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what could be considered a primary role for enzymes
enzymes accelerate the attainment of equilibrium, provides energy to subtrates so that the substrates readily reach the transition state, allow formation of transition state enabling reaction, enzymes only affect the energy of initiation or transition state energy
select the atoms that are (needed in trace amounts) by humans and probably gerbils
mg, v, cr,mn, fe, co, ni, cu, zn, se, mo,i
select the atoms that are (needed in abundance) by humans and probably gerbils
H,c,n,o (na,k,ca,p,s,cl)
from the list below select the biomolecule that is not used, metabolically as an energy source
nucleic acids (nucleotide)
what biomolecules are used as an energy source
proteins, lipids, carbohydrates, nucleic acids
a patient at (6 years old) presents with severe accumulation of lipids in many tissues and especially the liver. if the choices are wolmans disease and cholesterol ester storage disease what is the diagnosis
CESD (wolmans is lethal by age 1), exon splice error
what is expected from a wolmans disease patient
massive accumulation of exogenous cholesterol esters, results from premature stop codon, no functional protein detectable, lethal by age 1
what is expected of a cholesterol ester storage disease (CESD) patient
massive accumulation of exogenous cholesterol esters, caused by a single G to A mutation, disrupts splicing point for an exon, allows for low but functional levels of an enzyme
what is expected of a hers disease patient
phosphorylase deciciency (liver isozyme deficiency). symptoms is hepatomegaly (large liver), liver damage, hypoglycemia
what is expected of a diabetes melitus patient
overproduction of glucose by the liver, underutilization of glucose by other tissues
what is expected of a I Von Gierke disease patient
blood glucose deficiency caused by lack of enzyme glucose-6-phosphatase in the liver. symptoms is hypoglycemia, hepatomegaly (liver cancer), threat of lactic acidosis
which cellular compartment houses the enzymes related to wolmans disease and CESD
lysosomes
an enzyme that changes chirality would be classified as a
isomerase
what classification of enzyme is hexokinase
transferase
examination a lineweaver Burker plot for an enzyme system after an inhibitor is added reveals a sudden increase in the Y intercept. which of the following statements best describes what is happening at the enzyme level
the inhibitor is binding at a site that is not the active site and disrupting catalysis
competitive inhibition
inhibitor binds at the catalytic site inhibiting substrate binding but not catalysis
allosteric inhibition
inhibitor binds at a distal non catalytic site and blocks catalysis but not substrate binding
uncompetitive inhibition
inhibitor aids in susbtrate binding but also blocks catalysis
transition state inhibition
when bound, the enzyme achieves its lowest energy state and is no longer functional
suicide inhibition
binds to the enzyme and is catalyzed resulting in a covalent bond with the enzyme
which type of inhibitor would provide the best starting point for developing a therapy for ethanol sensitivity
uncompetitive inhibition
in hers disease what is the enzymatic failure
absence of liver phosphorylase
considering a muscle cells stimulated by epinephrine but is overloaded with atp. what is likely form and state of phosphorylase
A form, R state
why can liver cells generate glucose, but muscle cells cannot
muscle cells lack glucose-6-phosphatase
are the statements correct
(a) glucose is removed from glycogen by the enzyme phosphorylase creating glucose-6-phosphate
(b) this is how we know phosphorylase uses atp for the cutting
both are incorrect
both hers disease and type 1 von gierke disease possess the symptom of hypoglycemia. why does Von gierke also have the threat of lactic acidosis
Von Gierke clears glucose-6-phosphate by glycolysis rather than export
is the statements correct
(A) an isozyme is a variant of a given enzyme found in a different cellular location
(B) therefore, isozymes come from the same gene
B is incorrect
at which point is an enzyme in its lowest energy conformation
transition state
apoenzyme
inactive enzyme
holoenzyme
active enzyme
dG=0
equilibrium
dG>0
unfavorable
dG<0
favorable
what is the velocity formula
Vmax*[S}/kM + [S]
are the statements correct
(A) Km is a value of ½ of vmax
(B) is vmax is 200 units per second then km is 100 units per second
both are incorrect
nucleus
genomic storage/expression
mitochondria
ATP production
Rough ER
secreted/membrane-bound protein protection
cytoplasm
cellular protein synthesis
lysosome
cellular digestion
how was metabolism to be determined to be a highly conserved system across species
glycolysis was found in yeast and animals
what genetic error causes CESD
exon splice error
what genetic error causes Wolman’s disease
premature stop codon
proteins
structure/catalysis
nucleic acids
information storage/coenzymes
lipids
cell signaling/membranes
carbohydrates
storage/source of electrons
which of the diseases manifests due to dramatically reduced but still present activity of a particular enzyme?
CESD (cholesterol ester storage disease)
which biomolecule class plays the largest role in metabolism
proteins
which biomolecule class plays the largest role in energy storage
lipids
which biomolecule class plays the largest role in signaling
proteins
which biomolecule class plays the largest role in energy production
carbohydrates
which biomolecule class plays the largest role in catalysis
proteins
which cell compartment is the primary site of protein production
cytosol
which cell compartment is the primary site of atp production
mitochondria
which cell compartment is the primary site of cell digestion production
lysosome
which cell compartment is the site of protein generation for membrane bound proteins
rough ER
Which enzymes are likely to be significantly regulated?
unidirectional arrows
what does bold/underlined enzymes mean
they are considered to have higher binding affinity in the forward direction than other enzymes that consume the same substrate
steady state system
conditions remain constant, so no net charge
equilibrium system
rate of forward and reverse reactions are equal, so no net charge
dg<0
spontaneous
dg>0
non spontaneous
what is the formula for km
vmax(s)/v -s
what does km represent?
the concentration of S at which ½ of the active sites of the enzymes are filled and the velocity is ½ of vmax
if km is small
it takes low levels of s to fill the active site and the ES complex is strong
if km is large
it takes high levels of s to fill the active site and the ES complex is weak
graph for competitive inhibitors
km increases, vmax stays the same
graph for uncompetitive inhibitors
km drops and vmax drops
graph for noncompetitive inhibitor
km stays the same, vmax drops
kinase enzyme
catalyzes addition of PO4 to Serine, threonine, tyrosine
phosphatase
removes PO4 moiety
why do le chateliers principle technically does not apply to living systems (although we can use them to an extent)
cell pathways are never at equilibrium, temperature is likely to remain unchanged, living systems are not closes systems.
the enzyme catalyzes the conversion of organic compounds to alternative forms
isomerase
role of glycogen in liver
maintains blood glucose levels, highest concentration of glycogen by weight. glucose released during fasting periods.
which enzyme of glycolgenolysis is most likely to run in reverse
phosphoglucomutase
phosphorylase A
usually active, and usually R form. primarily in liver
phosphorylase B
usually inactive, and usually T form. resting muscles are almost all in B form
which metabolite is going to connect glycogenolysis to other pathways
glucose-6-phosphate
what is the role of glycogen in the muscle
serves as energy storage, used as last resort.
a technician is testing phosphorylase in muscle cells and notes that u