Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

Biochem > Test 3 > Flashcards

Test 3 Flashcards

1
Q

what are most enzymes

A

proteins

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

does a lower or higher activation barrier allow the system to come to equilibrium faster

A

lower

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

what are pros to enzymes

A

function at low temps
fast (order of milliseconds)
occurs in H2O
Few side products
higher yields

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

what is what slows down a reaction

A

the activation barrier

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

what causes an alternate pathway

A

enzyme

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

delta G

A

final - initial

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

what does a negative delta G mean

A

spontaneous

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

what are cofactors

A

molecules that the enzymes need help from, not an amino acid residue but involved in function of enzyme, ions

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

what is a coenzyme

A

not an ion, but some small organic molecule involved in enzyme function

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

acid

A

donates protons

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

base

A

accepts protons

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

covalent bonds in enzymes

A

temporary covalent bonds provide an alternative, lower energy reaction pathway

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

non covalent interactions in enzymes

A

form an ES complex: weak interactions between enzymes and substrate stabilize the transition state (binding energy)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

when does the ES complex form

A

when substrate binds active site

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Enzyme substrate complex equation

A

S+E –> ES –> E+P

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

is the enzyme substrate complex permanent

A

no it is is temporary held together by non covalent bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

what does lower substrate entropy mean

A

holds it steady (substrate), more ordered so they can react

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

substrate desolvation

A

removes water from around substrate which males available all functional groups of molecule

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

what does induced fit mean

A

enzyme active sites are complementary to transition states

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

what shape does the enzyme need to be

A

shape that the transition needs to be
bends when at ideal amount where it cant bend anymore

21
Q

what does the inhibotor look like

A

inhibitor looks similar to transition state but stops it from occuring

22
Q

typical enzyme enhancement

A

10^5 to 10^17 x

23
Q

what can you reduce for a reaction to happen faster

A

reduce entripy

24
Q

what is the rate of reation a function of

A

function of substrate concentration

25
Q

what does more S mean

A

more Product can be formed

26
Q

what is km

A

concentration of substrate at 1/2 max rate of concentration

27
Q

what is the best speed for an enzyme

A

10^9

28
Q

what is 10^9 known as

A

diffusion control limit, can’t go faster than that

29
Q

EI

A

enzyme inhibitor complex

30
Q

K1

A

dissociation complex

31
Q

what does the I do

A

takes up the S spot

32
Q

do good inhibitors have small or large KI

A

small

33
Q

uncompetitive inhibition

A

structural changes happens to enzymes once the enzyme binds
inhibitor can only bind to enzyme substrate complex

34
Q

apparent value

A

values mean what they appear to be when an inhibitor is present

35
Q

what chnages in mixed inhibition

A

both slope and Y intercept

36
Q

what does HIV 1 protease facilitate

A

direct attack of water on the peptide bond

37
Q

2 substrates of HIV 1 protease

A

H2O and protein

38
Q

why do we avoid chiral centers in drugs

A

too expensive

39
Q

how does hexokinase keep water out

A

without substrate present the enymes will close

40
Q

what does chymotrypsin do

A

catalyzes hydrolysis on peptide bonds using serine rsidues

41
Q

optimum pH of chymotrypsin

A

8

42
Q

Kcat

A

measure of speed, measured at turnovers per second

43
Q

how is chymotripsin activated

A

proteolytic cleavage

44
Q

chymptrypsinogen

A

inactive, when syntheizes not active yet, ready to be tunred on

45
Q

pi chymotripsin

A

partially active, 1 st cut is to remove ser14 and arg15

46
Q

what does peptidoglycan need

A

transpeptidase

47
Q

what inhibits transpeptidase

A

B lactan antibiotics

48
Q

gram negative vs gram positive bacteria

A

gram positive has a thick cell wall

Biochem (4 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions