Biochem Final Flashcards

1
Q

General acid catalysis

A

H+ Transfer from acid

Decrease G of transition state

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2
Q

General Base catalysis

A

H+ Abstraction by base

Decrease G of transition state

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3
Q

Concerted Acid-Base catalysis

A

Combined; Can occur simultaneously or sequentially.

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4
Q

Acid-base catalysis

A

pH sensitive

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5
Q

Bovine pancreatic RNase A

A

RNA hydrolysis

2 His Residue (acid/base)

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6
Q

Covalent (Nucleophilic) Catalysis

A

Transient formation of catalytic substrate covalent bond.
Features:
Nucleophilic
e- withdraw by enzyme

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7
Q

Example of Covalent Catalysis?

A

Acetoacetate decarboxylase
Acetoacetate can spontaneously become Acetone + CO2
This happens in Type 1 Diabetics; and people on the keto diet.

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8
Q

Acetate + Lysine

A

Lysine’s NH2 group causes it to form a Schiff Base (imino group).

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9
Q

What is the best Nucleophile?

A

Cysteine

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10
Q

Protonated refers to?

A

Acid

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11
Q

Deprotonated refers to?

A

Base

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12
Q

Metaloenzymes?

A
Metal ions
Roles in catalysis:
Substrate orientation
Redox Reactions (e- transfer)
Electrostatics--Stabilize or sheild charges
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13
Q

Examples of Metaloenzymes? (CA)

A

Carbonic Anhydrase
Cofactor: Zn2+
Zn2+, polarizes water to form OH-, and orient it.

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14
Q

Examples of Metaloenzymes? (RR)

A
Redox Reaction:
Chytochrome C (Fe2+)
Cytochrome C (Fe2+) ---> Cytochrome C (Fe3+)
Shuttles e-'s from Complex 3 to 4
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15
Q

Example of Proximity and Orientation?

A

Imidazole reacting with p-nitrophenylacetate

Tethering of imidazole increases reaction rate ~25%.

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16
Q

Transition State Binding

A

Transition State bound by the enzyme with a high affinity