Chapter 6 Review

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Campbell Biology
Chapter 6
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1

metalbolic pathway

a specific molecule that is altered in defined steps, resulting in a product. ( always catalyzed by an enzyme )

2

catabolic pathway

release energy by breaking down complex molecules to simpler compounds.

3

anabolic pathways

consume energy to build complicated molecules from simpler ones.

4

photosynthesis

decrease in energy

5

cellular respiration

increase in entropy

6

T

temperature

7

H

enthalpy

8

S

entropy

9

first law of thermodynamics

energy can be transferred and transformed but never created nor destroyed.

10

second law of thermodynamics

every energy transfer or transformation increases the entropy of the universe.

11

entropy

randomness

12

enthalpy

total heat of a system or internal energy

13

free energy

a systems energy that can preform work when pressure and temperature are constant. measure of systems instability.

14

spontaneous reaction

a process that leads to an increase in entropy without an input of energy.

15

exergonic

loss of free energy, increase of entropy, delta G is negative, temperature is increased, enthalpy is decreased.

16

endergonic

absorbs free energy, decrease of entropy, delta G is positive, temperature is decreased, enthalpy is increased.

17

ATP

ribose, 3 nitrogenous bases, adenine, and 3 phosphate groups that is a renewable source.

18

ADP

made by a hydrolysis reaction where terminal phosphate bond is broken and a molecule of inorganic phosphate is left over.

19

energy coupling

exergonic process to drive an endergonic one. ATP is responsible for this in cells and acts as an intermediate source of energy that powers cellular work.

20

phosphorylated intermediate

transfer of a phosphate group from ATP to another molecule and that molecule covalently bonds to a phosphate group.

21

hydrolysis of sucrose

involves breaking bonds between glucose and fructose and one of the bonds of a water molecule which then forms 2 new bonds

22

activation energy/ free energy of activation

the energy required to contort the reactant molecules so the bonds can break. pushes reactants to top so they can go “downhill”.

23

transition state

when molecules have absorbed energy for the bonds to break, the reactants are in an unstable condition.

24

formation of bonds

release energy

25

breaking of bonds

absorbs energy

26

catalysis

speed up enzyme reactions

27

substrate

the reactant an enzyme acts on

28

enzyme- substrate complex

an enzyme bonded to a substrate when there are 2 or more substrates.

29

active site

where enzyme binds to substrate

30

to speed up reactions…

add more enzyme.

31

activity of enzyme

effected by pH and temperature

32

cofactors

non protein helpers for catalytic activity.

33

cofactors of enzymes include…

metal atoms: zinc, iron, and copper.

34

competitive inhibitors

reduce productivity of enzymes by blocking substrates from entering active site.

35

noncompetitive inhibitors

do not directly compete with substrate but instead bind to another part of the enzyme, changing its shape.

36

mutation

permanent change in genes.

37

allosteric regulation

any case in which proteins function at one site is affected by the binding of a regulatory molecule to a separate site. This changes an enzymes shape and function of active site.

38

activator

stabilizes the shape of a functioning active site.

39

inhibitor

stabilizes the inactive form of an enzyme.

40

cooperactivity

a substrate molecule binding to one active site in its multi subunit enzyme triggers a shape change in all the subunits. This increases the catalytic activity at the other active sites and amplifies the response of enzymes to substrates.

41

equilibrium

forward and backward reactions occur at the same rate and delta G equals 0. This preforms NO work and has no net change.

42

disequilibrium

cells maintain this as open systems.