5 Flashcards

1
Q

what are bound molecules called

A

ligands

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2
Q

is ligand binding covalent

A

nah

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3
Q

where does ligang binding occur and what interactions help it

A

H-bonds, ionic interactions, hydrophobic ,van der waals

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4
Q

is ligand binding cooperative or non-cooperative

A

both

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5
Q

what are cofactors

A

additional chemical components that assist in enzyme function

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6
Q

what are the two types of cofactors

A

metal ions and coenzymes

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7
Q

what is a prosthetic group

A

metal ions or coenzymes associated with a protein

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8
Q

name all the enzyme types and classifications

A
  1. oxidoreductase
  2. transferase
  3. hydrolase
  4. lyases
  5. isomerase
  6. ligase
  7. translocase
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9
Q

what category do kinases fall into?

A

trasnferases

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10
Q

what are lyases also called

A

synthases

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11
Q

what category do dehydratases and decarboxylases fall into

A

lyases

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12
Q

what are ligases also called

A

synthetases

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13
Q

EC 3.4.21.4 describe what each number means

A

class substrate mechanism specificity

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14
Q

what are the 4 ways in which enzymes increase the reaction rate

A

participate in the reaction
desolvation
proximity and orientation
stabilizing transition state

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15
Q

what are the 3 ways in which enzymes can participate in a reaction

A

acid/base catalysis
nucleophilic catalysis
metal ion catalysis

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16
Q

how does RNase act as an acid/base catalyst

A

His 12 = base
His 119 = acid

17
Q

what does pH sensitivity relate to in catalysis

A

acid/base reactions
nucleophilic reactions
denaturation

18
Q

how can metal ions participate in a reaction

A

binding/orientation
stabilize TS
reduction / oxidation centres

19
Q

what is carbonic anhydrase

A

metalloenzyme

20
Q

how does PEP carboxykinase work

A

assisted by metal ion cofactors
active site brings groups together
phosphoryaltes pyruvate

21
Q

what enhances the difference between activation energies

A

transition state not substrate

22
Q

what is the nucleophilic AA in hexokinase

A

Asp

23
Q

what kind of enzymes are serine proteases

A

hydrolases

24
Q

how many domains in serine proteases

A

2

25
Q

what kind of domains in serine proteases

A

beta barrels

26
Q

are serine proteases extracellular or intracellular

A

disulphide bridges extracellular

27
Q

how are serine proteases synthesizes

A

zymogens

28
Q

how are serine proteases activated

A

cleavage of peptide chain

29
Q

what composes the catalytic triad

A

His 57 (acid/base)
Ser 195 (nucleotide)
Asp 102 (modulation of His 57)

30
Q

what forms the oxyanion hole

A

Gly 193 and Ser 195

31
Q

which amino acids contribute to zymogen activation

A

Asp 194 and Ile 16

32
Q

where does chymotrypsin cleave peptides

A

after large hydrophobic

33
Q

where does trypsin cleave peptides

A

after large positively charged residues

34
Q

where does elastase cleave peptides

A

SMALL nonpolsr

35
Q

what is the function of the oxyanion hole

A

TS stabilization

36
Q

what area from the AA form the oxyanion hole

A

backbone NH