7

Question 1

function of serine protease

Answer 1

to digest food: trypsin, chymotrtpsin
coagulate blood: thrombim and brkdown blood clot )plasmoin)
form a catalytic triiad vinvolveing HIS 57, Ser, Asp

Question 2

what happens in SERINE PROTEASE hydrolysis?

Answer 2

His accepts a proton from Ser. forms a transient cov bond to the substrate protein
cleaves its N-C bond in half

Question 3

lysozyme = part of ____ _____ system

has __ @ active site
found in tears ___ and saliva
stabilize by ___ bonds

Answer 3

innate immune
Asp
mucus
disulfide

Question 4

Enzyme lower delta G = activation E
to lower the delta G
1) Enzyme binds to __ S, reorg the __ rxn
2) rearrange the e— to encourage a favourable __/___ ___
3) strains the S, encourage a favourable ___ ___

Answer 4

2 / encourage
+/- charge
transietn state

Question 5

what is a transient state

Answer 5

transient high Energ state
an intermeidate from btw product and reactants
bonds on the verge of breaking and forming

Question 6

describes Enzymes

can be __ or __:
fidelity:

Answer 6

perform nearly all chemical transformation

ACCELERATE =/ dissapear

mostly proteins
- can be specific or not: recognize 1 or thousands molec
fidelity: almost never fail
in mild condition: 37C or neutral pH

Question 7

how does it work?

has a cleaaget: __ ___

Answer 7

E has a small active site (5%) where rxn happens
S binds to E @ active site -> ES complex -> catalysis -> form EP complex -> release -> regenerate

Has a cleft where S binds: multiple weak bonds, binding is reversible
iN ES, cleavage brks bond in half

Question 8

enzyme kinetics

Answer 8

study of rate of rxn as influenced by c of S, inhibitor and E’s affinity for S

Question 9

describe the enzyme kinetic graph

Answer 9

S starts @ high concentration
as S binds to E tp make ES complex, both >
=> ES increase until it achieves an unchanging steady state
> enzyme kinetic is determine @ that steady state

Question 10

describe v0 and S plot

Answer 10

v- is rate of txn
Km is determined at half of V max

as S <. v0 also increase until it ahieves vmax

Question 11

what is zymogen function? e.g

Answer 11

serine protease is initially created as zympgen = an inactive enzyme
in this case trypsinogen
to have a storage of zymogen activ if needed and not harm as E

Question 12

compounds tht resemble the transition state bt doesnt undergo the rxn (similar geometry, charge distri)

Answer 12

transition state analogue

are excellent competiive inhibitors bcs they ind tightly, block active sight
tamiflu is a neuraminidase inhibitor that prevent flu virus from releaseing itself from host

Question 13

cofactor need apoenzyems. T OR F

Answer 13

F. apoenzymes need cofactors. can be essential or elevate the rate of exn.

Question 14

what is the Michaelis-Menten equation

Answer 14

v (initial) = v max x [S] / Km + [S]\
starts with low c of S. as you < color gets bluuer and V <

Question 15

what is the Michaelis constant

Answer 15

Km
- reflects E’s affinity for S
- independent of E concentration

Question 16

describe double reciprocal of M-M

Answer 16

double reciprocal of M-M is Lineweaver -Burke plot
- Km reciprocal and V max reciprocal intersect at y axis ; straihgt line

Question 17

2 types of inhibiotr

Answer 17

reverssible: binding of inhibitor to E is non cov; inhibitior can be removed
irreversible: cov; blocks active site

reversible inhibitor is competiitive one