Lecture 5: functions and kinetics Flashcards

1
Q

Types of cofactors

A

1-inorganic: metal ions

2- organic: groups derived from vitamines

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2
Q

acceleration of reactions catalysed by enzymes compared to non-catalysed

A

10^6 to 10^12 fold

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3
Q

enzymes are complementary to ….

A

transition states

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4
Q

catalytic mechanisms leading to enzyme functions

A

1- acid-base catalysis
2-covalent catalysis
3- metal ion
4- orientation based catalysis

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5
Q

How can proton acceptor (general bases) contribute to base catalysis

A

they abstract a proton making the substrate a good nucleophile

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6
Q

How can metal ions catalyse reactions in enzymes

A

1- In oxidation-reduction reactions
2-electronically shielding and stabilising negative charges
3- By providing the correct orientation

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7
Q

which cofactor is used in carbonic anhydrase and what is the function?

A

zinc ions
zinc forces the water to release a proton.
The CO2 goes to the active site and the hydride attacks CO2 producing HCO3-

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8
Q

What are the 6 classes of enzymes

A
1- oxidoreductases
2-transferases 
3-hydrolyaser
4-lyaser
5-isomeraser
6-ligaser
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9
Q

oxidoreductases need…..

and often contain …. metal ions

A

Cofactors

Fe 3+/2+

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10
Q

Which enzyme class kinases do kinases belong to

A

transferases

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11
Q

Which catalytic mechanisms are used for peptide hydrolysis

A

covalent hydrolysis and acid-base catalysis

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12
Q

The active site of chymotrypsins can accomodate which …. side chains

A

aromatic

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13
Q

which enzyme class does adenylate cyklase belong to?

A

lyases

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14
Q

enolase belongs to

A

lyases (hydratase; danner vand)

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15
Q

Enzymer som fjerner carboxyl-grupper er…

A

lyases

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16
Q

Assumptions made in michael mentens kinetics

A

The rate of complex degradation is not reversible

The rate of the formation of complex is the same as the rate of the formation of reactants from the complex

17
Q

The optimum pH of an enzyme is close to the pH of the …….in which the enzyme is found

A

environment