Bio 20 Flashcards
metabolism
all of the reactions which occur within our bodies (how quickly for food to become energy
organic molecules
carbon based molecules
organic molecule’s function
energy storage
carbohydrates
our body’s most important source of energy, plants
3 elements in carbohydrates
carbon, hydrogen, oxygen (“CHO”)
C, H, O occurs in a __:__:__ ratio in glucose
1:2:1 ratio in glucose
the number of carbons determine
the size of the molecule
to identify a sugar it ends with a “______”
“-ose”
Monosaccharide
simple sugars (one molecule)
isomers
same molecular formula (C6H12O6) bud different structural arrangement
disaccharides
combination of two monosaccharides by the removal of a water molecule
ex. sucrose, lactose, maltose
dehydration synthesis
removal of water molecules
polysaccharide
union of many monosaccharides
polysaccharide: Starch
plant polysaccharide
polysaccharide: cellulose
building block of plant cell walls
polysaccharide: glycogen
animal carbohydrate storage form, stored in liver and muscles
lipids (fats)
non-polar compounds that are insoluble in polar solvents like water, fats float,
lipids function
help store energy
what are lipids made of
glycerol and fatty acids
triglycerides are formed by
glycerol and fatty acids
triglycerides have ______ and ______
fats from animals (solid) at room temperature
Oils from plants (liquid) at room temperature
animal fat
saturated fats that have single covalent bonds
plant fats
polyunsaturated (double covalent bonds)
saturated fats
more stable, difficult to break down, solid, ex. animal
unsaturated fats
liquid
phospholipids
add a phosphate molecule to a lipid
waxes
long, stable molecules, waterproofing
proteins
structural components
what are proteins made of
C,H,O and nitrogen
Amino acids
building blocks of protein
Amino Groups
NH2
Acid Group
COOH
dehydration synthesis
a change in single amino acid can alter the protein, proteins join together form a peptide bond through dehydration synthesis
polypeptide
when many peptide bond to make ______
how many amino acids are there
20
true/false, all amino acids can be made by the body
false
proteins can change due to
temperature, ph, heavy metals
denature
temporary protein change
coagulation
a permanent protein change
exothermic reaction
reactions that have a net loss of energy in the form of light, heat, or sound
initial energy
required to start raction
known as activation energy
endothermic reaction
requires the constant addition of energy from an external source
does products have more energy than reactants?
yes
ex. photosynthesis
catabolism
breaking down of complex molecules to more smaller one. ex. glycogen to glucose to use in the blood stream
anabolism
simple molecules, complex structures
ex. glucose to glycogen
catabolism
breaking down complex molecules to smaller ones. ex. glycogen to glucose to use in the bloodstream
catalysts
chemicals that control the speed of chemical reactions without altering the products formed, can be used again and again
enzymes
globular protein catalysis found within living organisms
enzymes permit low temperature reactions by
reducing the reaction’s activation energy
enzymes end in the surfix?
“ose”
orient molecules for?
interaction
substrate
molecules that the enzymes act upon, changes into a product for the reaction
how does enzymes increase the possibility of reaction
by bring reactants together
active site
area of the enzyme that combines with the substrate
The “lock and key” model is proposed by
Emil Fischer
“lock and key”
describes enzyme-substrate complex
induced fit model
theory modifies, suggest the actual shape of the active sight is modifies
cofactors
inorganic molecules that help enzymes to bind with substrate molecules
coenzymes
organic molecules synthesized from vitamins that help enzymes to bind with substrate molecules
can coenzymes and cofactors work with more than one kind of enzyme
yes
factors effecting enzyme reactions
- competitive inhibitors
- non-competitive inhibitors
- feedback inhibition
- temperature
- pH
- substrate or enzymes concentration
competitive inhibitors
molecules with shapes similar to the substrate and will compete with the substrate fir the active site
non-competitive inhibitors
a substance that binds to a site other than active site, changes shape of active site, adding more substrate has no effect
feedback inhibition
in a metabolic pathway by the final product of the pathway, slows the reaction rate, and combines with the enzyme at a regulatory site, changing enzyme shape
temperature
heat will increase reaction rates as the molecules involved move faster and collide more often
what does temperature peak at to have enzyme denature
37 degrees Celcius, higher temperatures change active site
pH
each enzyme functions within a certain ph scale
what can pH disrupt
the hydrogen bonds between the amino acid group, changing enzyme shape
what can stomach enzymes function to
pH 9
substrate concentration
the greater the # of substrate exceeds the number of available enzymes, the reaction rate will level off
