

1 micromole of substrate /minute

43
Q

Katal unit

A

1 mole of substrate/second

44
Q

Absorbance is made at 10-second intervals for 100 seconds

A

Nonkinetic assay

45
Q

Electrophoresis:

A

(+) Liver - Bone (Regan) - Placenta- Intestine (-)

46
Q

Heat fractionation:

A

(Stable) Regan - Placenta - Intestine - Liver- Bone (Labile)

47
Q

Inhibits Regan, placental and intestinal ALP

A

Phenylalanine

48
Q

Inhibits Nago ALP

49
Q

Inhibits live and bone ALP

A

Levamisole

50
Q

Inhibits bone ALP

ENZYME (1 decks)

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