1Serial reactions
product of one enzyme is often the substrate of the next enzyme, helps channel substrates into the enzymes , rate of cell metabolism increases
2Molecular tunnels
allows intermedietes to move efficently through active sites, some enzymes have multiple active sites and either lose or gain NH3
3Irreversible inhibition
Tightly wound covalent or noncovalent dissasociates slowly from target enzyme
4Reverseble inhibition
enzyme-inhibitor rapidly dessasociates and thie is compettive, noncompetitve, and uncompetitive
5Reverseble inhibitor type 1
Competitive inhibitor mimics the structure of substrate and competes w substrate for the same binding cite, only binds to free enzyme
6Reverseble inhibitor type 2
Non-competitive inhibitor binds to a side distinct from the active site does not substrate binding binds free enzyme or ES
7Revereble inhibitor type 3
uncompetitve only binds to ES complex
8allosteric protiens
protiens that can adopt two or more structures when a ligand binds
9ATP Case
displays sigmoidal kinetcs
10coopertiveity
in some multi subunit enzymes, ligand binding to to one unit chaning the effects
11hexokinease
most cells Low Km
12Glukokinase
liver high Km
13homotrophic events
effects of substrate on allosteric protiens
14heterotrophic
effects of non substrate molecules on the protiens
154 protoeases
Serine. cystine. aspartl process, and metalprotiease
16Tryspin has a substrate preference for
long polar side chains