M5 - Lesson 1: General Characteristic, Structure and Nomenclature of Enzymes Flashcards

1
Q

Proteins that increase the rate of biological reactions within the cells of the body.

A

Enzyme

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2
Q

Examples of Enzyme

A

Salivary amylase, Catalase, and Phenolase (water, cold temp and acidic environment)

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3
Q

Lower the activation energy and increase the rate of reaction.

A

Biological Catalyst

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4
Q

What is the largest and most highly specialized class of proteins, hence activity is lost if denatured?

A

Enzyme

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5
Q

A compound which lowers the energy required for a reaction.

A

Catalyst

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6
Q

Not consumed in the reaction, it can be used over and over again.

A

Catalyst

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7
Q

Without the enzymes in our _________ tract, it would take us about __ years to digest a single meal.

A

digestive, 50

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8
Q

Advantage and Disadvantage.

A

Economical; Fatal to eat again, no pleasure in eating.

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9
Q

It’s the protein part of the enzyme molecule

A

Apoenzyme

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10
Q

Are additional chemical groups that are required for enzyme activity. It consist of metal ions or complex organic molecules.

A

Activators

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11
Q

3 Types of Cofactors

A

Cofactor, Coenzyme, and Prosthetis Group

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12
Q

Inorganic substance that tend to increase the activity of an enzyme (Iron, Zinc). Also known as Metal Ion.

A

Cofactor

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13
Q

It’s a complex organic molecule other than a protein (thiamine).

A

Coenzyme

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14
Q

If the activator becomes a permanent part of the enzyme.

A

Prosthetic Group

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15
Q

It’s the specific area of the enzyme to which the substrate attaches during the reaction. An enzyme molecule can have several of this.

A

Active Site

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16
Q

It’s the chemical substance or substances on which the enzyme acts.

A

Substrate

17
Q

It’s a substance that will make an enzyme less active or render it inactive.

A

Inhibitor

18
Q

What are the 5 Important terms of Enzyme?

A
Apoenzyme
Activators
Active site
Substrate
Inhibitor
19
Q

It’s an active enzyme, which consists of an apoenzyme and one or more factors.

A

Holoenzyme

20
Q

It’s an enzyme in its inactive form.

A

Proenzyme/Zymogen

21
Q

What enzymes that are often synthesized in an inactive form, transported to the place where activity is desired, and then converted to their active forms?

A

Digestive Enzymes

22
Q

What are the enzymes that Inactive and Active Forms of Zymogen?

A

Pepsinogen (stomach)
Trypsinogen (pancreas)
Prothrombin

23
Q

What are the enzymes that Inactive and Active Forms of Holoenzyme?

A

Pepsin
Trypsin
Thrombin

24
Q

What are the six major classes and their several subcalsses (reactions that they catalyze) ?

A
Maltase - Maltose
Urease - Urea
Protease - Proteins
Carbohydrates - Carbohydrates
Lipases - Lipids
Hydrolases - Hydrolysis reactions
25
Q

Enzymes are now named by adding an ____ ending on the name of the substrate.

A

-ase

26
Q

What enzymes that acts on casein?

A

Rennin

27
Q

What enzymes that acts or hydrolyze protein?

A

Pepsin and Trypsin

28
Q

What enzyme that acts on carbohydrate?

A

Ptyalin