chapter 7

Question 1

kinetics

Answer 1

study of reaction rates

Question 2

velocity

Answer 2

rate of substrate A becoming product

Question 3

Decrease of substreate over increase in time

Answer 3

-D(A)/Dt

Question 4

increase in product over increase in time

Answer 4

D(P)/DT

Question 5

One substrate results in A=P

Answer 5

V=k(A)
first ordered reactions

Question 6

Two substrates result in A+B=P

Answer 6

V = K(A)(B)
Second ordered reactions

Question 7

What is michealis-menten equation and explain it

Answer 7

E+s=ES=E+P

E+s and E are reversible

Substrate in excess enzyme complexess with substrate, product formed

E+P is not reversibile

Question 8

michelis constant

Answer 8

indicates the enzyme-substrate affinity

Question 9

Vmax

Answer 9

describes the substrate concentration when enzyme is saturated

Question 10

does substrate concentration affect reaction

Answer 10

nop ammount of enzymes do and as more substrates come the velocity platues

Question 11

what does higher Km result in

Answer 11

a lower affinity

Question 12

isoenzymes

Answer 12

different enzymes that can catalyze the same reaction

• it can be different kinteics (reaction rate)
• it can have different regulations
• it can be expressed in diferent tissues

Question 13

sequential

Answer 13

2 substrates and 1 enzyme

Question 14

double-displacement

Answer 14

an enzyme substitution in the middle

Question 15

Alosteric enzymes

Answer 15

regulated enzymes taht allow for metabolism and metobolite flush and complex metabolic pathways

Question 16

metabloism and enzymes

Answer 16

it is a sereis of metabolic reations, only some enzymes are controled

Question 17

feedback inhibition

Answer 17

Once sufficient F has been reached the inhibotors are signaled to bind to the allosteric enzyme in E1

can inhibit one pathway and stimulate another and immedietly stops one pathway

Question 18

V0/(s) is what sigmoidal or hyperbolic with alosteric enzymes and why

Answer 18

it is sigmoidal, which tells that it doesnt shoot up in reletive velocity in low S (substrate concetration).

Alosteric enzymes are quaternary structures, meaning they have reglotory binding sites meaning some are blocked.

Question 19

what are the models of function and what do they do (summary)

Answer 19

concerted model- everything happens at once

seqeuntial model - everything is done step by step

Question 20

Concerted model and what are the steps

Answer 20

1. enzynme exists to two quaternary structers where they go into t-state(tense or R-state (relaxed)
2. R-state has more enzymitic activity than T-state
3. T-state goes into R-state once enzyme is binded
4. All activities must be completed at the same state

Question 21

sequential model

Answer 21

1. Rstate more enzamatically active than the T state
2. T-state more stable but goes into R state when binding
3. T and R-state are hybrid
4. binding at one site changes all the other sites aswell

Question 22

what stabilizes T and R states

Answer 22

Inhibitor stabilizes t-state - deoxiginated

Activitors stabilize the R-state- oxyginators