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

23
Q

what kind of enzymes are serine proteases

A

hydrolases

24
Q

how many domains in serine proteases

25
what kind of domains in serine proteases
beta barrels
26
are serine proteases extracellular or intracellular
disulphide bridges extracellular
27
how are serine proteases synthesizes
zymogens
28
how are serine proteases activated
cleavage of peptide chain
29
what composes the catalytic triad
His 57 (acid/base) Ser 195 (nucleotide) Asp 102 (modulation of His 57)
30
what forms the oxyanion hole
Gly 193 and Ser 195
31
which amino acids contribute to zymogen activation
Asp 194 and Ile 16
32
where does chymotrypsin cleave peptides
after large hydrophobic
33
where does trypsin cleave peptides
after large positively charged residues
34
where does elastase cleave peptides
SMALL nonpolsr
35
what is the function of the oxyanion hole
TS stabilization
36
what area from the AA form the oxyanion hole
backbone NH