ATP
How many phsophates does atp have
3
the electronegativity of what single element drives all of aerobic metabolism
oxygen
homotrophic effector binds at the
substrate site
what can act as an on/off switch for enzymes
phoshphorylation
Vitamin B3 (or nicotinic acid) is a precursor for this cofactor that appears in many metabolic pathways:
NAD, NADPH
Delta G for ATP hydrolysis
-30.5 kJ/mol
breaks down, produces energy, oxidation
catabolism
pathway in which a substance is converted into an enzyme by another enzyme
zymogen cascade
T/F allosteric enzymes fit the michealis menton model
F (they have multiple active sites)
what category of molecules can carry one or two electrons
flavins
why is the hydrolysis of ADP to AMP and Pi more favorable than AMP to Pi and adenosine
ADP is the higher energy form, so it releases more energy when hydrolyzed
flow of electrons released by ________ form high to low potential
combustion
what enzyme converts ATP to ADP
kinase
In humans, what may be done with excess glucose when the need for ATP and glycolysis intermediates is low?
stored in the liver as glycogen
when to use NADH vs NADPH
NADH: catabolism
NADPH: anabolism
enzymes transfer phosphate bonded to what amino acid
histidine
equation to convert energy to gibbs free energy
dG=-nF(dE)
what enhances reactions by faciliting a reaction by providing a thermodynamically-favorable leaving group (one use of ATP)
adenylation regulation
glycine, alanine, tryptophan, etc
A student working in a research lab prepared a mutant version of trypsin, where the aspartate within the catalytic triad was changed to a threonine. How would this mutation likely influence the enzyme?
A) The mutation would most likely increase the kcat of the enzyme.
B) The mutation would most likely increase the ratio kcat / KM of the enzyme.
C) None of the above are likely
C
What 4 things make a high energy phosphate bond
electrostatic repulsion, resconance stabilization, ADP and Pi ionization, interactions with H2O
where are electrons stored/taken from in NADH
nicotinamide ring
What are some possible reasons why glycolysis is 10 steps rather than 1 step
multiple molecules made could be used in other cellular processes, many opportunities for regulation
What is the Kcat for this reaction:
vo (millimolar/sec): 3.4, 9.8, 12.9, 19.9, 20.0, 20.0 [substrate] (millimolar): 0.10, 0.30, 0.40, 0.80, 1.6, 5.0
enzyme concentration is 1.0 micromolar
0.30 mM
what amino acids are commonly involved in acetylase reactions to change the amino acids enzymatic activity
lysine