1.2 Flashcards

1
Q

Macroelements (required in larger amounts) (2)

A

C, O, N, H, S, P
components of carbohydrates, lipids, proteins
and nucleic acids

K, Ca, Mg, Fe
exist as cations and play many roles, including
cofactors of enzymes

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2
Q

Trace elements (required in smaller amounts) (2)

A

Mn, Zn, Co, Mb, Ni, Cu

mainly needed as cofactors of enzymes

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3
Q

Sources of Energy

Phototrophs

A

Light

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4
Q

Sources of Energy

Chemotrophs (2)

A

oxidation of organic or

inorganic compounds

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5
Q

Sources of Reducing Equivalents

Need electron donors for (3)

A

electron transport chain (energy production)
oxidation-reduction rxns (includes energy production)
biosynthesis in autotrophs (from CO2)

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6
Q

Sources of Reducing Equivalents

Lithotrophs

A

reduced inorganic molecules

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7
Q

Sources of Reducing Equivalents

Organotrophs

A

organic molecules

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8
Q

Sources of Carbon

Autotrophs

A

CO2 main/only source

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9
Q

Sources of Carbon

Heterotrophs

A

reduced, preformed organic molecules

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10
Q

Photolithotrophic autotrophy (3)

A

light energy
inorganic electron donor
CO2 carbon source

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11
Q

Photoorganotrophic heterotrophy (3)

A

light energy
organic electron donor
organic carbon source

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12
Q

Chemolithotrophic autotrophy (3)

A

chemical energy source
inorganic electron donor
CO2 carbon source

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13
Q

Chemoorganotrophic heterotrophy (3)

A

chemical energy source
(all pathogens) organic electron donor
organic carbon source

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14
Q

N

A

source amino acids, ammonia

nitrate = ammonia N2

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15
Q

P source

A

inorganic phosphate (PO43-)

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16
Q

S source (2)

A
sulfate (SO42-)
reduced sulfur (e.g. cysteine)
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17
Q

Growth factors (3)

A

amino acids
purines and pyrimidines
vitamins (small organic molecules)

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18
Q

strict aerobes

A

perform aerobic respiration only

final electron acceptor is oxygen (reduced to H2O)

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19
Q

strict anaerobes

perform anaerobic respiration (2)

A

final electron acceptor is an inorganic molecule

examples: nitrate (NO3-), Fe3+

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20
Q
strict anaerobes 
perform fermentation (2)
A

final electron acceptor is an organic molecule
examples: pyruvate (reduced to lactate)
acetyl-CoA (reduced to ethanol)

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21
Q

facultative anaerobes

A

can perform respiration and fermentation

most medically relevant bacteria

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22
Q

Gram positive bacteria in the mouth (4)

A

Streptococcus spp. cocci facultative anaerobes
Peptostreptococcus spp. cocci strict anaerobes
Actinomyces spp. rods strict/facultative
anaerobes
Lactobacillus spp. rods facultative anaerobes

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23
Q

Streptococcus spp. cocci

A

facultative anaerobes

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24
Q

Peptostreptococcus spp. cocci

A

strict anaerobes

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25
Q

Actinomyces spp. rods

A

strict/facultative

anaerobes

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26
Q

Lactobacillus spp. rods

A

facultative anaerobes

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27
Q

Gram negative bacteria in the mouth (7)

A
Veillonella spp. cocci strict anaerobes
Aggregatibacter spp. rods capnophilic
Capnocytophaga spp. rods capnophilic
Porphyromonas spp. rods strict anaerobes
Prevotella spp. rods strict anaerobes
Fusobacterium spp. rods strict anaerobes
Spirochetes spirals strict anaerobes
28
Q

Veillonella spp. cocci

A

strict anaerobes

29
Q

Aggregatibacter spp. rods

A

capnophilic

30
Q

Capnocytophaga spp. rods

A

capnophilic

31
Q

Porphyromonas spp. rods

A

strict anaerobes

32
Q

Prevotella spp. rods

A

strict anaerobes

33
Q

Fusobacterium spp. rods

A

strict anaerobes

34
Q

Spirochetes spirals

A

strict anaerobes

35
Q

Facilitated diffusion (vs. passive diffusion) (3)

A

move from higher conc. to lower conc.
no energy requirement
permeases

36
Q

permeases

A

= carrier proteins embedded in

the plasma membrane

37
Q

Uptake is driven by

A

intracellular use of the
compound

Example: conversion of glycerol to glycerol-3-P

38
Q

Group translocation (4)

A

Transported substances are chemically altered during the process.
This process uses energy
Also called a phosphotransferase system (PTS or PEP-PTS)
Some sugars are transported this way

39
Q

This process uses energy:

A

phosphate bond
in phosphoenolpyruvate (PEP). Phosphate
from PEP is transferred to several protein
intermediates, eventually becoming linked
to the transported substance.

40
Q

Active transport

A

Energy is used to drive the accumulation of
a substance, which remains unchanged by
the transport process.

41
Q

Ion-driven transport systems use

A

proton
motive force (gradient of protons) by coupling
to an energetically unfavorable transport
event (concentration of a substance against a
gradient)
Common substances transferred are amino
acids.

42
Q

Binding protein dependent transport systems

use

A
membrane proteins that form a channel
and drive substances through the channel
using the energy from ATP hydrolysis.
Common substances transferred are sugars
and amino acids.
43
Q

All these transport processes use carriers that can be —.

A

saturated

44
Q

ferric iron is very — so uptake is difficult

A

insoluble

45
Q

• microorganisms use
— to aid
uptake

A

siderophores

46
Q

siderophore complexes

with

A

ferric ion

47
Q

complex is then

transported into —

A

cell

48
Q

• E. coli can grow on more than – different organic
compounds, using each to obtain C, H/electrons, and
energy

A

30

49
Q

• — can use several hundred compounds

A

Pseudomonas

50
Q

Nutritionally fastidious organisms have complex needs

and can only grow in association with

A

the human body or in
complex culture medium (example: blood agar).
Staphylococci and Streptococci

51
Q

Some bacteria are obligate intracellular parasites, such as

A

Chlamydia

52
Q

Growth in real world is suboptimal

A

variable growth rates for different organisms

53
Q

— responses protect bacteria

A

Stress

54
Q

Still cause damage to host when not growing (2)

A

immunogenic

toxin production

55
Q

Some bacteria — when they stop growth

A

sporulate

56
Q

Mechanisms of adaptation (2)

A
  • Maximize efficiency in using energy and resources

* Respond to changes

57
Q

The result of regulation:

pathways can be (2)

A

switched on and off

turned up or turned down

58
Q

How is control established? (2)

A
  1. Control of enzyme activity

2. Control of the number of enzyme molecules

59
Q

Control of enzyme activity

Example:

A

Allosteric regulation

60
Q

All enzymes have

A

active sites (for catalysis)

61
Q

Some enzymes also have

A

allosteric sites (for regulation)

62
Q

allosteric sites bind regulatory molecules (3)

A

noncovalent
reversible
affects activity of enzyme

63
Q

affects activity of enzyme
positive effectors — activity
negative effectors — activity

A

increase

decrease

64
Q

How do effector molecules act? (2)

A

a. change affinity of enzyme for substrate

b. change Vmax

65
Q

Control of the number of enzyme molecules

Regulation of enzyme synthesis) (2

A

A. Attenuation

B. Control of transcription initiation

66
Q

Catabolic pathways:

A

gene induction (by inducer)

67
Q

Anabolic pathways:

A

gene repression (by corepressor)