ek Flashcards
how many peptide chains does chymotrypsin have
3
linked by
disuphide bridges
secreated by what
pancreas as the pro-enzyme chymotrypsinogen
how is inactive form activated and where
proteolysis in the duodenum, to form active chymotrypsin
function if chymotypsin
hydrolyse peptide bonds and aid protein digestion.
Digestive system of mammals
Degradation of ECM by migrating cells
Breakdown of proteins facilitates absorption
why is it aclled a Serine protease
its a protease
active site there is a serine residue
what it cleaves
cleaves protien on carboxyl side of aramotic
and lrge hydrophobic residues
what is KM
Michaelis Constant and is defined as the concentration of substrate at which a particular enzyme works at half its maximal velocity.
what is a high km
indicative of weak binding.
what is a low km
tight binding of a substrate to an enzyme.
what is a Lineweaver-Burk plot
A double-reciprocal plot of 1/Vo against 1/[S]
initial reaction rate and subtrate concentration
where is x intercept
1/km
what is why intercept
1/Vmax
gradient is what
Km/Vmax
during initial phase when velocity is constat what is the reaction said to be
steady
