BMS 108 Ch. 04 Enzymes Flashcards

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0
Q

Where does the substrate fit? What might be needed to fully activate the enzyme?

A

One the activation site; cofactors and coenzymes

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1
Q

What is an enzyme? What is the mechanism by which it does its job?

A

A protein that speeds up a chemical reaction; works by lowering the energy of activation

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2
Q

What forces can easily destabilize an enzyme?

A

Changes in pH and body temperature

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3
Q

What is conformation?

A

Highly ordered three dimensional shapes of enzymes.

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4
Q

What is a conformational change?

A

Change in the three dimensional shape of a protein

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5
Q

What does it mean to denature a protein?

A

Change in the structure of a protein

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6
Q

What is the difference between a competitive and noncompetitive inhibitor? What is it called when a protein is inhibited by its own product? What is the mechanism?

A

Competitive - competes with the substrate for active sites
Noncompetitive - binds to regulatory sites (not necessarily active sites)

Feedback inhibition; Activity is blocked by the product of the reaction that was catalyzed by the enzyme

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7
Q

What is the action of phosphatases and kinases?

A

Phosphatases are enzymes that remove phosphate groups from substrates; kinases transfer phosphates from ATP to specific substrates.

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8
Q

How and why does a coenzyme binding to a regulatory site change the activity of the enzyme?

A

Coenzymes form an ionic bond with the enzyme causing a conformational change that changes the shape of the active sites of the enzyme.

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9
Q

The ability of enzymes to lower energy requirement is due to its __________.

A

structure

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10
Q

Enzymes contain pockets called _______ ______ into which __________ (reactants/ligands) fit.

A

Active sites; substrates

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11
Q

Enzymes act by bringing ________ close together so they can react.

A

substrates

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12
Q

Describe the mechanism of enzyme action.

A
  1. Substrates fit into the active sites
  2. Enzyme-substrate complex is formed
  3. Reaction occurs
  4. Products dissociate
  5. Enzyme is unaltered
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13
Q

Most enzymes end with ______.

A

-ase

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14
Q

What do phosphatases do?

A

removes phosphate groups

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15
Q

What two things effect the optimal range for enzyme activity?

A

Temperature and pH

16
Q

What are cofactors? and coenzymes?

A

molecules necessary for normal enzyme activities

metal ions; small biological molecules such as vitamins

17
Q

How do cofactors and coenzymes work?

A

Cofactor/coenzymes binding changes conformation of active site, which aids in temporary bonding between enzymes and substrates.

18
Q

How are enzymes activated and deactivated?

A

Many are activated by phosphorylation (with phosphatases) and dephosphorylation (with kinase).
- others are activated by 2nd messenger (diffusable intracellular molecules or ion carrying a message)

19
Q

Enzymes are also regulated by ______ of enzymes - breakdown and re-synthesis of enzymes therefore allowing genes to alter enzyme activitiy as conditions change.

A

turnover

20
Q

What are the three types of enzyme inhibitors?

A
  1. Competitive - compete with substrates for active sites
  2. Noncompetitive - bind to regulatory sites (not necessarily active sites)
  3. Feedback - activity is blocked by a product of the reaction that was catalyzed by the enzyme
21
Q

What does it mean when we say an enzyme is “rate-limiting” in a chemical reaction?

A

Rate of product formation increases as substrate concentration increases until reaction rate reaches a plateau. This is where the enzyme is said to be saturated.

22
Q

What is the law of mass activation?

A

The principle that reversible reactions will be driven from the side of the equation where the concentration is higher to the side where the concentration is lower.

23
Q

What is a metabolic pathway?

A

Sequences for enzymatic reactions that begin with initial substrate, procedes through intermediates and end with a final product.

24
Q

What is end-product inhibition?

A

It occurs when one product in a divergent pathway inhibits activity of the branch point enzyme.

  • prevents final product accumulation
  • causes the reaction to favor alternate pathway
  • occurs by noncompetitive/allosteric inhibition whereby product binds to enzyme causing it to change to an inactive shape