Lecture 3 Flashcards
Pepsin works at ?
PH 2 Stomach
Amylase works at ?
PH 7 Mouth
Arginase “
PH 10 kidneys
As temperature increases what happens to the flexibility in the protein back bone
increases
Optimum temperature is dependent on?
hydroponic and hydrophilic interactions
K=
turnover number
e+s> es
k for forward and reverse reaction
k1 k-1
Es>E+ P
K for forward and reverse reaction
k2
not reversible
competitive Inhibitor?
has a similar shape to substate and occupies the active site
Inhibitor effect is reduced by
substrate concentration
Can enzyme controlled reaction reach the same Vmax with and without the inhibitor present?
yes if substate concentration is great enough
Km of the inhibited enzyme controlled reaction?
greater than without the inhibitor
In linnear regression km?
is closer to zero
Non-competitive inhibitor?
a small molecule which binds to a remote site on an enzyme and effects Kcat
Where do non competitive inhibitors bind?
allosteric sites
effect on active site (when in the presence of a non-competitive inhibitor)
conformational change of the enzyme active site, cannot bind to a substrate
Effect non-competitive inhibitor has on km
no effect
Y intersect on the liner regression on Micheal-mentons graph when enzyme is in the presence of a non-competitive inhibitor ?
greater
Positive regulator ?
activator
negative regulator
repressor
Uncompetitive inhibitor?
A substrate which binds to the enzyme substrate complex and stops the formation of any further products
uncompetitive inhibitors effect what which Is measured on a Micheal menton’s graph
Both Km and Vmax
Allosteric inhibition?
In which a product from an enzyme cascade inhibits the first enzyme
Curve to represent allosteric kinetics ?
sigmoidal curve not Micheal menton
Cleavage activation is an example of?
Covalent regulation
Cell signalling an example of?
Covalent regulation
Adenylation is ?
addition of AMP to an enzyme
Trysin enzyme Is made in?
why?
an inactive form: Tripsogen which when activated by the absence of an inhibitor, becomes trypsin
This mechanism is to stop trypsin damaging cells until outside cells where it is activated
Oxidoreducases ?
oxidation reduction reaction
Transferases?
transfer chemical groups
Hydrolase’s ?
Induce hydrolytic cleavage
Lyases
Cleave c-n c-o c=0 by eliminating molecules. Leaving double bonds, rings or conversely addition of groups to double bonds
Isomerases
catalyse geometric/strctural changes within molecule
Ligases
joining together of two groups coupled with hydrolysis of diphosphate bond
