ENZYMES Flashcards

1
Q

enzymes that remove the elements of hydrogen, H2 or H− plus H+

A

Dehydrogenases

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2
Q

enzymes that hydrolyze proteins

A

Proteases

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3
Q

enzymes that catalyze rearrangements in configuration

A

Isomerases

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4
Q

enzymes that catayze oxidations and reductions

A

Oxidoreductases

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5
Q

enzymes that catayze transfer of moieties such as glycosyl, methyl, or phosphoryl groups

A

Transferases

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6
Q

Enzymes that catalyze hydrolytic cleavage of C—C, C—O, C—N, and other covalent bonds

A

Hydrolases

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7
Q

Enzymes that catalyze cleavage of C—C, C—O, C—N, and other covalent bonds by atom elimination, generating Double bonds

A

Lyases

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8
Q

enzymes that catalyze geometric or structural changes within a molecule

A

Isomerases

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9
Q

Enzymes that catalyze the joining together (ligation)of two molecules in reactions coupled to the hydrolysis of ATP

A

Ligases

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10
Q

are tighty an staby incorporate into a
protein’s structure by covaent bons or noncovaent forces.

A

Prosthetic Groups

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11
Q

serve functions simiar to those of prosthetic groups an overap with them. They bind weakly an transiently to their cognate enzymes or substrates, forming dissociabe compexes.

A

Cofactors

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12
Q

serve as recycabe shuttes that transport many substrates from one point within the cell to another.

A

Coenzymes

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13
Q

refers to reactions for which the ony participating acids or bases are protons or hydroxide ions

A

Specific Acid-Base Catalysis

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14
Q

Reactions whose rates are responsive to all the acis or bases present

A

general acid catalysis/ general base catalysis.

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15
Q

In orer to chemicay interact, substrate moecues must come
within bon-forming istance of one another. The higher
their concentration, the more frequenty they wi encounter
one another, an the greater wi be the rate at which reaction
proucts appear. When an enzyme bins substrate moecues
at its active site, it creates a region of high oca substrate concentration, one in which they are oriented in an ideal position
to chemically interact.

A

CATALYSIS BY PROXIMITY

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16
Q

invove breaking a covaent
bon, enzymes typicay bin their substrates in a conformation that weakens the bon targeted for ceavage through physical
distortion an eectronic poarization

A

CATALYSIS BY STRAIN

17
Q

invoves the formation of a covaent bon between the enzyme an one or more substrates. Also provies a new reaction pathway whose activation energy is lower—an rate of reaction therefore faster—than the pathways avaiabe in homogeneous soution.

A

COVALENT CATALYSIS

18
Q

model accounted for the exquisite specificity of enzyme–substrate interactions, the impie
rigiity of the enzyme’s active site faie to account for the
dynamic changes that accompany cataytic transformations.

A

Lock and Key Model by Fischer

19
Q

which states that as substrates bin to an enzyme, they induce a conformational change that is anaogous to placing a hand (substrate) into a gove (enzyme)

A

Induced fit Model- Daniel Koshland

20
Q

Ideal temperature for enzyme work

A

44- 55 C which is internal body temperature

21
Q

known as the least amount of energy need for a chemical reaction to take place

A

Activation energy

22
Q

what happens when the enzyme is subjected to higher or lower temperatures

A

Denaturation

23
Q

what happens when the enzyme is subjected to higher or lower pH values

A

Ionization

24
Q

Most enzymes exhibit optimal activity at pH value ______________

A

5 to 9

25
Q

o the reaction thus is essentially that o the rate
o the forward reaction.

A

initial velocity

26
Q
  • This is the prevention of enzymatic process as a result of interaction of an enzyme to an inhibitor
A

Enzyme Inhibition

27
Q

inhibits the enzyme outside of the active site, irreversible or reversible

A

NOn-competitive

27
Q

rare form of inhibition characterized by specific binding at the ES Complex, reversible

A

Uncompetitive Inhibition

27
Q

inhibitors compete with the substrate for the active site, reversible

A

Competitive Inhibition

27
Q

bind to the active site of the enzyme via covalent bond, irreversible

A

Irreversible Inhibition