Lecture 9- Substrate binding Flashcards

1
Q

Nucleophilic substitution

A

Swap functional groups

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2
Q

Nucleophilic addition

A

Add functional groups

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3
Q

Carbonyl condensation

A

Change # of carbons

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4
Q

Elimination

A

Change (increase) bond order

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5
Q

Oxidation-reduction

A

Move electrons

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6
Q

Oxidoreductases

A

Oxidation-reduction;

-Move electrons

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7
Q

Transferases

A

Move functional group (group transfer); PHOSPHATE and METHYL GROUP

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8
Q

Hydrolases

A

Hydrolysis reactions (transfer of functional groups to water)

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9
Q

Lysases

A

Addition or removal of groups to form double bonds

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10
Q

Isomerases

A

Isomerization (intramolecular group transfer)

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11
Q

Ligases

A

Ligation of two substrates at the expense of ATP hydrolysis

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12
Q

Oxidoreductases activated carriers/coenzymes

A

NADH, NADPH, FADH2, FMNH2

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13
Q

NADH, NADPH building blocks

A

[Oxidoreductases]
Building blocks: Vitamin B3** and Adenine;
Carrying a single electron (follow the H)

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14
Q

In CATABOLIC reactions, dehydrogenases do what to their substrate and use what

A

Oxidize, NAD+

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15
Q

In ANABOLIC reactions, dehydrogenases do what to their substrate and use what

A

Reduce, NADPH

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16
Q

Transferases activated carriers/coenzymes

A

ATP, Pyridoxal phosphate (moves phosphate/ Vitamin B6), SAM**, Tetrahydrofolate, 5’deoxyadenosylcobalamin

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17
Q

Transferases ATP and pyridoxal phosphate

A

Transfers PHOSPHATE GROUP;

Building blocks: Adenosine Triphosphate and Vitamin B6

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18
Q

Transferases SAM**, Tetrahydrofolate, 5’-deoxyadenosylcobalamin

A

Transfer of METHYL group;
Building blocks: Methionine and Adenine
[Note: SAME is the primary methyl donor in cells]

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19
Q

Adenosine Triphosphate

A

Usually the gamma-phosphate is removed, but the B+gamma phosphates can be removed as pyrophosphate

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20
Q

Vitamin B6

A

Refers to 6 molecules:

Pyridoxine, pyridoxal and pyridoxine; plus their phosphate derivatives

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21
Q

Vitamin 9

A

Glutamate derivative;
Forms of interest:
-Solid as Folic Acid
-Bioavailable after reduction as Tetrahydrofolate
-Donates a methyl from Methyltetrahydrofolate

22
Q

Vitamin B12

A

Can take many forms:
-Sold as Cyanocobalamin
-Metabolically active as 5’Deoxyadenosylcobalamin or Methylcobalamin
==> Unusual bc contains a metal (COBALT)

23
Q

FADH2, FMNH2 building blocks

A

Vitamin B2 (and Adenine)

24
Q

Hydrolases

A

BREAK a chemical bond by ADDING WATER across it (via hydrolysis)

25
Q

Isomerases

A

REARRANGE order of atoms in a molecule (isomerization)

26
Q

Lyases

A

BREAK chemical bond WITHOUT WATER

27
Q

Ligases

A

Paste two pieces together (MAKE chem bond), uses ATP

28
Q

Activators/coenzymes

A

TPP, CoASH, lipoamide, biotin

29
Q

TPP building blocks

A
Vitamin B1 (+2 phosphates);
Also uses redox chemistry (can help oxidize substrates)
30
Q

CoASH (COenzyme A) building blocks

A

Vitamin B5 and Adenine

31
Q

Lipoamide building blocks

A

Fatty acid derivative and Lysine

32
Q

Biotin

A

(=Vitamin B7); +/- CO2 GROUP

Biotin + Lysine–> Biocytin the version found in enzymes

33
Q

Ag-Ab binding site

34
Q

Receptor-ligand binding site

A

Target=ligand

35
Q

Enzyme-Substrate binding site

A

Target=substrate

36
Q

Apoenzymes

A

Incomplete, inactive, and lack cofactor/enzyme

- Coenzymes (Biotin, CoA, pyridoxal phosphate)

37
Q

Holoenzymes

A

Whole, active contain cofactor/enzyme

-Metals (Zn, Mg, K, Mn)

38
Q

KA

A

=1/KD

  • Affinity or association constant
  • Coming together
39
Q

KD

A

=1/KA

  • Dissociation constant
  • Breaking apart
  • Dissociation constant for ESn complex
  • Equal to the concentration of ligand where 1/2 the available binding sites are full
  • When the receptor is half-saturated**
40
Q

Measuring KD

A

Y= [S]/ KD + [S] <

41
Q

Possible values for Y (fractional saturation)

42
Q

Y=0

A

No ligand bound

43
Q

Y=1

A

Receptor is saturated

44
Q

Y=0.5

A

Receptor is half-saturated;

Note: definition of [S]=KD

45
Q

Y v [S] graph for

A

Hyperbolic curve

46
Q

Linear Plot (Scatchard Plot)

A

Slope: -1/KD
Y-intercept: -1/KD
X-intercept: [E]T

47
Q

Cooperativity

A

Binding of each subsequent (sites are no longer independent) ligand influences the affinity (strength of interaction) of the next ligand (each ligand influences the next) to bind an active site

48
Q

The “perfectly cooperative binder” (n>1)

A

“Angle sign”= Sn/KD +Sn

n= number of binding sites (aka nH or alphaH)

49
Q

Cooperative binder of n>1 graph

A

Slope is positive= (nH)

Y-intercept: log (1/KD)

50
Q

nH=1

A

No cooperatively (Sites are independent)

51
Q

nH>1

A

Positive cooperativity (Affinity increases)

52
Q

0 < nH <1 (decimal)

A

Negative cooperativity (Affinity decreases)