Exam 1 | Chp. 2 & 3 Flashcards

Light, Spectrophotometry, Electrochemistry, Enzymes, Chromatography, Electrophoresis, & Immunoassays (46 cards)

1
Q

Apoenzyme

A

protein core without cofactor

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2
Q

cofactor

A

non-protein that activates complex

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3
Q

holoenzyme

A

apoenzyme + cofactor(s)

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4
Q

Enzymes do not alter

A

chemical bonds

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5
Q

Enzymes allow

A

changes to occur with less energy expended

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6
Q

Chemical properties of an active site determine 2 things

A
  • Specificity of an enzyme for its substrate
  • The reaction it catalyzes
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7
Q

Absolute specificity

A

enz catalyzes only one rxn

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7
Q

Group specificity

A

enz only acts on molecules w/ specific functional groups

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7
Q

Linkage specificity

A

enz acts on particular types of chemical bonds regardless of mol structure

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7
Q

Stereochemical specificity

A

enz only acts on a particular isomer

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8
Q

3 types of cofactors

A
  1. Coenzymes
  2. Prosthetic Groups
  3. Metal ion activators
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9
Q

Coenzyme is a non-protein organic substance that

A

loosely attached to apoenzyme, related to vitamins

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10
Q

Prosthetic Group is a non-protein organic substance that

A

firmly attached to apoenzyme, ex is NAD, NADP

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11
Q

Metal Ion activators

A

may be an integral part or loosely bound to apoenzyme

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12
Q

Oxidoreductases catalyze

A

redox rxns

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13
Q

Transferases catalyze

A

transfer of functional group

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14
Q

Hydrolases catalyze

A

hydrolysis rxns

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15
Q

Lyases catalyze

A

removal of chemical groups

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16
Q

Isomerases catalyze

A

conversion of bonding patterns

17
Q

Ligases catalyze

A

coupling of molecules with the hydrolysis of ATP bonds

18
Q

Isoenzymes

A

different multimeric forms of an enzyme

19
Q

Energy required for a substrate to be activated is provided by

A

the free energy of binding S to E

20
Q

Enzyme substrate complex breaks down to give these two things

A

rxn products (P) and free enzyme (E)

21
Q

A rxn can be forced to proceed in only one direction by

A

using a secondary rxn to remove product from availability

22
Rxn rate is represented by the letter _ and is postive for a ________ _____ and negative for a _______ ___
k; + for forward rxn, - for reverse rxn
23
5 factors that affect enzyme activity
1. substrate concentration 2. enzyme concentration 3. temperature 4. pH 5. cofactors
24
First order kinetics
Velocity and [S] are directly proportional and almost equal. - [S] is rate limiting
25
Forming the E-S complex activates
the substrate molecule
26
Zero order kinetics
Reaction rate is independent of [S]
27
Measuring enzyme activity can only occur if
all reactions are at zero order kinetics
28
The MM constant (Km) is useful for
determining optimal [S] that is not rate limiting
29
If [S] > Km by a factor of 100, the reaction is following
Zero-order kinetics
30
If [S] > Km by a factor of less than 100, the reaction is following
First-order kinetics
31
Km represents the
[S] needed to achieve 1/2 Vmax
32
Activators
Small molecules like Zn++ and Mg++ that increase rxn rate
33
Coenzymes are similar to activators in that
some enzymes require their presence for their full activity
34
Inhibitors
Substances that selectively affect rxn velocity + Km to limit enzyme activity
35
Competitive Inhibitor (Def and Effect on KM + Vmax)
Similar to + competes w/ substrate for active site binding - ↑ Km - No effect on Vmax
36
Noncompetitive Inhibitor (Def and Effect on KM + Vmax)
Binds allosteric (non active) site -> conformational change -> altered active site that doesn't bind substrate - No effect on Km - ↓ Vmax
37
Uncompetitive Inhibitor (Def and Effect on KM + Vmax)
Binds E-S to form ES inhib. complex that yields NO product - ↓ Km - ↓ Vmax
38
You can reverse the action of a competitive inhibitor by
increasing [S]
39
What inhibitor only binds when substrate is bound to enzyme
uncompetitive
40
What inhibitor yields no product
uncompetitive
41
In electrochemistry, the anode is __ and the cathode is __
42
Absorbance and concentration are _____ proportional
directly - As concentration increases so does absorbance
43