Protein-Enzyme Flashcards

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1
Q

What are Enzymes?

A

Are biological catalysts - they speed up the rate of chemical reactions without being used up →lower the activation energy required

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2
Q

What is the active site?

A

-A specific shape to fit a specific substrate - they are complementary

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3
Q

Why do enzymes have complementary shape?

A

Is determined by the tertiary structure of protein that makes up the enzyme

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4
Q

What is an enzyme-substrate complex?

A
  • forms when an enzyme and its substrate join together
    -The enzyme-substrate complex is only formed temporarily, before the enzyme catalyses the reaction and the product(s) are released
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5
Q

What is a Catabolic reactions?

A

Involve the breakdown of complex molecules into simpler products

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6
Q

What is a Anabolic reactions?

A

Involve the building of complex molecules from simpler ones

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7
Q

How do enzymes lower the activation energy?

A

Enzymes speed up this process by making bond-breaking & bond-forming occur more readily → lowers the activation energy

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8
Q

What is the The lock-and-key hypothesis?

A

Based on the idea that the shape of enzymes are highly specific & fixed structures

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9
Q

The induced-fit hypothesis

A

The enzyme and its active site (and sometimes the substrate) can change shape slightly as the substrate molecule enters the enzyme - these are called conformational changes

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10
Q

Limiting Factors Affecting Enzymes: Temperature

A

Bonds (e.g., hydrogen bonds) holding the enzyme molecules together start to break

Tertiary structure of the protein (enzyme) changes

Active site becomes damaged → substrate cannot bind → enzyme becomes denatured

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11
Q

Limiting Factors Affecting Enzymes: pH

A

Too acidic solutions (H+ ions) or alkaline solutions (OH- ions) can cause hydrogen & ionic bonds to break

Shape of the active site changes → enzyme-substrate complexes form less easily - enzyme denatures

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12
Q

Limiting Factors Affecting Enzymes: Enzyme concentration

A

Higher the enzyme conc. → greater number of active sites available → greater likelihood of enzyme-substrate complex formation

This relationship is linear until the amount of substrate becomes limited …

… any further increase in enzyme concentration will not increase the rate of reaction - substrate becomes the limiting factor

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13
Q

Limiting Factors Affecting Enzymes: Substrate concentration

A

Greater the substrate concentration → greater likelihood of enzyme-substrate complex formation → higher the rate of reaction

When all active sites are saturated (full), no more enzyme-substrate complexes can form → rate of reaction plateaus

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14
Q

Competitive inhibitors

A

Have a similar shape to substrate molecules → compete with the substrate for the active site

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15
Q

Non-competitive inhibitors

A

Bind to the enzyme at an alternative site → alters the shape of the active site → prevents the substrate from binding to it

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16
Q

Inhibitors in metabolism

A

-Metabolic reactions must be tightly controlled and balanced → presents the excess formation of products
-End-product can then detach from the enzyme → allows the active site to reform and the enzyme to return to an active state → occurs in a continuous feedback loop