Lecture 4 - Biochemistry Rules of Engagement

Question 1

steps to create products from the enzymes

Answer 1

1: substrate enters active site on enzyme
2: creates an enzyme/substrate complex
3: becomes a enzyme/product complex
4; products leave the active site of the enzyme

Question 2

what are the 4 major things needed to help create biological reactions

Answer 2

enzymes, energy (ATP), the redox class of helpers (NADH,FADH2, and NADPH), and electric charge across membranes

Question 3

the enzyme substrate E-S complex

Answer 3

when a substrate enters the enzyme active site

Question 4

what reaction would be used to find the substrate concentrations of an enzyme

Answer 4

velocity reaction

Question 5

how would you quantify a substrate in a velocity reaction

Answer 5

use an electric scale to weigh out starch and put in in known solution volumes to know starting concentration

Question 6

how would you quantify a product in a velocity reaction

Answer 6

use a metabolite specific test to measure color and intensity with a spectrophotometer

Question 7

how is the standard curve plotted in a velocity reaction

Answer 7

make up a range of sucrose concentrations from sugar and make up a range of standards

Question 8

what is vmax/reaction velocity

Answer 8

looking at how much product an enzyme can make in a given time frame

Question 9

how could an enzyme be inhibited

Answer 9

could be driven by having more substrate, product could reduce enzyme activity (like a backlog), toxins/metabolites could temporarily or permanently block enzyme sites

Question 10

what is the easiest enzyme reaction curve

Answer 10

the Michaelis Menton Curve

Question 11

what does the km of the Mechaelis Menten curve mean

Answer 11

is 1/2 of vmax, where vmax is the maximum velocity

Question 12

at what conditions do enzyme operate (in regards to vmax, oxygen and pH)

Answer 12

enzymes operate below their vmax, at specific pH conditions, and under certain aerobic/anaerobic conditions

Question 13

what are enzymes activated by

Answer 13

metabolites

Question 14

classes of enzymes inhibition

Answer 14

Competitive and non-competitive inhibition

Question 15

competitive inhibition

Answer 15

reversible. adding more of proper substrate can out-compete and flush out the inhibitor

Question 16

non-competitive inhibition

Answer 16

where the inhibitor cannot be removed and you have to replace them enzyme with new enzyme

Question 17

where do inhibitors typically operate

Answer 17

the active site and at the allosteric site

Question 18

what can override or cancel inhibition at the allosteric site

Answer 18

activators

Question 19

what is ATP regulated by

Answer 19

ATP synthase (ATPase)

Question 20

energy charge

Answer 20

the sum of ATP and 1/2 the ADP/ all the ATP +ADP+AMP

Question 21

what is the energy charge of ATP producing reactions

Answer 21

1

Question 22

what is the energy charge of ATP consuming reactions

Answer 22

0

Question 23

what is the energy charge in healthy cells

Answer 23

0.7 and 0.9

Question 24

what are the 3 kinds of ATP synthase

Answer 24

F, V, and P-ATPase

Question 25

where is ATP synthase present

Answer 25

in the mitochondria, chloroplasts, and bacteria

Question 26

F-ATPase

Answer 26

the regular H+ transporting type found in the mitochondria
Fat type

Question 27

V-ATPase

Answer 27

types found on the vacuole
vacuole type

Question 28

P-ATPase

Answer 28

stands for pumping types

Question 29

T/F: ATPase can rotate

Answer 29

t

Question 30

What is the other use for ATP synthase besides as a catalyst for the ATP reaction

Answer 30

used to move H+ ions and generate electric charge

Question 31

what part of ATP synthase is the active site that makes ATP

Answer 31

the roof

Question 32

membrane potential

Answer 32

an electric charge across a membrane

Question 33

to hold a charge, you need a ________

Answer 33

membrane

Question 34

what direction do electrons flow

Answer 34

to the area with less electrons

Question 35

proton motive force

Answer 35

the gradient of H+ ions