Final PP 3

Question 1

what happens to the rate of glycolysis during hypoxia?

Answer 1

increases

Question 2

what enzyme produces GTP in the TCA?

describe the reaction

Answer 2

succinyl co A synthase

succinyl -> succinate

Question 3

describe the reaction catalyzed by PDH?

Answer 3

pyruvate+SH-coA+NAD -> Acetyl coA+NADH+H

Question 4

name an inhibitor of mitochondrial ATP synthase

Answer 4

Oligomycin

Question 5

what is the bond btw the sucrose units?

Answer 5

C1 in glucose -> C2 infructose

glycosidic bond

Question 6

what is the bond btw the lactose units?

Answer 6

galactose 1 - 4 glucose

Question 7

what is the position of the OH group on primary bile acids?

Answer 7

3
7
12
in secondary we always wont have the 7!

Question 8

describe the reaction catalyzed by Threonine Dehydratase

Answer 8

Threonine -> a-KB + NH3

Question 9

How many ATP molecules directly produced during the Krebs cycle?

Answer 9

10
NADH x 3 = 2.5x3= 7.5
FADH x 1 =. 1.5 ATP
GTP x 1 = 1 ATP

Question 10

what is the cofactor of complex 1 in oxidative phosphorylation?

Answer 10

NADH

Question 11

which enzyme in glucose metabolism is located in the ER membrane?

Answer 11

glucose-6-Pase

Question 12

what enzymes will give us NADH in the TCA?

Answer 12

1. isocitrate DH
2. aKG DH
3. malate DH

Question 13

where does LXR located?
a?
b?

Answer 13

a= liver, lungs , adipose
b= all tissues
mnemonic!!! by RK
a- LLAA - like los angeles b - Bekol makom

Question 14

which compounds are substrates for monoamine oxidase?

Glu
serotonine
dopamine
NE
Gln

Answer 14

serotonine
dopamine
NE

Question 15

arterial natriuretuc factor (ANF) activates guanylate cyclase true/flase

Answer 15

true

Question 16

what are the allosteric activators of PFK1?

Answer 16

AMP and F2,6BP

Question 17

what is the cofactor of methyl malonyl co A mutase?

Answer 17

vit B12

Question 18

what is the reaction of methyl malonyl co A mutase?

Answer 18

methyl malonyl co A -> succinyl co A

Question 19

what is the prosthetic group of pyruvate carboxylase?

what else does the reaction need?

Answer 19

Biotin

needs ATP

Question 20

write down the reaction catalyzed by Malate DH

Answer 20

malate + NAD -> OAA + NADH + H

Question 21

name an inhibitor of mitochondrial ATP synthase

Answer 21

Oligomycin

Question 22

what is the difference btw the bonds in sucrose and lactose?

Answer 22

sucrose: glucose a1-2b fructose
lactose: galactose b1-4 glucose

Question 23

describe the reaction catalyzed by Threonine dehydratase

Answer 23

Thr -> a-KB + NH3

Question 24

what are the NADPH generators? (3)

Answer 24

PPP
isocitrate DH
malic enzyme

Question 25

what are the enzymes in FA synthesis that uses NADPH?

Answer 25

3-ketoacyl reductase | enoyl reductase

Question 26

which complexes pump H to the intermembrane space?

Answer 26

I III IV

Question 27

which complex uses NADH? | wich uses FADH2?

Answer 27

NADH- I | FADH2- II

Question 28

what is the location of hormone sensitive lipase?

Answer 28

adipose tissue

Question 29

what is the prosthetic group of homocysteine methyl transferase?

Answer 29

vit B12

Question 30

which AA are modified in collagen?

Answer 30

Pro+Lys | we need vit.C for that!!

Question 31

what 3 AA are in the active site of serine protease?

Answer 31

Ser His Asp

Question 32

what protein regulates CFTR ch?

Answer 32

cAMP dependant kinase

Question 33

which biogenic amine will be produced from Try?

Answer 33

serotonin

Question 34

what are the branched AA?

Answer 34

Iso Leu Val

Question 35

what happens to Vmax and Km in the case of non-competitive inhibitor?

Answer 35

``` Vmax decrease (think about yourself running in a race with usain bolt. you are non competitive to him and your speed is lower.) Km stays the same (there is enough place for both of you in the race place) ```

Question 36

what is the primary difference btw. competitive and non-competitive inhibition?

Answer 36

competitive inhibition affects the substrate's ability to bind by binding an inhibitor in place of a substrate, which lowers the affinity of the enzyme for the substrate

Question 37

what happens to the Km in the presence of competitive inhibitor?

Answer 37

increases

Question 38

what happens to Vmax and Km when UNCOMPETITIVE inhibitor is present?

Answer 38

both decrease

Question 39

what is the function of SCARB1?

Answer 39

scavanger receptor. | involved in the uptake of cholesterol ester from HDL

Question 40

AA with amide side chain?

Answer 40

Asparagine Glutamine

Question 41

Myoglobin-O2 binding curve shape is-

Answer 41

hyperbolic

Question 42

Myoglobin releases O2 only during -

Answer 42

severe hypoxia (strenous excersize-or diving!) resting human muscle Mb is near saturated

Question 43

how many heme group does Mg have?

Answer 43

1

Question 44

which one has higher affinity to O2? Mg/Hg

Answer 44

Mg (bcs its job is to store O2!)

Question 45

what is the structure of Hg?

Answer 45

tetramer 2xa+2xb in adults 2xa+2xy in fetals

Question 46

what are the two forms of Hg?

Answer 46

Tense | Relaxed

Question 47

(not from PP) | R state binds O2 more loosly/tightly

Answer 47

tightly

Question 48

(not from PP) | The T state has more/less of an affinity for oxygen than the R state

Answer 48

less!!!!

Question 49

(not from PP) | T state binds CO2 more tightly/loosly

Answer 49

tightly

Question 50

(not from PP) | BGP binding stabilizes T/R state

Answer 50

T

Question 51

(not from PP) | At high altitudes blood BPG levels increase/decrease

Answer 51

increase

Question 52

what is the job of 2,3BPG in Hg?

Answer 52

It interacts with deoxygenated hemoglobin beta subunits and so it decreases the affinity for oxygen and allosterically promotes the release of the remaining oxygen molecules bound to the hemoglobin

Question 53

what is the definition of Denaturation

Answer 53

loss of native tertiary structure

Question 54

what is the shape og Hg-O2 binding?

Answer 54

sigmoidial