induced fit model of enzyme binding
substrate alters the enzyme active site (hand shake changes the other person’s hand)
4 catalytic strategies
n/a
enzymes form a covalent bond with the target molecule
electron carrier - decarboxylation (removes carboxyl group)
DNA is negatively charged with phosphate groups, magnesium 2+ can stabilize the negative charge (used by DNA pol)
?
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)
one of six types of enzymes
catalyzes forward/reverse directions by moving electrons between molecules
ex. lactate dehydrogenase is able to remove a hydrogen from lactic acid (see picture)
changes one isomer into a different isomer (ex. phosphoglucose isomerase, chances glucose-6-P to fructose-G-P)
uses water to cleave a molecule
ex. Protease (cuts Lys-Ala into two)
cleaves a molecule without water or oxidation
6 types of enzymes
LOT-IHL
transfers one functional group to another
co-enzyme
organic carrier molecules
co-factor
stabilizes the charge of DNA