Enzymes 1 Flashcards

1
Q

Two models of substrate binding

A

Lock and key

Induced fit

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2
Q

What does substrate binding induce

A
Conformational change (enhanced interaction). 
Transitional state complex is formed which is an unstable complex in which bonds in substrate are strained
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3
Q

What is the lock and key model

A

-binding through hydrophobic, es and hydrogen bonds

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4
Q

In the lock and key model, what is binding prevented by

A

steric hindrance and charge repulsion

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5
Q

In induced fit, what happens

A

Side chains of amino acids reposition

Binding interactions increase

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6
Q

Why are transitional state complexes useful in the pharmaceutical industry

A

Bind more tightly to enzymes than substrates so when making an inhibitor, can make a transition state comples

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7
Q

What are coenzymes

A

Non peptide molecules

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8
Q

What can we get coenzymes from

A

vitamins: water soluble or lipid soluble

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9
Q

Classes of coenzymes and their functions

A

Activation transfer

Ox-Red

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10
Q

What do activation transfer enzymes do and what bonds do they form

A

move functional groups around

form covalent bonds

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11
Q

What do ox-red enzymes do

A

Help electrons on/off

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12
Q

What do metal ions in catalysis do

A

electrophiles can stable anions

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13
Q

What are isoenzymes

A

Different amino acid sequence but catalyst same reaction

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14
Q

What are multi enzyme complexes

A

Enzymes that are similar/in same biological pathway stay together and associate to form a multi-enzyme comples

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15
Q

Different types of enzymes in serum

A

Serum specific enzymes
Secreted enzymes
Non serum specific enzymes (i.e. released due to cell turnover/damage)

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