Principles 1-2 Flashcards
what are the elements required for cell components
- macroelements
- trace elements
which element is required in larger amounts
macroelements
what are C, O, N, H, S and P required for
they are components of CHO, proteins and lipids and nucleic acids
what are K, Ca, Mg, and Fe required for
they exist as cations and play many roles including cofactors of enzymes
what are the trace elements
Mn, Zn, Co, Mb, Ni, and Cu
what are the trace elements required for
cofactors of enzymes
what are the sources of energy
-phototrophs use light
-chemotrophs use oxidation of organic or inorganic compounds
what are electron donors needed for
-ETC (energy production)
- oxidation reduction reactions
- biosynthesis in autotrophs from CO2
what are lithotrophs
reduced inorganic molecules
what are organotrophs
organic molecules
what are sources of carbon
-autotrophs : CO2 main/only source
- heterotrophs: reduced, preformed organic molecules
what are sources of reducing equivalents
lithotrophs and organotrophs
what are the major nutritional types of organisms
- photolithotrophic autotrophy
- photoorganotrophic hetertrophy
- chemolithotrophic autotrophy
- chemioorganotrophic heterotrophy
what type of light energy, electron donor, and carbon source do photolithotrophic autotrophs use
- light energy
- inorganic electron donor
- CO2 carbon source
what type of light energy, electron donor, and carbon source do photoorganotrophic heterotrophs use
- light energy
- organic electron donor
- organic carbon source
what type of light energy, electron donor, and carbon source do photoorganotrophic heterotrophs use
- light energy
- organic electron donor
- organic carbon source
what type of light energy, electron donor, and carbon source do chemolithotrophic autotrophs use
-chemical energy source
- inorganic electron donor
- CO2 carbon source
what type of light energy, electron donor, and carbon source do chemoorganotrophic heterotrophs use
-chemical energy source
- organic electron donor
- organic carbon source
what are the other nutrient sources and what are they
-N source: amino acids, ammonia nitrate -> ammonia
- P source: inorganic phosphate (PO4)3-
- S source: sulfate (SO4)2-
- growth factors: amino acids, purines and pyrimidines, vitamins
what do strict aerobes do and what is the final electron acceptor
-perform aerobic respiration only
- final electron acceptor is oxygen ( reduced to H2O)
what do strict anaerobes do and what is the final electron acceptor
- perform anaerobic respiration
- final electron acceptor is an inorganic molecule such as (NO3)- and Fe3+
- perform fermentation
- final electron acceptor is an organic molecule such as pyruvate reduced to lactate and acetyl Co-A reduced to ethanol
what do facultative anaerobes do
can perform respiration and fermentation
what is the most medically relevant bacteria
facultative anaerobes
what are the gram positive bacteria in the mouth and what is the shape of each and type of bacteria
- streptococcus spp. : cocci, facultative anaerobes
- peptostreptococcus spp.: cocci, strict anaerobes
- actinomyces spp.: rods, strict/facultative anaerobes
- lactobacillus spp.: rods, facultative anaerobes
what are the gram negative bacteria in the mouth and what is the shape of each and type of bacteria
- veillonella spp: cocci, strict anaerobes
- aggregatibacter spp: rods, capnophillic
- capnocytophaga spp: rods, capnophilic
- porphyromonas spp: rods, strict anaerobes
- prevotella spp: rods, strict anaerobes
- fusobacterium spp: rods, strict anaerobes
- spriochetes: spirals, strict anaerobes
what are permeases
carrier proteins embedded in the plasma membrane
what is the difference in the rate of transport between facilitated and passive diffusion
facilitated diffusion reaches a maximum, passive is linear
what happens in group translocation
- transported substances are chemically altered in the process
- process uses energy from the phosphate bond in PEP
- phosphate becomes linked to the transported substance
what is another name for group translocation
PTS or PEP-PTS or phosphotransferase system
what is transported in group translocation
some sugars
what do ion driven transport systems in active transport use
proton motive force (gradient of protons) by coupling to an energetically unfavorable transport event (concentration of a substance against a gradient
what are common substances transferred using ion driven transport systems in active transport
amino acids
what do binding protein dependent transport systems in active transport use
membrane proteins that form a channel and drive substances through the channel using the energy from ATP hydrolysis
what are common substances transported using the binding protein dependent transport system
sugars and amino acids
all transport processes that use carriers can be _____
saturated
why is uptake of ferric iron difficult
it is very insoluble
what do microorganisms use to uptake ferric iron
siderophores which complexes to iron then is transported into the cell
what does E. coli use organic compounds it grows on for
C, H/electrons and energy
how many organic compounds do E coli grown on
more than 30
how many compounds can pseudomonas grow on
several hundred
where do nutritionally fastidious organisms grow and give example
in association with the human body or in complex culture medium such as staphylococci and streptococci
what is an example of a bacteria that is an obligate intracellular parasite
chlamydia
what are the microbial growth and resting states
lag, exponential, stationary
growth in real world is ____
suboptimal
____growth rates for different organisms
variable
what do stress responses do
protect bacteria
can microbes cause damage to host even when not growing and how
yes, immunogenic and toxin production
some bacteria _____ when they stop growth
sporulate
what are the mechanisms of adaptation
-maximize efficiency is using energy and resources
- respond to changes
what are the possible results of regulation
- pathways can be switched on and off
- pathways can be turned up or turned down
how is control established
- control of enzyme activity
- control of the number of enzyme molecules
how can enzyme activity be controlled
allosteric regulation
all enzymes have active sites used for ____
catalysis
some enzymes have allosteric sites for _____
regulation
what do allosteric sites do
bind regulatory molecules
what are the different types of allosteric sites
- noncovalent
- reversible
- affects activity of enzyme where positive effectors increase activity and negative effectors decrease activity
how do effector molecules act
- change affinity of enzyme for substrate
- change Vmax
how can you control the number of enzyme molecules
by regulating enzyme synethsis through attenuation or control of transcription initiation
how can transcription initiation be controlled
-catabolic pathways: gene induction (by inducer)
- anabolic pathways: gene repression by corepressor
