Enzyme Kinetics II Flashcards
in the concentration vs time reaction, when the reactions is starting what is high
substrate & enzyme
in the concentration vs time reaction, when the reactions is starting what is low
ES low
product low
the state when the enzyme is just enzyme with the substrate, it is called
pre-steady
rate of formation of enzyme substrate complex is
directly proportional to the rate of the ES complex
For an enzyme catalyzed reaction, if the Vo is 10mM min-1 when the substrate concentration is 10mM, then what must Vmax be if we know that Km=30mM
40 mM min-1
what type of allostery is when it is the same ligand that is modifying the subunit to either positively or negatively
homotropic
what type of allostery is when it is the different ligand that is modifying the subunit to either positively or negatively
heterophic
when the binding of the inhibitor changes the site making it impossible for the substrate to bind is called
allosteric inhibition
when the binding of the ligand changing the active site allowing for the substance to bind to the substrate is called
allosteric activation
how are enzyme regulation
allostery
covalent modification
cleavage
inactive form of enzyme is called
proenzyme=zymogen
inactive form of chymotrypsin and trypsin
chymotrypsinogen and trypsinogen
when pro is added to like protein or non enzyme, what doe that mean
procollagen
what is the direction of converting inactive precursor to active enzyme by enzymatic cleavage
one-way street, unidirectional
benefit of making an inactive enzyme to active enzyme
because u have to wait to get the stimulus from the cell to do that so the enzyme doesn’t eat up other rthings
chymotrypsinogen chews to which amino acids
aromatic residue
Trypsinogen chews at which amino acids residue
Lysine residue
enzyme that add modification to the protein are called
writers
enzyme that remove modification to the protein are called
erasers
what do covalent structure affect
affect structure (therefore function)
changes charges
alter binding surface
blocks active sites
what do covalent structure result in
enzyme on/off
change localization
change substrate preference
change binding partners
degradation
—– enzyme adds phosphorylates and —– enzyme removes phosphorylation
kinases, phosphotases
which is specific kinase or phosphotases
kinase
glycogen phosphorylase exist in which form
active and less active
