Exam 3 enzymes Flashcards

1
Q

Plasma/serum enzyme concentration levels are useful in

A

diagnosis in disease or physiologic abnormalities

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2
Q

Isoenzyme

A

particular enzyme may exist in multiple forms in varying quaternary structures.

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3
Q

Isoenzymes are differentiated based on

A

Electrophoretic mobility, solubility, or resistance to inactivation.

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4
Q

Isoform

A

Enzyme is subject to post-translational modifications.

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5
Q

___ and ____ contribute to heterogeneity in properties and functions.

A

Isoenzyme and Isoforms

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6
Q

Proenzyme (zymogen)

A

secreted in inactive form (mostly digestive enzymes)

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7
Q

Inorganic co factors are composed of

A

Metal Ions as activators (Cl-, Mg+, Cu-)

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8
Q

Organic cofactors include

A

Coenzymes: NAD; ATP; ADP
Prosthetic group: coenzyme bound tightly to the enzyme
Holoenzyme: complete and active system
Apoenzyme: (enzyme portion + coenzyme)

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9
Q

Michaelis and Menten Theory

A

Substrate readily binds to free enzyme at a low substrate concentration. Reaction rate (velocity) steadily increases when more substrate is added. With the amount of enzyme exceeding the amount of substrate.

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10
Q

Michaelis- menten constant

A

Km= [S] 1/2 max, indicates the amount of substrate needed for a particular enzymatic reaction.

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11
Q

In the michaelis-menten constant, if [S] is greater than Km by factor of 100

A

Follow zero order kinetics

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12
Q

If more than one substrate

A

Lowest Km is a natural substrate (not man made)

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13
Q

Lineweaver-burk plot

A

is a double reciprocal of Michaelis-Menten- yields a straight line.
Most accurate and convenient to determine Vmax and Km.
Reciprocal is taken of both substrate concentration and velocity of enzymatic reaction.
Can be used to identify the type of inhibitor.

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14
Q

Optimal pH for enzymes

A

7.0-8.0, may denature an enzyme or influence in ionic state if >,<

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15
Q

Common activators:

A

Calcium, iron, magnesium, manganese, zinc, and potassium.
Nonmetallic: bromide and chloride.
If there is excess, it may inhibit reaction.

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16
Q

Coenzymes (organic)

A

Nucleotide phosphate and vitamins.
When quantitating an enzyme that requires coenzymes, always provide excess to avoid dependency.

17
Q

When measuring enzyme activity:

A

No inhibitors.
Control variables.
Use coupled reactions.
Colorimetric.
UV involving NAD and NADH (340 nm)
Measured at zero order region.

18
Q

Measurement of Enzyme Mass

A

Quantify enzyme concentration by mass.
CK-MB.
Can overestimate due to cross-reactivity with inactive enzymes, macroenzymes, zymogens or partially digested enzymes.
Can also be quantified by electrophoretic techniques- isoenzymes/isoforms