Cellular energies

Energy

ability to do work

kinetic energy

energy of motion

potential energy

stored energy

example of potential energy

food

first law of thermodynamics

energy can’t be created nor destroyed, changed from 1 form to another

second law of thermodynamics

energy cannot be changed from one form to another without a loss of usable energy

metabolism

sum of chemical reactions that occur in a cell

reactants

substances that participate in a reaction

products

substances that are formed as a result of reaction

anabolic

creating bigger, complex molecules from smaller molecules. requires energy

catabolic

breaking down complex molecules and releasing energy for the body

exergonic reactions

reactions that release energy

ex of exergonic reactions

cellular respiration

endergonic reactions

require energy input

ex of endergonic reactions

photosynthesis

activation energy

energy needed for molecules to react with one another

catalyst

substance that increases rate of chemical reaction without undergoing permanent chemical change

enzymes

protein that facilitates chemical reactions

enzyme functions

join molecules together, break molecules apart

enzyme names

typically end in -ase, name relates to the substrate

substrate

reactant of enzymatic reaction

active site

location of enzyme that comes in direct contact with substrate

enzyme-substrate complex

intermediate formed when substrate and enzyme attach at the active site

enzyme shape

3D shape, specific to certain substrates,

what causes protein denaturization

heat

induced fit

when substrate initially binds w enzyme and isnt a perfect match, substrate and enzymes will change their shape to join together

enzyme reaction rate

how fast enzymes break down substances

Vmax

maximal reaction rate of an enzymatic reaction when enzyme is saturated with substrate

substrate concentration

as you increase the amount of substrate, more product can be produced by the enzyme

optimal pH

regulate structural configuration of enzymes *EACH ENZYME HAS AN OPTIMAL pH*

pH of most human enzymes

6-8

salvilary amylose pH

6-7

trypsin pH

7.5

lipase pH

8

pepsin pH

2-3

denatured

protein bonds break if temp/pH rises past a certain point

enzyme inhibition

occurs when molecules bind to an enzyme and decreases activity

2 types of enzyme inhibition

competitive, noncompetitive/allosteric

competitive inhibition

inhibitor binds w active site and competes w substrate

allosteric site

region away from active site, changes active site in some way

noncompetitive inhibition

inhibitor binds w allosteric site, it changes the active site and regulates the enzyme reaction

allosteric activation

occurs when binding of one ligand enhances the attraction between substrate and active sites

compartmentalization

division of something into sections for a specific function

enzyme pathway

series of link reactions

enzyme cycle

enzyme pathway that does not have a specific end product

misconception about the enzyme cycle

they do not go around in a circle, scientists illustrate it in a circle so it is easier to visualize

feedback inhibition

product produced by an enzyme binding to the enzymes active site