enzymes Flashcards
what is an enzyme an example of
a functional protein
what monomer is enzymes made of
amino acids
how do i identify an enzyme by name
ends in “ase”
what makes an enzyme
polypeptide chains between amino acids
whats the minimum number of amino acids in an enzyme
50
what is the primary structure in an enzyme and what bond is involved
order of amino acids determined by DNA sequence, with polypeptide bonds between amino acids
what is secondary structure in an enzyme and what bond is involved
alpha helixes and beta pleated sheets; form by H-bonds between amino acids.
what is the tertiary structure in an enzyme and what bond is involved
3D folding, formed by R-group interactions (ionic, disulfide bridges, hydrophobic)
what is the quaternary structure in an enzyme
2 or more polypeptide chains.
what is an enzyme and its function
a organic catalyst that speeds up rate of rxn in organic processes by lowering activation energy.
whats activation energy
minimum amount of energy needed to start reaction
are enzymes changed or used in a reaction
no
what quantities are enzymes effective in
minute quantities
why are enzymes specific
because they can only catalyze one substance, and this substance is called a substrate.
what do cofactors and coenzymes do
increase rate of enzyme in catalyzed reaction
what are coenzymes
organic molecules that are required by certain enzymes to carry out the chemical reaction
how do coenzymes work
attach to enzyme and allow substrate to bond and reaction occurs (ex. Vitamin D)
what are cofactors often classified as
metal ion substances (ex. Fe)
what do inhibitors do
slow rate of reaction in enzyme catalyzed reaction
what is a irreversible inhibitor
one that bonds to the enzyme and doesnt come off, permanently blocking it (ex. lead)
what is a reversible inhibitor
one that forms a temporary bond and slows the rate of rxn while bound. it can be overcome by adding more substrates.
what does the attaching and removing of a reversible inhibitor create
feedback that allows for normal body regulation. increasing a substance stimulates release, and inhibiting it decreases the amount. this allows for us to stay in the small range of homeostasis.
what are competitive inhibitors.
inhibitors that closely match the substrate and compete for the active site with the substrate. it lowers the likelyhood of a enzyme binding to a substrate, decreasing overall rate of reaction
whats an example of a competitive inhibitor
antibiotics