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Biochemistry > Enzymes > Flashcards

Enzymes Flashcards

1
Q

define the rxn: nucleophilic substitution

A

swapping of functional groups

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2
Q

define the rxn: nucleophilic addition

A

addition of functional groups

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3
Q

define the rxn: carbonyl condensation

A

change # of carbons

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4
Q

define the rxn: elimination

A

change (increase) bond order

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5
Q

define the rxn: oxidation-reduction

A

move electrons

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6
Q

how do we know oxidation/reduction occurred in a redox rxn?

A

follow the e-s as it carries the H. OIL RIG

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7
Q

oxidoreductases are what type of rxn?

A

oxidation-reduction

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8
Q

transferases are what type of rxns?

A

group transfer

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9
Q

hydrolases are what type of rxns?

A

hydrolysis rxns ie break a chem bond by adding h20

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10
Q

lyases are what type of rxns?

A

Break a chem bond w/oo using h20

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11
Q

isomerases are what type of rxns?

A

isomerization ie rearrange order of atoms in a molecule

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12
Q

ligases are what types of rxns?

A

Use ATP to piece 2 pieces together ie make a chem bond

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13
Q

what are the coenzymes fo oxidoreductases?

A

NADH, NADPH, FADH2, FMNH2

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14
Q

what is the vitamin precursor for NADH and NADPH

A

B3 niacin (nicotinate)

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15
Q

what group does the coenzymes for oxidoreductases carry?

A

electrons

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16
Q

what is the vitamin precursor for FADH2 and FMNH2?

A

b2 (riboflavin)

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17
Q

ribitol is a reduced form of _

A

ribose

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18
Q

what is the enzyme for the coenzyme NAD?

A

lactate dehydrogenase

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19
Q

what is the enzyme for the coenzyme flavin adenine nucleotide?

A

monoamine oxidase

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20
Q

what are the coenzymes for trasnferase: transfer of a phosphate group?

A

ATP, pyridoxal phosphate

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21
Q

the carrier molecule ATP (in its active form) carries what group?

A

phosphoryl

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22
Q

what are the coenzymes for trasnferase: transfer of a methyl group?

A

SAM, tetrahydrofolate, and 5’deoxyadenosylcobalamin

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23
Q

for the conezyme pyridoxal phoshate, what is the enzyme?

A

glycogen phasphorylase

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24
Q

what is the vitamin precursor for tetrahydrofolate

A

Folate B9

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25
Q

the group carried by tetrahydrofolate?

A

one-carbon units

26
Q

SAM is the primary _ donor in cells

A

methyl

27
Q

what is the enzyme for coenzyme tetrahydrofolate?

A

thymidylate synthase

28
Q

what is the enzyme for coenzyme 5’-deoxyadenosylcobalamin

A

methylmalonyl mutase

29
Q

hydrolases _ a chemical bond by _ h20 across it

A

break by adding h20

30
Q

isomerases _ order of atoms in a molecule

A

rearrange

31
Q

lyases _ a chem bond _ h20

A

break without h20

32
Q

ligases use _ to _ a chem bond

A

use ATP to make a chem bond

33
Q

what are the coenzymes with +/- aldehyde group?

A

TPP

34
Q

what is the vit precursor for TPP?

A

B1

35
Q

what is the enzyme for coenzyme TPP?

A

pyruvate dehydrogenase

36
Q

what are the conenzymes for +/- an acyl group?

A

CoAsh and lipoamide

37
Q

what is the vit precursor for CoAsh

A

B5 (pantothenate)

38
Q

what are the building blocks for lipoamide

A

a fatty acid derivative and lysine

39
Q

what is the enzyme for coenzyme A

A

acetyl CoA carboxylase

40
Q

for +/- CO2, what is the coenzyme?

A

biotin

41
Q

what is the vit precursor for biotin?

A

B7 biotin

42
Q

what is the conenzyme for coenzyme biotin

A

pyruvate carboxylase

43
Q

the active site is only a few residues out of the protein, t/f?

A

true

44
Q

the active site is 3D pocket creating a unique _

A

microenvironment

45
Q

the active site determines substrate specificity by __

A

size and charge complimentary

46
Q

the active site contacts with the substrate through __ interactions

A

non-covalent ie temporary

47
Q

a receptor just binding a __

A

just binding a protein (ligand)

48
Q

an enzyme-substrate not only binds to target substrate but also

A

does something with what we bind

49
Q

allosteric binding occurs where

A

does not occur at the active site

50
Q

allosteric binding involves a 2nd substrate which can be a _ or a _

A

activator of inhibitor

51
Q

how does an allosteric inhibitor fcn

A

inhibitor binds to allosteric site and changes protein active binding site so substrate no longer binds; build up of unbound substrate

52
Q

how does an competitive inhibitor fcn

A

inhibitor looks close enough to actual substrate and able to fit in the active binding site for it

53
Q

how does an allosteric activator fcn

A

conformational change of enzyme causes rxn to be halted bc of its incorrect shape. activator binds and changes to correct shape so substrate can bind and rxn can continue

54
Q

holoenzymes are whole and active and contain _

A

cofactor/coenzyme that are allosteric activators

55
Q

apoenzymes are incomplete and inactive and lack __

A

cofactor/conenzyme

56
Q

when Y =0

A

no ligand bound

57
Q

when Y =1

A

receptor is saturated

58
Q

when Y = 0.5

A

receptor is half saturated ; kD =[S]

59
Q

what is cooperativity

A

binding of each subsequent ligand influences the affinity of the next ligand to bind

60
Q

nH=1

A

no cooperativity (sites are independent)

61
Q

nH is greater than 1

A

positive cooperativity (affinity increases)

62
Q

nH is greater than 0 but less than 1

A

negative cooperativity (affinity decreases) ie next ligan is even more difficult to bind

Biochemistry (32 decks)

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