Videos- Biochem

Question 1

induced fit model

Answer 1

substrate changes enzyme

Question 2

Lock and key model

Answer 2

perfect fit; no conformational change

Question 3

when something binds to the allosteric site…

Answer 3

It causes a conformationalshift int eh enzyme–changes the functionality

Question 4

Cofactors

Answer 4

Inorganic

i.e. zinc, copper, iron

Question 5

Coenzymes

Answer 5

Organic

Vitamins

Question 6

Fat soluble vitamines

Answer 6

DAKE

Question 7

Something that has it’s cofactor/coenzyme

Answer 7

holoenzyme

Question 8

Something that lacks its cofactor/coenzyme

Answer 8

apoenzyme

Question 9

Prosthetic group

Answer 9

enzymes that bind very tightly (often permanently) (i.e. hemoglobin)

Question 10

How are phosphatases and kinases related?

Answer 10

phosphatases removes phosphate groups while kinases add them

Question 11

Ligase

& examples

Answer 11

joins compounds together; usually requires ATP

Synthetase, ligase

Question 12

Isomerase

& examples

Answer 12

Rearranges compounds; new isomer

isomerases, mutases

Question 13

Lyase

& examples

Answer 13

Breaks thigns apart w/o water

phosphorylase

-lyase; -ase

Question 14

Hydrolase

& examples

Answer 14

breaks compounds apart by adding water

Pepsinogen, peptidase, nuclease, lipase, amylase

Question 15

Oxidoreductase

& examples

Answer 15

Transfer electrons like in the Krebs cycle with dehydrogenase; redcutase, oxidase

Question 16

Transferase

& examples

Answer 16

transfers functional groups

transferase, kinase

Question 17

Example of a process that uses a lyase

Answer 17

Glycogenolysis uses phosphorylase

Question 18

Does a calayst alter thermodynamics?

Answer 18

no

Question 19

Hill coefficient

Answer 19

if > 1 = cooperative binding

Question 20

Km

Answer 20

the concentration at which you get half of the max rate

Question 21

inhibitor line is above regular line AND 1/[S] spot is different

Answer 21

Competitive inhibition

Question 22

Competitive inhibition

• active site
• binding
• overcome?
• relationship between Km and Vmax
• shift

Answer 22

Competes for the active site

Inhibitor binds and STOPS the substrate from binding

overcome by increasing substrate concentration

Increases Km; Vmax stays the same

shift to the RIGHT

Question 23

inhibitor line is above regualr line, same 1/[S]

Answer 23

non-competitive inhibition

Question 24

Non-competitive inhibition

• active site
• binding
• overcome?
• relationship between Km and Vmax

Answer 24

binds to the active site

conformational shift other than active site

No change in Km, Vmax decrease

increase substrate concentration will not overcome

Question 25

Inhibitor line is below regular line; 1/[s] is different

Answer 25

mixed inhibition

Question 26

Mixed inhibition bind vmax and Km relationships

Answer 26

binds to allsoteric site cuasing shape change Decreaes vmax if prefer enzyme = KM increase Prefer complex = KM decrease

Question 27

Lower Km = \_\_\_\_affinity

Answer 27

increase affinity

Question 28

inhibitor line and regular line are parallel

Answer 28

Uncompetitive inhibition

Question 29

Uncompetitive inhibition - binding - KM and Vmax relationship

Answer 29

Binds to the allosteric site of enzyme/substrate complex, preventing the release of substrate Decreases KM and Vmax "the amount or the ratio fo change between KM and Vmax is the same"