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Biochem Muscle Weakness Self Study

Terms

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catabolism vs anabolism
ox/red
ATP use/gen
exergonic/endergonic
catab:
oxidative, ATP generation, exergonic

anab:
reductive, ATP use, endergonic
metabolic rate
basal metabolic rate
enthalpic change
normal heat production/time

basal: resting state
what metabolic processes are reflected in basal metabolic rates?
involunatry muscle work
osmotic grad maitenance
body temp
turnover/syn of cell constituents
Are the reactions A->B and B->C coupled?
how can A->B and c->D be coupled
coupling can occur provided delta G is neg, need a common intermediate, in an enz cat rxn the intermediate may exist only on the enz
NAD and NADP have the same standard reduction potentials,
but in the CELL NADP has a much more neg red. potential
which of the two nt's are more reduced?
NADP b/c lower reduction potential means more of your species is reduced, the nernst equation shows this
reduction potentials
relative affinity of the system for electrons compared to protons (- is a weaker affinity, + is higher)

note
nernst eqn gives the relationship b/w reduction potentials and ratio of (ox)/(red)
high energy bond
A large negative standard Gibb's free energy of hydrolysis
what is the mimimum value for a high energy bond
-7 kcal/mol(more neg = better)
as is seen in the ATP phosphoanyhdride bond
AMP + ATP -> 2 ADP
what enz does this
adenylate kinase
amp is often the product of a rxn, so converting it will often drive a rxn to the right
PPi + H2O -> 2Pi
what enz does this
pyrophosphatase
metabolic pool
a number of molecules that behave simultaneously reacting with the same enz and pathways
nucleotide pool
ATP ADP AMP rapidly interconvert and their concentrations can vary depending on E use, but the total [] of nucleotide pool varies slowly
describe energy charge
0 = all amp
1 = all atp
question 5 pg #365
??
rates of reaction are quantitatively controlled by the workload
kjb
reduction potentials

large vs small number
the smaller the number, the more reduced species there is according to the nernst equation, general rule of thumb as redox potentials as the gimme factor are skewed because they rely on the concentrations.


SMALLER NUMBER MEANS THERE IS MORE REDUCED SPECIES PRESENT
catabolism makes or uses ATP?
makes atp, it is an exergonic reaction

anabolism is coupled to the hydrolysis of ATP
how many high energy bonds does ATP have?
only 2

AMP has none
what types of bonds does ATP have?
phosphoanhydride
what does glutamine synthase do?
makes glutamine from glutamate and ATP,

example of the typical use of a SINGLE phosphoanhydride bond
Glutamyl tRNA synthetase what does it do
it makes glutamyl-tRNA from glutamate ATP and tRNA

example of typical use of two phosphoanyhdride bonds
co substrate
prosthetic group
prosthetic group
organic - coenzyme (vitamins)
inorganic

note: not all coenz are prosthetic groups, some are loosley bound and are then called cosubstrates(weakly assoc and get changed)

cofactor - in certain enz metal ion is neither cosubstrate or prosthetic group
what is the equation for energy charge?
1/2 [ADP] + 2ATP
AMP + ADP + ATP


fraction of high energy bonds to max high energy bonds possible
what are three ways to say ATP is plentiful?
high energy charge
resting cell
large negative delta G
what is the most sensitive parameter of change in adenine nucleotide pool and cytosol of cell?
AMP levels
this usually initiates the response to decreased ATP

ie stimulates PFK in glycolysis
two ways to control enzymes of a pathway
enzyme activity and amount of enzyme
critical control of a pathway
(2)
covalent regulation: p of a ser/thr, result of a balance between kinase and phophatase

control through the balance between the activities of two enzymes, one that does an irrev rxn one way and another that does the same rxn the opp way, this amplifies control of the catabolic pathway
ie PFK and frc1,6di phosphatase

THIS IS known as substrate cycling
substrate cycling control
see page 368

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