Biochemistry Question Review Flashcards
Where would you find hydrophilic and hydrophobic amino acids in cells?
You would find hydrophilic AA in the cytosol and hydrophilic in the phospholipid bilayer
What Amino acids undergo phosphorylation by protein kinase enzymes?
Serine, Threonine and Tyrosine due to hydroxyl groups on side chains
Vmax is?
When an enzyme is working at maxium velocity
What is the Michaels-Menten Equations?
E+S⇔ES⇒E+P
V0=(Vmax [S])/(Km + [S])
Vmax=[K]Kcat
V=(Kcat[E][S])/(Km+[S])
V=((Kcat)/(Km))•[E][S} Only at low substrate concentrations
What are the units for Vmax?
Moles of enzyme per second
What is Kcat and what are the units?
Rate of Catalytic conversion of a substrate
Units: Number of substrate molecules turned over per enzyme/ second
What is Km?
Michael’s constant
The substrate concentration at which half of the enzyme’s active sites are full
At certain conditions, a High Km can indicate?
The high Km can indicate that the enzyme has a lower affinity for it’s substrate because it requires a higher substrate concentration
What is the one type of inhibition that does not bind to the allosteric site?
Competitive Inhibition-the inhibitor binds to the active site
Competitive Inhibition can be overcome by?
Adding more substrate
In Competitive inhibtion what are the differences in Vmax and Km?
In Competitive inhibition:
Vmax is not altered
Km is higher because substrate concentration has to be high to reach max velocity
In Non-competitive Inhibition, what is the difference to Vmax and Km?
In Non-competitive Inhibition:
Vmax is lower because less enzyme is available to react
Km remains the same
In mixed inhibition, what are the differences to Vmax and Km?
In mixed inhibition:
Vmax is lower
If inhibitor is bound to enzyme Km is higher
If inhibitor is bound to substrate Km is lower
In Uncompetitive Inhibition, what are the differences in Vmax and Km?
In Uncompetitive Inhibition:
Vmax is lower
Km is lower
A good way to remember if a passage is talking about an enzyme is to?
Look at the ending, if it ends in -ase it’s an enzyme
How do enzymes work in a reaction?
They increase reaction rates by facilitating the formation on a more stable transition state between reactants and products. This increased stability decreases the activation energy.
How is Delta G affected by enzymes?
Delta G is not affected by enzymes because they only stablize transition states
List the weight of the nucleotides from largest to smallest?
Largest
deoxyguanosine monophosphate (dGMP)
deoxyadenosine monophosphate (dAMP)
deoxythymine monophosphate (dTMP)
deoxycytidine monophosphate (dCMP)
Smallest
What Enzymes facilitate the dephosphorylation of ATP in Glycolysis?
Hexokinase/Glucokinase
PFK-1 (and if stimulated by insulin-PFK-2, because PFK-1 will be inactivated)
What Enzymes facilitate the phosphorylation of ADP in Glycolysis?
Phospholglycerate kinase
Pyruvate kinase
What Enzyme is involved in the reduction of NAD+ to NADH in Glycolysis?
Glyceraldehyde-3-P dehydrogenase
It occurs during the step of Glyceraldehyde 3-P→1,3 Bisphosphoglycerate
NADH is oxidized in what step of Glycolysis (assuming anerobic respiration)?
In the step of Pyruvate →Lactate by lactate dehydrogenase
What are the irreversable steps of glycolysis?
3 irreversible steps in glycolysis:
hexokinase (Glucose→Glucose 6-P);
phosphofructokinase (Fructose 6-P → Fructose 1,6-BisP);
pyruvate kinase (Phosphoenolpyruvate→Pyruvate)
What is alternitive splicing?
Rearrangement of introns and exon elements that are joined by splicing to alter mRNA coding sequences
A splice acceptor site is where?
The splicing site is at the end of intron 3’
What is the mneumonic for remembering nonpolar AA?
Grandma Always Visits London In May For Winston’s Party