1: Bacterial Metabolism Flashcards
Francisella tularensis
gram neg coccusbaccilus (between round and rod)
Bioterrorism
Tularemia: lung infection leads to septicemia and lymph node swelling
not usually deadly
carried by rabbits and small rodents
easily areosolized… like by lawn mowed rabbit
Hittite Plauge
earliest bioweapon attack 14th cent Francisella tularensis a lady walked a sick ram by the other soliders for days and then they got sick they retreated, they didn't die
Francisella tularensis as a bioweapon
"rabbit fever" easy to aerosolize very infectious... only 10-15 bacteria needed to infect non-persistend, easy to decontaminate highly incapacitating low lethality
Types of work within cell
Chemical work: make and break bonds
Transport work: move molecs against gradients
Mechanical work: movement of organism/structures in cell
activation energy
amount of nrg we have to put into system to get it over the hump
nrg required to overcome instability of rxn intermediate/the transition state (unstable halfway point)
enzymes
lower activation nrg
by stabilizing intermediate
this incs rate of transition from A and B to A+B
what drives chemcial reactions?
ENTROPY
enzymes help…
reaction happen more stablely and more quickly
where does the energy come from if we have no enzymes?
HEAT
substrate
the thing the enzyme is going to change
active site
where the chemistry of enzyme and substrate interaction happens
parameters for enzymes
pH
temperature
temp body/bacteria in body enzymes work best at
37 degrees
pH body/bacteria in body enzymes work best at
7
at temps that are higher
enzymes have decreased activity
because of denaturation
at temps that are low
enzymes don’t work as well bc of lack of heat energy
too acidic
too many protons… they get in the way, interact with stuff they shouldn’t
too basic
potons may leave the thing they’re supposed to be with
but ultimately, bacterial pH and temperature requirements depend on….
the environment they live it
substrate concentration
inc conc, inc enzymatic rate (up till saturation)
substrate ineraction happens randomly
cofactor
non-protein
associated with enzymeatic activity
metal ions (iron, copper, magnesium, zinc)
holoenzyme
apopenzyme and cofactor together… has activity
components don’t have activity on their own
apopenzyme
protein part of enzyme
sterility of stomach
bc the pH is so low
coenzyme
subset of cofactor ORGANIC molecules NAD often derived from vitamins used repeatedly
proenzyme
innactive form of enzyme
must be modified before it is active
this happens pretty quickly
Enzyme Inhibition types
Competitive
Non-competitive
Uncompetitive
how we kill bacteria
Competitive Inhibition
inhibitior binds to active site, competes with substrate
more inhibitor means enzyme is inactive bc susbstrate can’t bind to it
Non-competitive Inhibition
bind somewhere other than active site
cause conf change
enzyme has different shape, substrate can’t bind to active site
Uncompetitive Inhibition
inhibitor binds to the enzyme/substrate complez so that the substrate can’t be released
enzyme can’t function bc product not made, can’t bind to new substrates.
important inhibitors
Toxins (effector proteins)
Antibiotics: Kanamycin inhibits bacterial ribosomes
Antivirals
Zidovudine: HIV antiviral inhibits reverse transcriptase
Tamiflu: inhibits influenza enzyme for viron release
antivirals are usually
competitve or non-competiative
metabolism
catabolism and anabolism
catabolism
breaking down of compunds
releases more ATP
anabolism
synthesis
catabolism and anabolism…
BOTH release nrg
in the form of heat
glucose made of
6 carbons
6 oxygens
12 hydrogens
whats special about glucose?
super soluble in water
ATP and money
the “loose change”
but everyone can deal in it
NAD
$100 bill
how you take lots of money across state lines
what is ATP good for
storing nrg for a SHORT period of time
ATP phosphate bonds
transition from ATP to ADP: phosphate release
VERY LOW activation nrg req… easy to break off that phosphate
Making RNA… break off 2 phosphates
the second one is more stable, so breaking the second one off releases more nrg
high activation nrg
high activation nrg
stable
low activation nrg
unstable
is ATP stable or unstable
unstable
easy to break
good for short term storage
What is NADH
a coenzyme
REDOX
OIL RIG
movement of electrons
be able to identify what’s reduced and what’s oxidized… you got this
NADH
reduced electron carrier
NAD+
electron carrier… gets reduced
proton
a hydrogen atom without an electron
aka a hydrogen ion
the Role of NAD+
cofactor for lotssss of enzymes
NADH
reduced form of NAD+ has 2 extra electrons and one extra proton
neutral (not pos charged)
more stable than ATP
NADH is
the $100 bill
carries electrons
- to ETS
if no oxygen, it must be recycled to NAD+… this is why we have fermentation
glycolysis
glucose to pyruvate
uses a little ATP… gains a litle ATP
fermentation recycles NADH to NAD+
oxidative phosphorylation
when oxygen present
transfer electrons to slightly lower nrg states
move protons from one side membrane to other
oxygen
final electron acceptor
takes electron to its lowest nrg state
