Enzyme Structure and Function Flashcards
induced fit model of enzyme binding
substrate alters the enzyme active site (hand shake changes the other person’s hand)
4 catalytic strategies
- acid/base
- covalent
- electrostatic
- proximity/orientation
- [catalytic strategy] acid/base catalysis*
n/a
- [catalytic strategy] covalent catalysis*
enzymes form a covalent bond with the target molecule
electron carrier - decarboxylation (removes carboxyl group)
- [catalytic strategy] electrostatic catalysis
DNA is negatively charged with phosphate groups, magnesium 2+ can stabilize the negative charge (used by DNA pol)
- [catalytic strategy] proximity/orientation effects*
?
the crashing effect is increased; orientation also matters
kinase*
adds phosphate functional groups to different substrates
peptidyl transferase
transferring an amino acid to a chain of amino acids using tRNA (see picture)
- ligase
one of six types of enzymes
- joins two DNA fragments together
- oxidoreductase
catalyzes forward/reverse directions by moving electrons between molecules
ex. lactate dehydrogenase is able to remove a hydrogen from lactic acid (see picture)
- isomerase
changes one isomer into a different isomer (ex. phosphoglucose isomerase, chances glucose-6-P to fructose-G-P)
- hydrolase
uses water to cleave a molecule
ex. Protease (cuts Lys-Ala into two)
- lyase
cleaves a molecule without water or oxidation
6 types of enzymes
- ligase - joins two molecules
- oxidoreductate - moves electrons
- transferase - transfers one functional group to another
- isomerase
- hydrolase
- lyase
LOT-IHL
- transferase
transfers one functional group to another