Final Exam Part 3

Front 1

NAD+ will be ___ to NADH and a substrate will be ____

Back 1

reduced to NADH, oxidized

Front 2

NADH and NAD derived from

Back 2

ADP

Front 3

coenzyme A is a large carrier of what group?

Back 3

acetyl

Front 4

What potential does acetyl CoA have? high or low?

Back 4

high potential for acetyl group transfer

Front 5

NADH and FADH react___ with ___ in the ___ of a catalyst

Back 5

slowly with O2 in the absence of a catalyst

Front 6

In the absence of a catalyst, __ and __ are hydrolyzed slowly

Back 6

ATP and acetyl CoA

Front 7

Glycolysis involves the breakdown of

Back 7

?glcose into pyruvate

Front 8

Does glycolysis yield ATP?

Back 8

yes, only 2 molecule

Front 9

Where does glucose come from? (2)

Back 9

precursors like pyruvate, enymatic breakdown of glucose polymers like starch and glycogen

Front 10

ATP goes in before the creation of what two steps?

Back 10

Glucose 6 phosphate, fructose 1,6 biphosphate

Front 11

Irreversible rxn

Back 11

PFKase conversion F6P to F1 6BP

Front 12

How many opportunities for irreversible reaction are there?

Back 12

3

Front 13

Three control strategies: list in order of shortest to fastest

Back 13

allosteric, phosphorylation, trxn control

Front 14

All reactions of glycolysis occur in the

Back 14

cytosol

Front 15

Difference between glucose 6 phosphate and fructose 6 phosphate

Back 15

6 ring to 5 ring

Front 16

Reactant and product of fructose 6 phosphate conversion to fructose 1, 6 biphosphate

Back 16

ATP in, ADP out

Front 17

What is this? What comes immediatly prior? After? are there reactants, products?

Back 17

glucose 6 phosphate, ATP is a reactant to catalyze this from glucose

ADP let off in its formation

After it is turned into fructose 6 phosphate

Front 18

What is this? What comes immediatly prior? After? are there reactants, products?

Back 18

Fructose 6 phosphate

No use of ATP

Before is glucose 6 phosphate

After comes fructose 1,6 biphosphate

Front 19

What is this? What comes immediatly prior? After? are there reactants, products?

Back 19

Fructose 1,6 biphosphate. ATP and PKase catalyzes reaction and lets off ADP. Next comes two phosphate groups formed through aldolase

Front 20

Steps that create ATP are called

Back 20

phosphoryl transfer steps

Front 21

Aldol cleavage of fructose 1, 6 biphosphate in 2 phosphate molecules has what delta G?

Back 21

negative delta G, postiive delta G'

Front 22

3C intermediate G6P will be cleaved into

Back 22

glyceraldehyde 3 phosphate

Front 23

How is ATP generated in the later steps?

Back 23

compound with higher phosphoryl transfer potential synthesized

Front 24

Purpose of hexose isomerization. What step do you see it in?

Back 24

Create an intermediate that will cleave two symmetrical 2, 3C intermediates. Glucose 6 phosphate---fructose 6 phosphate

Front 25

Delta G or Delta G' == which is the actual real life measure?

Back 25

delta G

Front 26

why are some delta g values positive?

Back 26

concentration of metabolites in vivo in glycolysis unknown

Front 27

PFKase: substrates bind where? regulators bind where?

Back 27

substrates bind in the catalytic sites, regulators bind in the allosteric sites

Front 28

PFKase and ATP relation: allosteric

Back 28

ATP inhibits PFKase allosterically. This causes the enzyme to have a lower affinity for its substrate F6P

Front 29

Reverses inhibitory action of ATP on PFKase

Back 29

AMP

Front 30

ATP:AMP increases causes ___PFKase activity

Back 30

decreased

Front 31

Low ATP effect on PFKase

Back 31

its a subtrate, so it will increase reaction velocity

Front 32

PFKase reaction velocity highest at ___ ATP. Why?

Back 32

moderate ATP. ATP acts as an allosteric inhibitor and a substrate

Front 33

Y axis of PFKase curve

Back 33

Relative rate of fructose 1,6 biphosphate synthesis

Front 34

Positive regulator of PFFase

Back 34

2, 6 BP

Front 35

Delta G vs delta G prime: which tend to be higher?

Back 35

delta G prime (except for 1 phsphoryl transfer step) in the production of ATP

Front 36

Ligation requiring ATP cleavage description

Back 36

formation of covalent bond

Front 37

Isomerization definition

Back 37

formation of isomers

Front 38

Group transfer defininton

Back 38

transfer of functional groups

Front 39

Three ways to control metabolic processes

Back 39

control amount of enzyme, control catalytic activity, control access to substrate