Brainscape's Knowledge GenomeTM

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


See full index

BMS I > Protein/Enzyme Function > Flashcards

Protein/Enzyme Function Flashcards

1
Q

Oxireductases

Transferases

Hydrolases

Lyases

Isomerases

Ligases

A

Catalyze redox rxns

Catalyze trasfer of C, N, P containing groups

Cleave of bonds by addition of H20

Cleave CC, CS, CN

Catelyze racemization of optical geo isomers

Catalyze formation of bonds between C and O, S, N coupled to hydrolysis of high energy phosphates

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

Synthase vs syntheses

phosphatase vs phosphorylase

oxidase vs oxygenase

A

req atp vs no req atp

uses water to remove P, uses P to break bond and make phosphorylated product

O2 acceptor but no oxygen in product, one or both Oxygen atoms incorporated

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

Vmax

A

Velocity when all enzyme is saturated

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

Hyperbolic vs sigmoidal curve

A

Allosteric
-due to cooperative subject binding

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

Michaelis Menten Eq 92)

rate of reaction and [E], [S]

[S]>Km

A

v=Vmax[S]/Km+[S]

v=kcat[E][S]/Km+[S]

directly proportional

v=[S]

v=Vmax

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

Km

A

Michaels constant

depends on enzyme and sub
-refelcts affinity

Km=Vmax/2

no vary with [E]

Low Km-high affinity-low concentration needed to half saturate enzyme

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

Lineweaver burk axis

intercepts

A

1/Vo x 1/[S]

x intercept=-1/km
y intercept=1/Vmax

DRAW

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

Competitive inhib

Vmax

Km

Lineweaver Burk

A

bind reverisble to same site as substrate

Reverse effect by increasing [S]
high[S]=Vmax as in absence of inhib

increases apparerent Km
More substrate needed to hit 1/2Vmax

vmax unchaged
Km increased in presence of inhib, -1/Km moves closer to 0

DRAW

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

Noncompetitive Inhib

Vmax

Km

Lineweaver burk

A

binds to either ES complex or enzyme

Decrease Vmax-cannot overcome noncomp inhab by increasing substrate

Same Km-does not interfere with binding affinity

Vmax is notably decreased and Km is unchanged

draw this bitch

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

Holoenzymes

A

active enzyme with non protein component

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

apoenzyme

A

inactive enzyme

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

cofactor

A

metal factor for enzyme

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

coenzyme

A

small organic molecule

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

prosthetic group vs cosubstrate

A

bind to enzyme to make work

transiently bind to enzyme to make work

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

isoenzymes

A

same chemical run but different primary structure/aa seq

different in different tissues

Different temp/ph/kcat/Km properties

Can use to diagnose

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

Keq

A

[P]/[S]

amt of substrate and product present @ eq

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

REDOX enzymes

A

typically regenerated by other enzymes (NADH, FADH)

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

Enzyme rate limiting step and how to slow even more

A

ejection of product

slowed by tighter binding

19
Q

Why doesn’t lock and key work

A

reaction site can be same-but territory strutreu must allow/help

20
Q

Induced fit

A

Enzyme creates CONFORMATIONAL change in enzyme

flexible active site

21
Q

Reaction rate and AE relationship

A

inverse

22
Q

Transition state stab

A

ENZYME BINDS BETTER TO TS then substrate-but still well to substrate

23
Q

Enzymes change

A

Velocty

NOT-Keq or free energy,

24
Q

Cat starts (5)

A

proximity, tss, covalent cat/nuc cat, acid base cat, metal ion cat

25
Q

Chymotripsin

3 types of cat+where

cat triad

cleaving?

activation cleaving

A

Has nuc/covalent cat

  • serine O- bonds with amide covalently
  • serine is potent nucleophile when deprotonated

general acid/base cat

  • HIs accepts proton from Ser
  • his becomes potent Nucleophile
  • forms key intermediate tetrahedral
  • HisH then donates H to help acyl enzyme formation
  • creates acyl enzyme (slow step)

TSS by oxyanion hole

  • READY FOR - GROUP
  • Made of Ser and Gly
  • stabilize tetrahedral

serine, histidine, aspartate

cleave after aromatic AA’s

peptide bond

26
Q

how to make endergonic rxn go

A

Couple with exergonic

27
Q

Energy in ATP/ADP

Cov bond vs noncov

A

3.5 and 2.5 kj/mol

50 to .5

28
Q

Does delta G say anything about rate?

A

NO

can have long pathway-end is exergonic so -G is low, but long

29
Q

Velocity

A

change in concentration of S or P over time (slope of conc vs time graph)

30
Q

Kcat=

relation to enzyme, substrate, Km, pH and temp

A

Vmax/[E]

rate at which substrate on enzyme becomes free product
-turnover time for conversion

changes for pH and temp

similar to Km

constant for enzyme and substrate

31
Q

slide 69 and 3 amino acid at ph problems

A

do these

32
Q

phosphorylation of enzymes

A

mostly on Ser, some on Thr, and 1% of tyr-these have neg charges

can activate or deactiate enzyme

33
Q

Proteolysis

A

irreversible means of activating enzymes

ex. hydrolyze peptide to activate chymotrypsin

34
Q

Inhibition pathways (4)

A

irreversible (covlanent bond), reversible, comp (looks similar)/noncomp

35
Q

Transition state analogs

A

amazing inhibits

stable molecules that resemble geo/electro features of highly unstable TS

binds tighter to enzyme TS

36
Q

allosteric enzymes

oligomeric

active and all site binds what?

A

have actie and allosteric site

all oligomeric

active site binds s
allo site binds effector/regulator

molecules do not resemble substrates

37
Q

K.05 meaning

A

when half substrate velocty????

38
Q

R and T

how modulate eq

A

R=relaxed-active
-binds S better and higher cat activity

T=taught-inactive
-binds S weakly and lower cat activity

effectors/regulators

39
Q

Allo activator binding vs allo inhibitor binding

A

act-stabilizes R-increases S binding and increased activity

Inact-stabilizes T-decrease S bindng and decreased activity

40
Q

K type inhib

A 
increase k.05
not affect Vmax
decrease apparent affinity for S
low[S]-enzyme activity lower than normal
high[S]=enzyme activity is normal

makes substrate binding weaker

41
Q

v-type inhib

A

􏰢V-type inhibitor will decrease Vmax 􏰢V-type inhibitor will not affect K0.5
􏰢Will not affect the affinity of S for the E 􏰢At all [S], activity of E is lower

42
Q

k-type activator

A

􏰢K-type activator will decreases K0.5 􏰢K-type activator will not affect Vmax
􏰢Will increase the affinity of the S for the E 􏰢At low [S], activity of E is higher
􏰢At higher [S], activity of E is normal.

43
Q

v-type activator

A

􏰢V-type activator will increase Vmax 􏰢V-type activator will not affect K0.5
􏰢Will not affect the affinity of the S for the E 􏰢At all [S], activity of E is higher

BMS I (30 decks)

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