Lecture 4 Flashcards

protein function/ enzymes and kinetics

1
Q

enzymes

A

complex biological molecules that behave as biological catalysts

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2
Q

functions of enzymes

A

-highly specialized proteins
-can accelerate chemical reactions

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3
Q

active site

A

one region on the enzyme directly responsible for interactions with the reacting molecules

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4
Q

enzyme classification:

oxidation-reduction reactions

A

oxidoreductases

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5
Q

enzyme classification:

transfer of functional groups

A

transferases

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6
Q

enzyme classification:

hydrolysis reactions

A

hydrolases

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7
Q

enzyme classification:

group elimination to form double bonds

A

lyases

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8
Q

enzyme classification:

isomerization

A

isomerases

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9
Q

enzyme classification:

bond formation coupled with ATP hydrolysis

A

ligases

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10
Q

ligand

A

molecules that reversibly binds to a macromolecules

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11
Q

what are the two things interaction specificity between ligand and enzyme are based on?

A

shape (geometric), charge (electronegativity)

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12
Q

the _ _____ of amino acids contribute to the shape and charge of both the ligand and the enzyme active sites

A

R groups

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13
Q

where does enzyme catalysis occur?

A

binding or active site

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14
Q

an enzyme and substrate can be modeled as a …

A

lock and key

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15
Q

what are the 2 models of ligand binding?

A

lock and key, induced fit model

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16
Q

which model is this?

the shape of a ligand or substrate must match exactly to the shape of the active site of an enzyme

A

lock and key model

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17
Q

which model is this?

a loosely bound ligand can interact with functional groups on the protein and cause the protein to alter its conformation so as to better fit and bind the ligand more tightly

A

induced fit model

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17
Q

how do enzymes accelerate reactions?

A

by stabilizing the transition state and reducing the free energy of the transition state

17
Q

in the induced model, the enzyme can be seen as …

A

clay because of how it will mold to the substrate’s form

18
Q

what type of catalysis is a proton donor?

A

acid catalysis

19
Q

what type of catalysis is a proton acceptor?

A

base catalysis

20
Q

covalent catalysis

A

a transient covalent bond forms between the enzyme and the substrate during formation of the transition state

21
Q

simply binding substrates facilitates reactions in 2 ways:

A
  1. bring substrates into contact with each other and catalytic groups
    2.enzymes bind substrates with a specific orientation that aligns the substrate and catalytic groups
22
Q

what kind of catalysis involves metals tightly bound to the enzyme?

A

metal ion catalysis

23
Q

what are common metal cofactors?

A

Fe2+, Fe3+, Cu2+, Mn2+, Co2+

24
Q

what kind of reversible changes do metal ions do to mediate oxidation-reduction reactions?

A

-the metal’s oxidation state
-orient the substrate for reaction
-stabilize or shield negative charges

25
Q

digestive enzymes that cleave peptide bonds have _____ catalytic mechanisms but _____ in substrate specificity

A

similar; differ

26
Q

what type of curve results from when an enzyme becomes saturated as [S] increases

A

hyperbolic

27
Q

Km measures…

A

substrate concentration

28
Q

what is Km inversely related to?

A

the affinity of an enzyme for its substrate

the higher the affinity the lower the Km

29
Q

what is the Michaelis-Menten equation?

A

V0= Vmax[S]
————
Km+[S]

30
Q

What is the catalytic constant or Turnover number?

A

Kcat

31
Q

what does Kcat describe?

A

-describes how quickly an enzyme can act
-how fast the ES complex proceeds to E + P

32
Q

what does Kcat/Km represent?

A

catalytic efficiency

33
Q

what does the catalyic efficiency describe?

A

-how avidly the enzyme binds its substrate
-how rapidly it converts it to product

34
Q

what are two types of enzyme inhibition?

A

irreversible and reversible

35
Q

what kind of inhibition results from binding to the enzyme so tightly that activity is blocked?

A

irreversible inhibition

36
Q

what are the 3 types of reversible inhibition?

A

competitive, uncompetitive, mixed

37
Q

small molecules that bind an enzyme at sits different than the substrate binding site and effects, positively or negatively, the activity of that enzyme

A

allosteric effectors

38
Q

what are the two types of allosteric effectors?

A

allosteric activators
allosteric inhibitors

39
Q

1 molecule acts as both the ligand and the allosteric modulator

A

homotropic enzyme

40
Q

modulators are different than ligands with different binding sites

A

heterotrophic enzyme

41
Q

what preferentially binds to a high affinity R state

A

ATP

42
Q

what preferentially binds to a low affinity T state

A

CTP