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BMS 102 > Enzymes > Flashcards

Enzymes Flashcards

1
Q

Apoenzyme

A

an enzyme without a cofactor

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2
Q

Holoenzyme

A

complete catalytically active enzyme

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3
Q

Cofactors

A

small organic molecule derived from vitamins and called coenzymes and metals.

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4
Q

Metals

A

tightly bound coenzymes are called prosthetic groups

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5
Q

Free energy

A

the measure of useful energy

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6
Q

When can a reaction take place spontaneously?

A

only if G is negative

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7
Q

When can this reaction NOT take place spontaneously?

A

only if g is positive

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8
Q

The amino acid position is in the N-terminus

A

acetylation

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9
Q

The amino acid position is in the C-terminus

A

Amidation

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10
Q

Ser, Tyr

A

phosphorylation

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11
Q

Pro

A

hydroxylation

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12
Q

Tyr,Lys

A

Methylation

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13
Q

Ser, Thr

A

Palmitaylation

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14
Q

Ser, Thr, Tyr

A

Sulphination

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15
Q

What is the heart of enzyme catalysis

A

the stabilization of the transition state

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16
Q

What are some characteristics of an active site?

A

1) There is a 3-D Cleft
2) Small part of the total volume of the enzyme
3) Unique micro environment
4) Substrates bound to enzymes by multiple weak attractions
5) Binding specificity depends on precisely defined arrangements

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17
Q

Induced Fit Theory

A

Daniel Koshland Jr. states that the active sites of some enzymes assume shape that is complementary to substrate after substrate binds

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18
Q

Binding Energy

A

The free energy that is released when weak interaction between complementary enzymes and substrates are formed.

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19
Q

Kinetics

A

study of the rates of chemical reactions- enzyme catalyzed reactions

20
Q

Velocity

A

the quantity of the reactant A that disappears

21
Q

Rate Constant

A

the way velocity is directly related to concentration of A by constant K

22
Q

First-order reaction

A

where V is directly proportional to the reactant concentration

23
Q

Second-order reaction

A

reaction with 2 reactants

24
Q

Pseudo-first -order reaction

A

if reactant B is more than reactant A, and if A is present in low concentrations, reactions will be first order with respect to A and will not depend on B.

25
Q

Michaelis -Menten Model

A

Initial velocity of catalysis is defined as the number of moles of product formed per unit time shortly after the reaction has begun

26
Q

Vmax

A

when the enzyme is saturated with substrate

27
Q

Km

A

substrate concentration at which reaction velocity is 1/2 max. volume.

28
Q

lower value of Km

A

the tighter the substrates binding

29
Q

Km can be a measure of..

A

the affinity of enzyme for substrate

30
Q

Km values can vary

A

depending on environmental conditions (pH, Temp..)

31
Q

Kcat/KM

A

measure of catalytic efficiency

32
Q

Sequential

A

all substrates must bind to enzyme before any product released, these can be ordered or random

33
Q

Double-displacement

A

one or more products are released before all substrates bind enzyme

34
Q

Allosteric enzymes

A

enzymes that regulate the changes of biochemical compounds in metabolic pathways

35
Q

Allosteric site

A

Have a 2nd regulatory site different from active site

36
Q

Phosphofructokinase

A

one of the most important regulatory allosteric enzyme in glycolysis and composed of 4 subunits

37
Q

Catalytic Strategies

A
  1. Covalent Catalysis
  2. Acid-Base Catalysis
  3. Metal- ion catalysis
  4. Stabilization of transition State
38
Q

Metal Ion uses in catalysis

A
  • Binding substrates in the proper orientation and there fore increasing binding energy
  • may generate a nucleophile by increasing the acidity of a nearby molecule.
  • electrophilic catalyst
39
Q

Metalloenzymes

A

contain tightly bound metal ions

40
Q

Metal-activated enzymes

A

contain loosely bound metal ions

41
Q

Competitive Inhibition

A

resembles the substrate and binds only to the free enzyme active site-not enzyme-substrate complex

42
Q

Kinetics with competitive inhibition

A

no effect on Vmax, but increases Km

43
Q

Uncompetitive Inhibition

A

binds only to enzyme-substrate complex and NOt to free enzyme. Cannot be overcome by the addition of more substrate.

44
Q

Kinetics with uncompetitive inhibition

A

decreases Vmax and decreases Km

45
Q

Noncompetitive Inhibition

A

can bind at same time with substrate to enzyme at different binding sites and can bind free enzyme and enzyme-substrate complex. Cannot be overcome by addition of substrate

46
Q

Kinetics with noncompetitive inhibition

A

decreases Vmax and Km does not change

BMS 102 (7 decks)

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