Enzyme Part 1 Flashcards

1
Q

> Greek word en

A

means “in”

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2
Q

> zyme

A

which means “yeast”

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3
Q

> is an organic compound that act as a catalyst for a biochemical reaction; increases rate of reaction butare not changed in the process
water-soluble, globular proteins
Features:
a) Enhance reaction rates (pH 7.4 and 37°C). An enzyme catalyzed reaction can be 106 to 1012 times faster than uncatalyzed reaction
b) Enzymes are very specific.

A

Enzyme

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4
Q

> Features:

A

a) Enhance reaction rates (pH 7.4 and 37°C). An enzyme catalyzed reaction can be 106 to 1012 times faster than uncatalyzed reaction
b) Enzymes are very specific.

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5
Q

STRUCTURE OF ENZYME

an enzyme composed only of protein.

A

• simple enzyme

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6
Q

an enzyme that has a nonprotein part in addition to the protein part.

A

conjugated enzyme

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7
Q

is the protein part of a conjugated enzyme

A

> apoenzyme

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8
Q

is the nonprotein part of a conjugated
enzyme

A

cofactor

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9
Q

is the biochemically active conjugated enzyme produced from an apoenzyme and a cofactor
Apoenzyme + cofactor = holoenzyme

A

holoenzyme

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10
Q

Why do apoenzymes need cofactors?

A

• A cofactor is a non-protein chemical compound that is required for the protein’s biological activity.
• Cofactors can be considered “helper molecules” that assist enzymes in their action. Cofactors can be ions or organic molecules (called coenzymes).

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11
Q

is a small organic molecule that serves as a cofactor in a conjugated enzyme.

A

Coenzyme

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12
Q

Inorganic ion cofactors include zinc, magnesium, manganese, and iron; chloride occasionally acts as a

A

Cofactor

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13
Q
  • It is bound tightly to the enzyme and is not dissociated even after several extensive steps of purification.
A

Metallo-enzymes

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14
Q

are the focal points for nomenclature.

A

type of reaction catalyzed and substrate

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15
Q

is the reactant in an enzyme-catalyzed reaction; it is the substance upon which the enzyme”acts”

A

substrate

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16
Q

Few enzymes exist in their inactive form called.

A

proenzymes or zymogens

17
Q
  • become active after prior modification in its structure by certain agents. Many times the active form of enzyme acts on zymogen and catalyzes its conversion into active form - process called AUTOCATALYSIS
A

Zymogens

18
Q

PROPERTIES OF ENZYMES

  • special pocket or cleft within the enzyme molecule
  • contains amino acids side chains that participate in substrate binding and catalysis
A

Active sites

19
Q
  • Highly efficient (103
  • 108) times faster than uncatalyzed reactions
A

Catalytic efficiency

20
Q
  • highly specific, interacting only with one or a few substrates and catalyzing only one type of chemical reaction
A

Specificity

21
Q
  • some enzymes require molecules other than proteins for enzymatic activity
  • Holoenzymes refers to the active enzymes with its nonprotein component, whereas the enzyme without its nonprotein moiety is termed an apoenzyme and is inactive.
    If the nonprotein is a metal ion (Zn2+ or Fe2+), it is called a cofactor
    If it is a small organic molecule, it is termed as coenzyme.
  • Coenzymes that only transiently associate with the enzyme are called cosubstrates.
  • Cosubstrates dissociate from the enzyme in an altered state. (ex. NAD+)
A

Holoenzymes

22
Q
  • Enzyme activity can be regulated, that is, increased or decreased, so that the rate of product formation responds to cellular need.
A

Regulation

23
Q
  • Many enzymes are localized in specific organelles within the cell. Such compartmentalization serves to isolate the reaction substrate or product from other competing reactions. This provides a favorable environment for the present in the cel into purpose tipathways of enzymes
A

Location within the cell

24
Q

requires a coenzyme that is oxidized or reduced as the substrate is reduced or oxidized.
Lactate dehydrogenase is an oxidoreductase that removes hydrogen atoms from a molecule.

A

Oxidoreductase

25
Q

is an oxidation that increases the number of C-O bonds and/or decreases the number of C-H bonds.

A

organic oxidation reaction

26
Q

is a reduction that decreases the number of C-O bonds and/or increases the number of C-H bonds.

A

An organic reduction reaction

27
Q

an enzyme that catalyzes the transfer of a functional group from one molecule to another.

A

Transferase

28
Q

Two subtypes of transferase:

catalyzes the transfer of an amino group from one molecule to another;

A

Transaminase

29
Q

Two subtypes of transferase:

-catalyze the transfer of a phosphate group from adenosine triphosphate (ATP) to give adenosine diphosphate
(ADP) and a phosphorylated product (a product containing an additional phosphate group)

A

Kinases

30
Q
  • an enzyme that catalyzes a hydrolysis reaction in which the addition of a water molecule to a bond causes the bond to break. Hydrolysis are central to the process of digestion.
A

Hydrolase

31
Q

enzymes digest fatty
substrates.

A

Lipase

32
Q

enzymes digest protein substrates.

A

Protease

33
Q

enzymes digest carbohydrate substrates.

A

Carbohydrase

34
Q

is an enzyme that catalyzes the addition of a group to a double bond or the removal of a group to form a double bond in a manner that does not involve hydrolysis or oxidation.

A

Lyase

35
Q

effects the removal of the components of water from a double bond

A

Dehydratase

36
Q

effects the addition of the components of water to a double bond

A

Hydratase

37
Q

an enzyme that catalyzes the isomerization (rearrangement of atoms) of a substrate in a reaction, converting it into a molecule isomeric with itself.
• There is only one reactant and one product in reactions where isomerases are operative.

A

Isomerase

38
Q

is an enzyme that catalyzes the bonding together of two molecules into one with the participation of ATP.

A

Ligase