Enzymes (Chapter 3 ) Flashcards

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1
Q

WHAT ARE ENZYMES

A

Enzymes are biological molecules

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2
Q

WHAT IS THE DEFINITION OF BIOLOGICAL MOLECULES

A

Biological molecules are substances which speed up a chemical reaction by lowering the activation energy in living organisms without changing nor being used up

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3
Q

WHAT KIND OF PROTEINS ARE ENZYMES

A

Enzymes are globular proteins

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4
Q

WHAT ARE SUBSTRATES?

A

Substrates are substances on which Enzymes act.
E.g. Lipase act on lipids
Protease act on proteins

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5
Q

WHAT ARE ACTIVE DOES ALSO KNOWN AS

A

They are known as catalytic sites.
It is were the reaction takes place

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6
Q

STRUCTURE OF ENZYMES

A

Enzymes have a teritary structure and some enzymes have also have Quaternary structure

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7
Q

ENZYMES ARE SPECIFIC TO THEIR ACTIONS.
WHAT PROPERTIES MAKE ENZYMES SPECIFIC IN THEIR ACTIONS?

A

Presence of specific active site - contain survivors sequence of amino acids in the polypeptide, folding of amino acids and form a 3D shape and specific bonds maintain its shape

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8
Q

MECHANISM OF ENZYME ACTION

A

Enzyme + substrate —-> enzyme substrate complex —> formation of enzyme-product complex —> enzyme + product

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9
Q

LOCK AND KEY MODEL

A

Enzyme = lock.
Substrates = key.
Fire the enzymes to work you need a specific substrate
In this principle, The active site is specific due to the specific sequence of amino acids and is rigid.

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10
Q

INDUCED FIT MODEL

A

In this principle The substrate is partially complementary to the active site.
In this the active site of enzymes are slightly changeable, sure to it’s flexibility enzymes are slightly changeable.

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11
Q

FACTORS AFFECTING ENZYMATIC ACTIVITY

A
  1. Enzyme concentration:
    Concentration : Rate of reaction
  2. Substrate concentration
    Substrate concentration : Rate of reaction
  3. Temperature
    Temperature : Rate of reaction
  4. pH
    Increasing or decreasing the pH slightly can denature the enzyme
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12
Q

SUBSTRATE CONCENTRATION

A

• When every substrate is occupied by enzymes it is known as the substrate saturation.
• If as you increase the substrate concentration but the graph remains constant, this indicates that the enzyme concentration is limited ( enzyme acts as a limiting factor), and in order to increase the graph we should increase the enzyme concentration.
• Inc substrate/ enzyme concentration, collisions Inc, the ES complex formation Inc, and therefore the product amount per unit time Inc.

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13
Q

TEMPERATURE

A

Temp Inc, K.E. Inc, random movement of enzymes and substrate Inc, effective collisions Inc, ES complex formation Inc, and product formation Inc, RoR Inc.

If temperature increases beyond optimum temperature then the enzyme bibs break and the active site shape changes and enzyme denatures.
H2 bonds break first, then ionic bonds and then peptide bonds.
Once the enzyme denatures it will not return to it’s original shape. However, if the enzyme is inactive it will become active of you one the temp.

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14
Q

PH

A

If you slightly increase our decrease the pH then the enzyme immediately denatures.
When OH and H starts to form a bonds with the active site, it alerts the shaper of the active site. If the active site changes, no ES complex forms.

1-6 pH is acidic - have high concentration of H+
7pH is neutral - have equal concentration of H+ and OH-
8-13pH is alkali - have high concentration of OH-

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15
Q

WHAT IS OPTIMUM TEMPERATURE

A

It is the temp where the rate of reaction is max, where the most ES complexes are formed.

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16
Q

WHAT IS VMAX

A

The point where there’s a maximum rate of reaction/maximum enzymatic activity.
• When all the enzymes are attached to the substrate
• there’s a substrate saturation on active site

17
Q

WHAT OS SUBSTRATE SATURATION

A

The point where all of the substrates are occupied by enzymes

18
Q

WHAT IS THE TURN-OVER RATE

A

No. Of substrate molecules converted into products by enzyme per time unit

19
Q

WHAT IS THE KM VALUE

A

Concentration of substrate that produces half VMAX is referred as Michoelis Menton constant which is represented as KM.

20
Q

MICHAELIS-MENTON CONSTANT

A

• Half of the A.S. are occupied by the substrate
• The KM value indicates affinity of enzyme to it’s substrate
• The lower the KM value the higher the affinity
• KM is irreversibly proportionally with enzyme affinity to the substrate VMAX won’t be affected by KM

21
Q

ENZYME AFFINITY

A
22
Q

FACTORS AFFECTING THE KM VALUE

A
  • Type of substrate
  • Temperature ( works best at opt. Temp)
  • pH value
  • Presence of particular ions
  • Presence is inhibitors ( decrease the enzymatic activity)