enzymes Flashcards
(44 cards)
enzyme
biological catalyst
birds and mammals
endotherms
maintain optimum body temp for enzymes
even if environment changes
catalase
breaks down hydrogen peroxide
(toxic molecules made in metabolic reactions)
2H20 –> 2H20 + O2
examples of living tissues with high amounts of catalase
liver cells
potato cells
what is a limiting factor? give examples
determines the rate of reaction when at a sub optimal level
eg temp
conc of substrate
conc of enzyme
bio washing powder
removes biological stains
contains enzymes
save energy/environment
can work at low temps
some only work at 40C
activation energy
minimum energy required to start a chemical reaction
enzymes lower activation energy by forming ESC
speeds up metabolic reaction without high temps needed
enzymes as a globular protein
tertiary structure
specific 3D shape
soluble in water
metabolic role
hydrophobic R groups inside
hydrophilic R groups inside
enzyme tertiary structure dependence
specific sequence of amino acids in a polypeptide chain
primary
secondary
R group interactions can alter 3D shape H+ OH-
intracellular enzymes
inside of cell
eg digestive enzymes inside lysosomes bacterium
extracellular enzymes
outside of cell
eg saliva (amylase starch–> maltose)
enzymes breaking down
catabolic
hydrolysis
enzymes building up
anabolic
condensation
renaturation
small pH changes away from optimum pH
back to optimum pH
active site returns to complementary
denaturation
big pH changes
cant return
active site will never fit again
how pH affects enzyme action
ACID pH below 7 -> high conc H+
ALKALI pH above 7 -> high conc OH-
changing these conc changes interactions of R groups and H bonds/ ionic bonds
changes active sire of R groups
tertiary structure of active site changes
substrate no longer binds
DENATURE
initial rate of reaction
rate of enzyme substrate reaction is highest when enzyme and substrate are initially mixed
low temps below optimum
less Ke
decreases collisions of substrate and active site PER SECOND
less ESC formed per second
slower rate of reaction
high temp below optimum
more KE
more collisions of substrate and active site PER SECOND
more ESC per second
faster rate of reaction
heat denaturing
temp increase molecules have more Ke
too much Ke so H bonds and ionic bonds break
active site 3D shapes changes
no longer complementary
no more ESC form
optimum temp
highest rate of activity of enzymes
humans = 37C
thermophilic bacteria = 70C
cold climate organism = less than 5C
inhibitor
substance that slow down the rate of reaction
affects the enzyme in some way
competitive inhibitor
similar shape to substrate
can bind to active site
temporary reversible
prevents substrate binding to active site
effect can be reversed by increasing the conc of substrate
examples of competitive inhibitors
STATIN
competitive inhibitor of enzyme used to synthesise cholesterol
ASPIRIN
irreversibly binds to active site of cox enzyme
prevents synthesis of prostaglandins and thromboxane
(produces pain and fever)