ENZYMOLOGY Flashcards

(35 cards)

1
Q

also called relative specificity

A

Bond specificity

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2
Q

Apoenzyme + Coenzyme

A

Holoenzyme

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3
Q

Chemical reactants which bind with enzymes

A

Substrate

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4
Q

Class of enzymes

A
Oxidoreductases
Transferases
Hydrolases
Lyases
Isomerases
Ligases
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5
Q

Enzymes that catalyze the same chemical reaction but have slightly different structures

A

Isoenzyme

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6
Q

Examples of lyases

A

Glutamate decarboxylase
Pyruvate decarboxylase
Tryptophan decarboxylases
Aldolase

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7
Q

Factors that affect Km

A

pH
Temperature
Ionic strength
Nature of substrate

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8
Q

In the nomenclature of enzymes, the 4th digit signifies what

A

Serial number

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9
Q

In what temperature can enzyme denaturation occr

A

40-50C

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10
Q

Key part of enzyme structure

A

Active site

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11
Q

LDH is a type of

A

Isoenzyme; Oxidoreductase

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12
Q

Methods used to measure enzyme reactions

A

Fixed time or end point analysis

Continuous monitoring/ kinetic assay

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13
Q

Place for regulator binds

A

Allosteric site

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14
Q

Serve as second substrate for enzymatic reactions

A

Coenzyme

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15
Q

T or F: all enzymes contain allosteric site

A

F

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16
Q

T or F: enzymes are not high molecular weight compounds

17
Q

T or F: reaction rate is directly proportional to the concentration of the substrate

18
Q

The enzyme nomenclature is made by

A

Enzyme commission of International Union of Biochemistry

19
Q

Theory in which the interaction of the enzyme and substrate causes a mild shift in the structure of the enzyme that confirms an ideal binding arrangement between the two

A

Induced Fit Theory

20
Q

Types of Specificity

A

Absolute specificity
Group specificity
Bond specificity
Sterioisometric specificity

21
Q

Most physiologic reactions occur in the pH __

22
Q

Amount of enzyme that catalyzes 1 micromole of substrate/minute

A

International unit (IU)

23
Q

Amount of enzyme w/c converts 1 mole of substrate per second

24
Q

Catalyze the removal or addition of electrons

A

Oxidoreductases

25
Difference of competitive inhibitor and noncompetitive inhibitor
Competitive inhibitor competes for the active site, while the non competitive inhibitor binds to the allosteric site causing the change in shape of the enzyme
26
Factors affecting enzyme reactions
``` Substrate concentration Enzyme concentration pH Temperature Cofactors Inhibitors ```
27
Kinds of Inhibitors
Competitive Noncompetitive Uncompetitive
28
Substances which decrease the rate of enzyme reaction if they are present in the reaction system
Inhibitors
29
In what temperature is the analysis of enzymes carried out?
25C, 30C, 37C
30
T or F Increasing the concentration of cofactor will decrease the rate of enzyme reaction
False
31
Nomenclature of Amylase
EC 3.2.1.1
32
Nomenclature of Alanine aminotransferase
EC 2.6.1.2
33
Catalyze the hydrolysis of a bond by the addition of water
Hydrolases
34
Catalyze intermollecular arrangement of the substrate
Isomerases
35
Catalyze the joining of two molecules
Ligases