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BIOCHEM MIDTERM > CHAPTER 6 > Flashcards

CHAPTER 6 Flashcards

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1
Q

BIOLOGICAL CATALYST

A

ENZYME

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2
Q

INCREASE RATE OF RXN 10^20

A

ENZYME

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3
Q

CATALYZE ONLY ONE STEREOISOMER OTHERS FAMILY OF REACTIONS

A

ENZYME

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4
Q

ALL ENZYMES ARE PROTEINS

A

ALL ENZYMES ARE PROTEINS

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5
Q

Rate of Rxn depends on

A

Activation Energy DG

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6
Q

Provides an alternative pathway with a lower activation Energy

A

Enzyme

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7
Q

The free Energy of Activation are the
Free Energy of Change

A

Arrow under the parabola
Arrow under the Free Energy of Activation

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8
Q

Free Energy of Activation Catalyzed reaction is
Free Energy of Activation Uncatalzyed rxn is

A

Much Less/ Less than the
Greater

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9
Q

Most Important Function of Proteins is
Performed by the

A

Catalysis
Protein, Enzyme

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10
Q

Enzyme Activity Decreases because of

A

Thermal Denaturation

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11
Q

Two models for Binding of Substrate to an Enzyme:

A

Lock and Key Model
Induced Fit Model

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12
Q

Complementary Shape of the Substrate and The Binding Site/ Portion of the Enzyme

A

Lock and Key Model

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13
Q

Induces Changed after the Substrate Binds to the Active Site Resulting in Complementary change of the active site and the substrate

A

Induced Fit Model

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14
Q

What Occurs After Enzyme Transition Complex is Formed

A

Catalysis Occurs

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15
Q

In the complex, S is bound to the enzyme with correct orientation with respect to the atoms it is to react with
Both Proximity and Orientation _______
Substrate + Enzyme Forms —–>

A

Speed Up the Reaction
Product + Enzyme —–> Product is released into
Enzyme + Product

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16
Q

Enzyme Catalyze Reaction Example is
It: Cleaves
Catalyzes Hydrolysis of

A

Chymotrypsin
Lys, His, Gln
Peptide bonds

17
Q

Hydrolysis of P-nITROPHENYL Ester by Chymotrypsin
Rate is _________ on Substrate
At _____ (S) rxn rate increase with _____ on (S)
At _____ (S) rxn rate changes very_____ and a _____ rate is reached
Graph is __________

A

Dependent
low, increase
Very Little
max
Hyperbolic

18
Q

ATCase- an _________
Similar to kinetic behavior of_______
Allosteric Proteins- Proteins in which subtle changes at one site affect the ________ and ________ at another site
_____________ and myoglobin are ____________

A

Allosteric Protein
Hemoglobin
Structure and Function
Chymotrypsin, Non allosteric Proteins

19
Q

ATcase-
_________ the reaction
Carbamoyl Phosphate +_________ —-> Carbamoyl Aspartate +
Leads to formation of CTP and UTP needed for biosynthesis of _____ and ______
Rxn rate depends on (S) which is _______
Graph is ________

A

Aspartate Transcarbamoylase
catalyzes
Aspartate
HPO42-
RNA AND DNA
Aspartate
Sigmoidal

20
Q

Michaelis-Menten Approach to Enzyme Kinetics
Full names: (1913, __________ and __________)
Basic Model for __________
Enzymatic Conversion the S——>___
Mechanism of Enzymatic Reaction:

A

Leonor Michaelis and Maud Menten
Nonallosteric Enzymes
P
E+S k-1<——>k1 ES —–>k2 E+P

21
Q

Solve for Concentration of Complex (ES)

Michaelis Menten Constant: Km

ES COMPLEX CONCENTRATION

A

(E) = (E)t -(ES) (E)t= Total (E)

(E)t-(ES)(S)/(ES) = Km

(E)t(S)/km+(S)

22
Q

If S Completely Saturates E (ES) = (E)t
If S saturates E

A

(ES) = (E)t
k2(E)t(S)/Km+(S)

23
Q

Michaelis Menten Equation:
When (S)=Km
When the Rxn rate is half of its max value,
the (S) conc. is
Km is only appropriate for Enzymes that Exhibit

A

V= Vmax(S)/Km+(S)
Vmax/2
Equal to Km
Hyperbolic Curve V vs (S)

24
Q

Linearizing Michaelis Menten Equation:
Equation For Hyperbola:
Equation For a Straight Line:

A

V=Vmax(S)/Km+(S)
1/V=Vmax(S)/Km+(S)= Km/Vmax+(S) +(S)/Vmax+(S)
1/V = Km/Vmax(S) + 1/Vmax

25
Q

Line Weaver Burk Double Reciprocal Plot:
Gives Straight Line: Y and X
Gives Slope: M
Gives Intercept: B

A

1/V = Km/Vmax(S) x 1/(S) + 1/Vmax
1/V vs 1/(S)
Km/Vmax(S)
1/Vmax

26
Q

Enzyme Inhibition:
An _________ ,Is a substance that interferes with the _____ of and enzyme and ____ the rate of reaction
An _______ is a substance that decreases the rate of an ___________ reaction

A

Inhibitor, Action, Slows
Inhibitor, enzyme-catalyzed

27
Q

Reversible Inhibitor:
A substance that ______ to an Enzyme it can inhibit but it can be ______

A

Binds, Released

27
Q

Competitive Inhibitor:
Binds to the _____ site and ______ access to it by substrate
Compete with the _______ for binding to the enzyme’s ________ site
Non-Competitive Inhibitor:
_______ to a site other than the _____ site and inhibits enzyme by _______ its conformation
Cannot be overcome by _________ substrate concentration
Mixed Competitive: The binding of Inhibitor affects the binding of S, and Vice Versa
Uncompetitive Inhibitors: Binds only to ES Complex preventing the Complex from releasing Products

A

Active, Blocks
Substrate, Active
Binds, Active, Changing
Increasing

28
Q

Irreversible Inhibitor:
A substance causes ________ that cannot be _________.
Usually Involves the formation or breaking of covalent bonds to or on enzyme

A

Inhibition, Reversed

29
Q

Competitive Inhibition:
EI <—-> +I E <—–> +S ES <—–> E+P
I = (I)/KI
I/V=Km/Vmax (I+(I)/KI) x 1/(S) + 1/Vmax
Km ________ because High S outcompetes I both vying at the same site, Vmax does not change.

A

Increases

30
Q

Competitive Inhibitor Non-Comp
Site Binding:
Change of
Structure of E:
Effect on Km:
Effect on Vmax:

A

Active Site At a Site other than the Active Site
No Yes

Change No Change
No Change Change

30
Q

Non-Competitive Inhibition:
1/V= Km/Vmax (I + (I)/KI) x 1/(S) +1/Vmax (I + (I)/Ki)
Vmax _______ while Km remains _______
S does not overcome Noncomp I as they are not _______ for the same site

A

Decreases
Constant
Competing

31
Q

Enzyme Commission Classification and Nomenclature
- __ MAJOR CLASSES
Class. Sub Class, Sub-subclass, Specific Enzyme
1. Oxi
2. Trans
3.Hydro
4.Ly
5.Isome
6.Liga

A

6
Oxidoreductases
Transferases
Hydrolases
Lyases
Isomerases
Ligases

32
Q

Catalyze oxidation-reduction reactions, electrons are –__________ from _____ molecule to another
Example: Alcohol ______ EC (1.1.1.1)

A

Oxidoreductases
Transferred, one
Alcohol Dehydrogenase

32
Q

Transfer ___________ from one molecule to another
Example: Hex_____ EC (2.__.__.1)

A

Transferases
Functional Groups
Hexokinase (2.7.1.1)

33
Q

Catalyze the ______ of Various bonds, Breaking molecules down using _______
Example: Lip_____ EC (__.__.1.__)

A

Hydrolases
Hydrolysis, Water
Lipase (3.1.1.3)

34
Q

Catalyze the ________ or ________ of groups to form double bonds or break double bonds without _______ or oxidation
Example: ________ Decarboxylase EC (__.1.1.1)

A

Lyases
Addition or Removal, Hydrolysis
Pyruvate Decarboxylase (4.1.1.1)

35
Q

Catalyze the ________ of atoms within a molecule, facilitating _______ changes.
Example: Phospho____ Isomerase EC (__.__.__.9)

A

Isomerases
Rearrangement, structural
Phosphoglucose Isomerase (5.3.1.9)

36
Q

Catalyze the formation of ___ molecules, with the formation of new _____________ usually accompanied by hydrolysis of _____
Example: DNA ______ EC ( __.5.__.1)

A

Ligases
Two, chemical bonds, ATP
DNA Ligase (6.5.1.1

BIOCHEM MIDTERM (4 decks)

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