Midterms_Enzymes Flashcards

1
Q

Explains the specificity of enzyme, enzyme is pictured as conformationally rigid.

A

Emil Fischer’s Lock and Key Model (1984)

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2
Q

For catalytic isomerizations.

A

Isomerases

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3
Q

Occurs when an inhibitor binds with an enzyme but does not dissociate from it under reaction conditions or within time-frame.

A

irreversible inhibition

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4
Q

Aka absolute specificity

A

Substrate Specificity

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5
Q

Oxidizes or reduce substrate by transferring hydrogen or electrons

A

Oxido-Reductates

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6
Q

Cause condensation of two molecules by splitting a phosphate bond

A

Ligases or synthetases

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7
Q

characterized by the maintenance of enzyme activity even at high inhibitor concentrations

A

partial inhibition

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8
Q

Structure is maintained by weak IMF

A

Koshland’s Induced Fit Hypothesis (1958)

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9
Q

Hanes-Woolf Plot

A

S/v = (1/vmax)S + Km/Vmax

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10
Q

Inhibitor binds to the enzyme at non active sites and reduces affinity of enzyme to substrate.

A

Noncompetitive inhibitors

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11
Q

Approach of the substrate in induced fit is viewed as

A

perturbation

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12
Q

Studies enzyme-catalyzed reaction rates and how changes in experimental conditions affect the reaction rates.

A

Enzyme kinetics

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13
Q

Inhibitor may dissociates more easily from the enzyme after binding

A

Reversible inhibitors

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14
Q

enzymes for hydrolytic reactions

A

hydrolases

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15
Q

Lineweaver-Burk equation

A

1/v = km/vmax (1/s) + 1/Vmax

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16
Q

Michaelis Menten Kinetics do not apply to irreversible inhibition (True or False)

17
Q

compounds bind to enzyme and reduce their activity

A

enzyme inhibitors

18
Q

removes groups and transfer them to acceptor molecules

A

Transferases

19
Q

Selectivity of the enzyme to their substrate, molecular recognition mechanism

A

Specificity

20
Q

proteins produced by living cells and acts as biological catalysts

21
Q

Essential feature of enzyme-catalyzed reactions is

A

saturation

22
Q

In the absence of _______, the enzyme will be inactive even if there are plenty of substrates.

A

Specific co-factor

23
Q

inhibitor forms a stable complex with the enzyme

A

Irreversible inhibitors

24
Q

Factors affecting enzyme activity

A

Temperature, pH, enzyme concentration and substrate concentration

25
Recognition and specificity is based on ______
Structural complementarity
26
are specific to substrates having similar bonds and similar structure
Bond specificity
27
Eadie-Hofstee Plot
v = -km(v/s) + Vmax
28
Enzyme activity depends on substrate concentration
Michaelis-Menten Theory
29
is specific to a bond and groups surrounding the bonds
Group specificity
30
enzyme can act on different substrates having similar molecular geometry and hence, here specificity is very less.
geometrical specificity
31
Enzymes are highly specific and produce only the expected products from the given reactants or substrates (there are no side reactions). (True or False)
True
32
remove groups from the substrate by hydrolysis to form double bonds or conversely, add groups to the double bond
Lyases
33
specific not only to substrate but also to its optical configuration
Optical or stereo specificity
34
Inhibitors bind to ES complex but not to enzyme
Uncompetitive
35
refers to the catalytic ability of an enzyme to increase the rate of reaction.
Enzyme activity