enzyme types
move functional group from 1 molecule to another
transferase
_ activation energy of a reaction (do not get used up by the rxn)
lower
these are inorganic, usually minerals (Mg2+, Zn2+, etc) involved directly in catalysis
cofactors
responsible for muscle contraction
myosin
sequence of AA
primary structure
join 2 large biomolecules
ligase
do they have an effect in thermodynamics of the reaction?
NO
these are organic molecules req for enzyme to function eg NAD, FAD, vitamin complexes often remove e- from the molecule and transfer elsewhere
coenzymes
motor proteins: _ anterograde and _ retrograde and motility of cilia. Both used for intracellular transport
stabilized by H-bonds and disulfide bonds
tertiary structure
oxidoreductase
_ determines the function of the enzyme
structure
this model states the location where E reacts w S determines whether a S will bind
active site model
this structure is an organization of water around protein, forming H bonds
solvation shell
this number is determined by the avg of the pka values
isoelectric point
cleavage with the addition of water
hydrolase
enzymes may lose shape during temperature change and _
denature
induced-fit
this process separates proteins by size or charge, moves them across an electric field and larger molecules will move slowest. This specific one retains structure
NATIVE PAGE (charge to mass ratio)
this linkage occurs between two cysteine residues
disulfide linkage
cleave w/o water or electrons. Generate ring or double bond
lyase
this state is most energy during the reaction and is highly unstable, enzymes lower the activation energy by stabilizing this
transition state
these are components of adaptive immune sys, find foreign antigens and target them for destruction
antibodies
These two AA disrupt the a-helix
proline and glycine
every aa is _ configuration except cysteine which is _ because of the sulfhydryl group
S, R