Enzymes II Flashcards

1
Q

Nucleophilicity is related to

A

basicitiy

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2
Q

Nucleophilies can

A

covanteltly bond to electron deficient centers

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3
Q

electrophilic group are.

A

electron deficient so they love electrons

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4
Q

Some nucleophiles groups are

A

hydroxyl group, sulfhydryl group, amino group, imidazole group

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5
Q

Some electrophilles groups are

A

protons, metal ions, carbonyl carbon atom, cationic imine

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6
Q

Partial proton donation is also

A

general acid catalysis

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7
Q

abstraction is also known as

A

general base catalysis

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8
Q

What amino acids participate in acid-base catalysis?

A

Asp, Glu, Lys, Arg, and His

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9
Q

What makes a good catalyst

A

good leaving groups

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10
Q

for a good catalyst, reverasibily

A

of the bond fromed is key

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11
Q

A good catalyst correlates with

A

polarizability and how mobile electrons are

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12
Q

highly polarized equals

A

highly breakables

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13
Q

Step 1 in RNase A for His 12

A

abstracts proton from 2’-OH

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14
Q

His 12 causes

A

a nucleophillic attack on P

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15
Q

His 119 step 1

A

protonates a leaving group causing bond breaking

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16
Q

Step 2 for RNase A His 119

A

deprives H+ from H2O which results in OH- attacking P

17
Q

Step 2 His 12

A

donates its proton → 2’,3’ cyclic intermediate is broken.

18
Q

Covalent catalysis is via

A

transient formation of covalent ES intermediate

19
Q

covalent catalysis is usually

A

a nuucleophile attacjs abn electrophile and forms covalent bond with it

20
Q

What are the 2 classes of metal ion catalysis

A

metalloenzymes and metal-activated enzymes

21
Q

Decarboxylation of acetoacetate is by

A

primary amine (via Schiff bond)

22
Q

What is the first step Decarboxylation of acetoacetate

A

Nucleophilic attack by amine
 formation of covalent bond

23
Q

What is step 2 of the Decarboxylation of acetoacetate

A

Catalyst becomes electron-
deficient  e - from reaction cente

24
Q

Metal ion catalysis acts in 3 ways

A
  1. Bind to substrates (orient properly for reaction).
  2. Transiently change redox state (mediate redox reaction).
  3. Stabilize/shield negative charges.
25
Q

Metalloenzymes are

A

tightly bound and usually transition metals

26
Q

Examples of matelloenzymes

A

Fe 2+ , Fe 3+ , Cu 2+ , Zn 2+ , Mn 2+ , Co 2+

27
Q

Metal activated enzymes

A

loosely bound metal from solution, alkaline

28
Q

Zn2+ is coordinated

A

by the imidazole of 3 His and a water

29
Q

Binding to E forces

A

substrate in a orient way which is rotational, translational motions cease and actives groups face each other

30
Q

Proximity and orientation effects comes at the expense of

A

lost of entropy and is compensated by the binding energy of E to S

31
Q

theres a preferential binding to the

A

ES -transition state

32
Q

the transition state binds

A

the enzyme’s active site tighthly and acts a potent inhibtor

33
Q

The transition state analog helps

A

confirming the structure of the natural transition state

34
Q
A