Enzymes - Biochemistry Flashcards

Dr. Smolanoff, 9/5/2013

1
Q

What is an enzyme? what is the function?

A
  • a biological catalyst, usually a protein
  • function as catalyst (lower activation energy and provide alternate pathway but does not change delta G or free energy difference between substrate and product)
  • enhances speed of forward and reverse reactions
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2
Q

what is a substrate?

A

the reactant that is acted upon by the enzyme

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3
Q

Enzyme characteristics

A
  • effective catalyst
  • high specificity
  • domains. active site where catalysis occurs. have potential control functions.
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4
Q

What are isozymes?

A

Different structural forms of an enzyme that have the same function. Different kinetics.

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5
Q

What are zero order reactions?

A

reaction rate is independent of substrate concentration. V=K

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6
Q

What are first order reactions?

A

reactions rate depends on the concentration of one substrate. V=k (A)

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7
Q

what are second order reactions?

A

Reaction rate depends on the concentrations of two substrates. V=K (A*B)

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8
Q

What are pseudo first order reactions?

A

There are two substrates but only one of them is rate limiting, for example, hydrolysis reactions in aqueous solution. A + H2O C + D

V= K(A)

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9
Q

What are the classes of enzymes? what do they do?

A

1) Oxidoreductases = catalyze oxidation-reduction reactions (NADH)
2) transferases
3) Hydrolases
4) Lyases
5) Isomerases
6) ligases

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10
Q

Describe exergonic and endergonic reactions in thermodynamics.

A

Exergonic reactions (negative delta G), reaction is spontaneous.

Endergonic reactions (positive delta G), reaction is non spontaneous.

When delta G is zero, the reaction is at equilibrium.

possible test question: that exergonic reactions drive endergonic reactions. Therefore the overall free energy change for the reaction in negative (spontaneous)

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11
Q

Why are coupled processes important to living things?

A

many important cellular reactions must run against their thermodynamic potential, that is in direction of positive delta G. for example, hydrolysis of ATP coupled for the reaction of glucose and inorganic Phosphate to occur spontaneously.

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12
Q

What are the difference between “delta G” and “delta G zero”?

A

delta G is an actual value at a cellular level, depends on the actual concentration of reactants and products.

delta G zero is the biochemical standard free energy change value that you can calculate

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13
Q

what are simple enzymes?

A

contain only the polypeptide portion

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14
Q

what are conjugated enzyme?

A

enzyme that contains the polypeptide portion and a non-polypeptide portion.

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15
Q

What are apoenzyme?

A

the protein portion of a conjugated enzyme

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16
Q

what are cofactor (prosthetic group)

A

the nonprotein (commonly metal ions: Fe, Mg, Zn) portion of a conjugated enzyme.

17
Q

what are coenzymes?

A

an organic cofactor, commonly vitamins

18
Q

what are Holoenzyme?

A

the complete, native enzyme

19
Q

what are proenzyme?

A

also known as zymogen. its an inactive precursor of a native enzyme. for example, pepsinogen is a proenzyme which is not active in its present form. needs a part of it cleaved to be the active form of pepsin.

20
Q

what are the functions of coenzymes?

A

accomplish goals amino acide side chain can not, such as in reductions and oxidations

21
Q

what are the characteristic of high energy molecules?

A

energy transfer! 2 classes of biomolecules do this: (1) reduced coenzyme (NADH, FADH2)
(2) high energy phosphate compounds (ATP)

22
Q

give 2 examples of phosphoric acid anhydrides.

A

ADP and ATP

23
Q

why does ATP have a large negative free energy change?

A

The hydrolysis of ATP to ADP (and ADP to AMP) leads to relief of electrostatic repulsion, and stabilization of products by ionization and resonance.