(LEC) Intro to Enzymology Flashcards

1
Q

Study of enzymes

A

Enzymology

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2
Q

Protein catalysts that increases the speed of reaction

A

Enzyme

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3
Q

The molecule upon which an enzyme acts

A

Substrate

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4
Q

Defined as the minimum energy required to start a chemical reaction

A

Activation Energy

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5
Q

Activation Energy is aka

A

Excess Energy

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6
Q

Region of an enzyme where substrate molecules bind

A

Activation site

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7
Q

Place on an enzyme where a molecule that is not a substrate may bind

A

Allosteric Site

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8
Q

Allosteric site:

Impairs activity of the enzyme

A

Allosteric Inhibitor

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9
Q

Allosteric Site:

Enhances activity of the enzyme

A

Allosteric Activator

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10
Q

Results when an enzyme is subject to posttranslational modification

A

Isoform

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11
Q

Isoform of Enzymes

A

Isoenzymes

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12
Q

Enzyme existing in different forms within the same individuals but the same action

A

Isoenzymes

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13
Q

Nonprotein molecule that may be necessary for enzyme activty

A

Cofactor

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14
Q

Inorganic cofactor

A

Activator

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15
Q

Organic cofactor

A

Coenzyme

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16
Q

Apoenzyme + Coenzyme = ?

A

Holoenzyme

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17
Q

Proenzyme is aka?

A

Zymogen

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18
Q

Inactive form or precursor of enzyme

A

Proenzyme / Zymogen

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19
Q

Reaction Type that Catalyzes one type of reaction for a single substrate

A

Absolute

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20
Q

Reaction Type that Catalyzes one type of reaction for similar substrates

A

Group

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21
Q

Reaction Type that Catalyzes one type of reaction for a specific type of bond

A

Linkage

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22
Q

Example of Enzyme with Absolute Reaction Type

A

Urease

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23
Q

Example of Enzyme with Group Reaction Type

A

Hexokinase

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24
Q

Example of Enzyme with Linkage Reaction Type

A

Chymotrypsin

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25
Q

Enzyme for Lipid Substrate

A

Lipase

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26
Q

Enzyme for Ester Substrate

A

Esterase

27
Q

Enzyme for Protein Substrate

A

Protease

28
Q

Enzyme for Oxidation Reaction

A

Oxidase

29
Q

Enzyme for Reduction Reaction

A

Reductase

30
Q

Enzyme for Hydrolysis Reaction

A

Hydrolase

31
Q

Enzyme for Removal of Hydrogen

A

Dehydrogenase

32
Q

Enzyme for Removal of Carboxyl groups

A

Decarboxylase

33
Q

1st digit in Enzyme Commission Nomenclature

A

Class

34
Q

2nd digit in Enzyme Commission Nomenclature

A

Subclass

35
Q

3rd or 4th digit in Enzyme Commission Nomenclature

A

Serial Number

36
Q

Classification of Enzymes for EC Nomenclature (1-6)

A
  1. Oxireductase
  2. Transferase
  3. Hydrolase
  4. Lyase
  5. Isomerase
  6. Ligase
37
Q

EC of Lactate Dehydrogenase

A

1.1.1.27

38
Q

EC of G6P

A

1.1.1.49

39
Q

EC of Glutamine dehydrogenase

A

1.4.1.3

40
Q

Transfer of functional groups other than hydrogen from one substrate to another

A

Transferase

41
Q

EC of Aspartate aminotransferase

A

2.6.1.1

42
Q

EC of Alanine aminotransferase

A

2.6.1.2

43
Q

EC of Creatine Kinase

A

2.7.3.2

44
Q

EC of y-Glutamyltransferase

A

2.3.2.2

45
Q

EC of g-S-transferase

A

2.5.1.18

46
Q

EC of Glycogen phosphorylase

A

2.4.1.1

47
Q

EC of Pyruvate Kinase

A

2.7.1.40

48
Q

Addition of water to a bond resulting in bond breakage

A

Hydrolases

49
Q

EC of Alkaline phosphatase

A

3.1.3.1

50
Q

EC of Acid phosphatase

A

3.1.3.2

51
Q

EC of alpha-Amylase

A

3.2.1.1

52
Q

EC of Cholinesterase

A

3.1.1.8

53
Q

EC of Chymotrypsin

A

3.4.21.1

54
Q

EC of Esterase-1

A

3.4.21.36

55
Q

EC of 5-Nucleotidase

A

3.1.3.5

56
Q

EC of Triacylglycerol lipase

A

3.1.1.3

57
Q

EC of Trypsin

A

3.4.21.4

58
Q

Catalyzes removal of groups from substrates without hydrolysis

A

Lyases

59
Q

Lyases reaction products contains

A

Double bonds

60
Q

Rearranges the functional groups within a molecule and catalyzes the conversion of isomer to another

A

Isomerase

61
Q

Catalyzes the joining of two large molecules by forming a new chemical bond

A

Ligase

62
Q

EC of Lyase

A

4.1.2.13

63
Q

EC of Isomerase

A

5.3.1.1

64
Q

EC of Ligase

A

6.3.2.3