Ch 3 - Enzymes Flashcards
substances that speed up reactions without being permanently altered
catalysts
energy input required to initiate a chemical reaction
activation energy
reactants in an enzyme-catalyzed reaction
substrates
particular binding site on an enzyme
active site
typical suffix in the names of enzymes
“-ase”
model that describes how the active site of an enzyme changes shape to tightly bind the substrate molecule
“induced fit” model
enzyme that breaks down sucrose
sucrase
enzyme that breaks down proteins
proteases
there are many specialized proteases - may also be called peptidase
enzymes that break down lipids
lipase
enzymes that build nucleic acid molecules by adding nucleotides to nucleic acid strands
polymerase
How does enzyme concentration affect reaction rate?
As enzyme concentration increases reaction rate increases
more enzymes, more frequent collisions between enzymes and substrates
How does substrate concentration affect reaction rate?
As substrate concentration increases reaction rate increases
more substrates, more frequent collisions between enzymes and substrates
How does temperature affect enzyme function?
Optimum temp: greatest number of collisions.
Heat: speeds up molecular movement - but too much will “denature” the enzyme shape
Cold: molecules move slower - thus decreasing collisions
(all enzymes have an optimal temp)
How does pH affect enzyme function?
changes in pH (H+ concentration) will disrupt bonding between enzymes and substrates.
changes in pH can also change the shape of the enzyme itself (thus changing the very specific shape of the active site)
(all enzymes have an optimal pH)
Inorganic compounds that help enzymes function
cofactors
Organic compounds that help enzymes function
coenzymes
Compounds that reduce enzyme activity by blocking the enzyme’s active site
competitive inhibitor
(this is “competitive inhibition”)
compounds “compete” for active site so substrate cannot bind
Compounds that reduce enzyme activity by binding to the enzyme (at allosteric site - other than active site) and change the enzyme’s shape
non-competitive inhibitor
(“non-competitive inhibition”)
this causes the active site to no longer be functional
Inhibition in which the inhibitor permanently binds to enzyme by covalent bonding
Irreversible inhibition (competitor=binds at active site) (allosteric=binds to other "allosteric" site)
Inhibition in which the final product of the pathway inhibits one of the earlier steps in the pathway
Feedback Inhibition
An overall chemical reaction that is divided up into many small steps (a series of chemical reactions)
metabolic pathway
(this is the normal organization of the complex chemical reactions that drive live processes - each step typically involves its own specific enzymes)