Drugs that inhibit the catalytic activity of an enzyme
Enzyme inhibitors
compete with natural substrate for active site
Competitive
The greater (blank) of inhibitor the less chance for the natural substrate to enter the active site
concentration
Conversely, the greater the concentration of natural substrate, less efficient is the inhibition -> leads to
toxicity
do not compete with the natural substrate for the active site
Noncompetitive
Usually bind to a different region of the enzyme and in doing so produce an induced fit, which changes the enzyme’s shape such that the active site (allosteric site) is no longer recognizable to the
substrate
Interact with an enzyme through non-covalent intermolecular interactions (H bonding, ionic bonding, van der waals)
Reversible
If the intermolecular interactions are extremely (blank), the equilibrium could be so far over the enzyme-inhibitor complex that inhibition is effectively irreversible.
strong
Targets antimicrobial and anticancer agents
Nucleic Acids
contain all the information required for the biosynthesis of the cell’s proteins
DNA
Consist of 2 (blank) which form a double helix
polymeric oligonucleotide strands,
Each strand of the helix s made up of a
deoxyribose sugar-phosphate backbone
Each strand of the helix s made up of a deoxyribose sugar-phosphate backbone, with a (blank) linked to each sugar moiety
nucleic acid base
Correct pairing:
adenine-thymine, guanine-cytosine
a single polymer
RNA
“photocopy” carries the genetic code for a specific protein
mRNA
“adapter” interpret the genetic conde has two binding regions
tRNA
– function as factories for protein synthesis
rRNA
The monomeric units of nucleic acids are referred to as
nucleotides
The monomeric units of nucleic acids are referred to as nucleotides, made up of at least
one phosphate group, (2) a pentose (5-carbon sugar), and a (3) heterocyclic nitrogenous base (referred to as nucleobases