competitive inhibition
bind to active site, increase Km because decrease 1/Km
noncompetitive inhibition
bind to allosteric site, decrease Vmax because increase 1/Vmax
mixed inhibition
bind to allosteric site, increase or decrease Km, decrease Vmax because decrease 1/Vmax
uncompetitive inhibition
bind to the enzyme substrate complex, decrease Km because increase 1/Km, decrease Vmax because increase 1/Vmax
rate constant
k = Ae^-(Ea/RT)
impact of catalysts on a reaction
- no change in Gibbs energy (equilibrium products and reactants)
- decrease Ea, more stable transition state, increased rate constant
non-reducing sugar
lack of free anomerica carbon (ex: sucrose)
reducing sugar
presence of free anomeric carbon (ex: maltose)
glycosidic linkage
a covalent bond that joins a carbohydrate group to another molecule
epimers
a type of stereoisomer that differs in configuration at the anomeric carbon
anomers
type of stereoisomer that differs in configuration at the hemiacetal or acetal carbon
in vivo experiments
experiments conducted inside a living organism (animal model drug testing, clinical trials)
in vitro experiments
studies performed in controlled, artificial enviroments, focusing on specific cellular or molecular mechanism (purified enzyme kinetics, cell culture assays, PCR, western blotting)
aldose
sugar that contains aldehyde (carbon 1)
ketose
sugar that contains ketone (carbon 2)
pyranoses
6 membered ring sugars
fruranoses
5 membered ring sugars
