Enzymes II Flashcards

1
Q

what are perfect enzyme reaction rates limited by

A

Diffusion

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2
Q

Rate of reaction =

A

Kcat [ES]

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3
Q

Turnover number, Kcat =

A

Vmax / [enz]

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4
Q

whats on a serine protease active site and how does it work

A

A very reactive serine group, CH2OH

They attack the peptide bond to form an acyl-chloride so its more easily hydrolysed by water

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5
Q

What enzymes have serine active sites

A

Chymotryspin and tryspin

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6
Q

What is the catalytic triad

A

Ser 195, His 57 and Asp 102

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7
Q

How does the catalytic triad work

A
  • The positive charge is moved from the serine to the aspartate making the serine very negatively charged
  • The negative oxygen in the serine group will attack the ketone group in the peptide bond resulting in half of the polypeptide being protonated and released but the other half links onto the enzyme creating an ester intermediate
  • Water attacks the acyl-enzyme releasing the second half of the polypeptide, leaving the enzyme unchanged
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8
Q

Where does chymotrypsin cleave at

A

Aromatic tissues

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9
Q

Why does chymotrypsin cleave here

A

Its active site pocket is lined by hydrophobic residues therefore they have an attraction to the hydrophobic side chains of the aromatic residues

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10
Q

Where does trypsin cleave at

A

Lysine and arginine

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11
Q

Why does trypsin cleave here

A

Its active site pocket has a negatively charged side chain therefore will form an electrostatic attraction with the positive residues

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12
Q

Where does elastase cleave at

A

Small substrates

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13
Q

Why does elastase cleave at

A

Its active site pocket is very narrow since its constricted by other residues so only small side chains can enter

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14
Q

What is the electron transport chain

A

Cytochromes that take electrons and pass them along other cytochromes. Eventually they pass the electrons to oxygen to make water.

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15
Q

What is the net effect of the electron transport chain

A

Protons are generated and they are exported out of the mitochondria

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16
Q

What drives ATP synthase

A

The electrochemical proton gradient

17
Q

What is the structure of ATP synthase

A

has 3 active sites activated by a rotating spindle

Every time it rotates 120 degrees an ADP and Pi molecule is bound together forming ATP

18
Q

What does topoisomerase II do

A

Its an enzyme that untangles the mitotic spindle so that chromosomes can be separated

19
Q

How does topoisomerase II work

A
  1. Binds to a segment of one chromosome, the gate segment
  2. Binding of ATP causes a segment perpendicular to the gate segment, the transport segment, to be clamped into position
  3. The enzyme makes a transient break in the gate segment so the transport segment passes through into holder on the other side
  4. The break in the gate segment is resealed and the transport segment is resealed
  5. Hydrolysis of the ATP resets the cycle
20
Q

Why is this enzyme targeted

A

Anti-cancer drugs can interfere with enzyme as it can interfere with DNA replication