Metabolic energy and enzymatic activity

Question 1

ATP

Answer 1

adenosine triphosphate (contains adenine, a ribose sugar, and 3 phosphate groups)

Question 2

ADP

Answer 2

adenosine diphosphate.
one phosphate group went away through hydrolysis

Question 3

AMP

Answer 3

adenosine monophosphate.
2 phosphate group went away through the hydrolysis of ATP and then ADP

Question 4

ATP work performance

Answer 4

1) driving endergonic reaction through phosphorylation of reactant

2) changing the shape and binding ability of proteins through phosphorylation

3) changing the shape and binding ability of proteins through non-covalent binding

Question 5

endergonic

Answer 5

reaction that requires energy to be driven

Question 6

exergonic

Answer 6

reaction that releases free energy from the process

Question 7

ATP synthase

Answer 7

enzyme that promotes the endergonic reaction of ADP to ATP with a phosphate addition

in the inner layer of mitochondria, in the thylakoid membrane of chloroplast, in the plasma membrane of bacteria

Question 8

enzymes

Answer 8

macromolecules acting as catalysts

Question 9

substrate

Answer 9

the reactant that the enzyme acts on.
Every enzyme is extremely specific for its substrate

Question 10

enzyme-substrate-complex

Answer 10

when an enzyme binds to a substrate

Question 11

active site

Answer 11

the region of the enzyme where the substrate binds

Question 12

induced fit

Answer 12

the enzyme changes its shape due to chemical reactions

Question 13

cofactors

Answer 13

non-protein helpers for catalytic activity, bound tightly (inorganic as metals, non-reversible) or bound loosely (organic as vitamins, reversible)

Question 14

apoenzyme

Answer 14

part of the enzyme that is not enzymatically active

Question 15

holoenzyme

Answer 15

when an apoenzyme binds with a cofactor

Question 16

inhibition

Answer 16

the action of enzyme inhibited,
reversible inhibition (weak interactions) irreversible inhibition (covalent bonds)

Question 17

competitive inhibition

Answer 17

mimics the substrate, competing for the active site

Question 18

noncompetitive inhibition

Answer 18

binds to the enzyme away from the active site changing the shape of the active site

Question 19

allosteric regulation

Answer 19

Allosterically regulated enzymes are typically composed of several subunits, each with its active site.
The entire complex oscillates between an active and an inactive state

Question 20

allosteric activator

Answer 20

regulatory molecules that bind to the enzyme in order to stabilize its active form

Question 21

allosteric inhibitor

Answer 21

regulatory molecules that stabilize the inactive form of the enzyme

Question 22

allosteric cooperativity

Answer 22

the active form is stabilized by the presence of a substrate in one of the active sites

Question 23

feedback inhibition

Answer 23

the end-product of a metabolic pathway is used to regulate its own production