ENZYMOLOGY Flashcards

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

A

F

17
Q

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

A

T

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 __

A

7-8

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

A

Katal

24
Q

Catalyze the removal or addition of electrons

A

Oxidoreductases

25
Q

Difference of competitive inhibitor and noncompetitive inhibitor

A

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
Q

Factors affecting enzyme reactions

A
Substrate concentration
Enzyme concentration
pH
Temperature
Cofactors
Inhibitors
27
Q

Kinds of Inhibitors

A

Competitive
Noncompetitive
Uncompetitive

28
Q

Substances which decrease the rate of enzyme reaction if they are present in the reaction system

A

Inhibitors

29
Q

In what temperature is the analysis of enzymes carried out?

A

25C, 30C, 37C

30
Q

T or F

Increasing the concentration of cofactor will decrease the rate of enzyme reaction

A

False

31
Q

Nomenclature of Amylase

A

EC 3.2.1.1

32
Q

Nomenclature of Alanine aminotransferase

A

EC 2.6.1.2

33
Q

Catalyze the hydrolysis of a bond by the addition of water

A

Hydrolases

34
Q

Catalyze intermollecular arrangement of the substrate

A

Isomerases

35
Q

Catalyze the joining of two molecules

A

Ligases