Print Options

Card layout: ?

← Back to notecard set|Easy Notecards home page

Instructions for Side by Side Printing
  1. Print the notecards
  2. Fold each page in half along the solid vertical line
  3. Cut out the notecards by cutting along each horizontal dotted line
  4. Optional: Glue, tape or staple the ends of each notecard together
  1. Verify Front of pages is selected for Viewing and print the front of the notecards
  2. Select Back of pages for Viewing and print the back of the notecards
    NOTE: Since the back of the pages are printed in reverse order (last page is printed first), keep the pages in the same order as they were after Step 1. Also, be sure to feed the pages in the same direction as you did in Step 1.
  3. Cut out the notecards by cutting along each horizontal and vertical dotted line
To print: Ctrl+PPrint as a list

87 notecards = 22 pages (4 cards per page)

Viewing:

microbial metabolism

front 1

metabolism

back 1

all chemical reactions and physical workings of the cell

collects and spends energy in the form of ATP or heat

front 2

anabolism

back 2

biosynthesis of cell molecules and structures, requires energy input

front 3

catabolism

back 3

break the bonds of larger molecules, release energy

front 4

catalysts

back 4

speed up the rate of a chemical reaction without becoming part of the products or being consumed in the reaction

front 5

enzymes overcome activation energy allowing the reaction to proceed by

back 5

increasing thermal energy to increase the velocity of molecules

increasing the concentration of reactants to increase the rate of molecular collisions

adding a catalyst

front 6

enzyme characteristics checklist

back 6

most composed of protein and may require cofactors

act as organic catalysts to speed up the rate of cellular reactions

lower the activation energy required for a chemical reaction to proceed

have unique characteristics such as shape, specificity, and function

enable metabolic reactions to proceed at a speed compatible with life

front 7

substrates

back 7

reactant molecules upon which enzymes act

front 8

simple enzymes

back 8

consist of protein alone

front 9

conjugated enzymes

back 9

contain protein and some other nonprotein molecule

front 10

holoenzymes

back 10

whole conjugated enzymes

front 11

apoenzyme

back 11

protein portion of holoenzyme

front 12

cofactor

back 12

nonprotein protein of holoenzyme

can be organic or inorganic

front 13

active site or catalytic site

back 13

actual site where the substrate binds

three-dimensional crevice or groove formed by the way amino acid chains are folded

front 14

each enzyme has a different

back 14

primary structure, variation in folding, unique active site

front 15

metallic cofactors

back 15

iron, copper, magnesium, manganese, zinc, cobalt, selenium, etc.

assist with precise functions between enzyme and substrate

front 16

coenzymes

back 16

organic compounds that work with apoenzyme to alter substrate

remove chemical group from one substrate and add it to another substrate

front 17

vitamins are an important component of

back 17

coenzymes

front 18

oxidation

back 18

loss of electrons

a compound that loses electrons is oxidized

front 19

reduction

back 19

gain of electrons

a compound that gains electrons is reduced

front 20

two examples of coenzyme carriers

back 20

NAD and FAD

front 21

exoenzymes

back 21

transported extracellularly

break down large food molecules or harmful chemicals

front 22

endoenzymes

back 22

retained intracellularly and function there

most enzymes of metabolic pathways

front 23

constitutive enzymes

back 23

always present in relatively constant amounts, regardless of the cellular environment

front 24

regulated enzymes

back 24

production is turned on (induced) or turned off (repressed) in response to changes in concentration of substrate

front 25

denaturation

back 25

weak bonds that maintain the shape of an apoenzyme are broken by heat, low or high pH, or certain chemicals, distorts shape and prevent substrate attachment

front 26

competitive inhibition

back 26

a molecule that resembles the substrate occupies the active site, preventing the substrate from binding

enzymes cannot act on the inhibitor and is effectively shut down

front 27

noncompetitive inhibition

back 27

some enzymes have two binding sites - the active site and the regulatory site

regulated by the binding of molecules other than the substrate to the regulatory site

front 28

enzyme repression

back 28

stops further synthesis of an enzyme somewhere along its pathway

front 29

enzyme induction

back 29

enzymes appear (are induced) only when suitable substrates are present

front 30

exergonic reactions

back 30

release energy as they go forward

energy is available for doing cellular work

front 31

endergonic reactions

back 31

require the addition of energy to move forward

front 32

the removal of hydrogens from a compound during a redox reaction is called

back 32

dehydrogenation

front 33

NAD

back 33

most common electron carrier

carries hydrogens and a pair of electrons from dehydrogenation reactions

reduced NAD is presented as NADH + H+ or NADH

front 34

FAD

back 34

reduced FAD is presented as FADH

front 35

NADP

back 35

NAD phosphate

front 36

catabolic pathways

back 36

electrons are extracted and carried through a series of of redox reactions to a final electron acceptor

front 37

aerobic metabolism

back 37

oxygen is the final electron acceptor

front 38

anaerobic metabolism

back 38

some other inorganic or organic compound is the final electron acceptor (not oxygen)

front 39

adenosine triphosphate

back 39

three-part molecule

adenine, ribose, three phosphate groups bonded to the ribose

front 40

adenine

back 40

nitrogen base

front 41

ribose

back 41

5 carbon sugar

front 42

three phosphate groups bonded to ribose on ATP

back 42

bulky and negative, repelling electrostatic charges imposes a strain between the last two phosphate groups, removal of phosphates releases free energy

front 43

ATP

back 43

primary energy currency of the cell

it must be replaced, ongoing cycle

front 44

substrate-level phsophorylation

back 44

generation of ATP through a transfer of phosphate group from a phosphorylated compound directly to ADP

front 45

oxidative phosphorylation

back 45

a series of redox reactions occurring during the final phase of the respiratory pathway

front 46

photophosphorylation

back 46

ATP formed through a series of sunlight-driven reactions in phototrophs

front 47

three basic catabolic pathways

back 47

aerobic respiration, anaerobic respiration, fermentation

front 48

glycoysis

back 48

most common pathway used to break down glucose

front 49

fermentation pathway

back 49

facultative and aerotolerant anaerobes

uses only glycolysis

oxygen not required and use organic compounds as electron acceptors

front 50

aerobic respiration

back 50

a series of enzyme-catalyzed reaction

principal energy-yielding scheme for aerobic heterotrophs

provides ATP and metabolic intermediates for other pathways

front 51

glycolysis

back 51

glucose is enzymatically converted to pyruvic acid

may be the first phase of aerobic respiration or the primary metabolic pathway

synthesizes a small amount of ATP anaerobically

pyruvic acid is essential intermediary metabolite

front 52

pyruvic acid

back 52

a central metabolite

used in several pathways by many organisms

front 53

pyruvic acids in strict aerobes (and some anaerobes)

back 53

sent to the Krebs cycle

front 54

pyruvic acid in facultative anaerobes

back 54

re-reduced into acids or other products

front 55

the Krebs cycle

back 55

pyruvic acid into acetyl coenzyme A

oxidation releases first CO2

enzymes and coenzyme A dehydrogenate pyruvic acid to a 2-carbon acetyl group

NAD reduced to NADH

NADH is shuttled to ETC to produce ATP

front 56

how many times does the Krebs cycle happen

back 56

twice

front 57

Krebs cycle purpose

back 57

transfer energy stored in acetyl CoA to NAD+ and FAD by reducing them

front 58

main products of the Krebs cycle

back 58

reduced NADH and FADH2

two ATP produced through substrate-level phosphorylation

front 59

electron transport system

back 59

chain of special redox carriers that receives electrons from NADH and FADH2

electrons are passed sequentially from one redox molecule to the next

flow of electrons allows the active transport of hydrogens outside the cell membrane

oxygen receives hydrogesn and electrons and produces water

front 60

energy cascade sequence

back 60

NADH dehydrogenase

FMN

coenzyme Q

cytochrome b

cytochrome c1

cytochrome c

cytochromes a and a3

front 61

ATP synthase

back 61

stationed along the membrane in close association with the ETS carriers

captures released energy from the ETS carriers

front 62

oxidative phosphorylation

back 62

the coupling of ATP synthesis to electron transport

each NADH that enters the ETS gives rise to three ATP molecules

NAD and FMN enter the ETS at a different point, so there is less energy released, and only give rise to two ATP molecules

front 63

chemiosmosis

back 63

as the electron transport carriers shuttle electrons, hydrogen ions are actively pumped into the periplasmic space or the space between the cell wall and the cytoplasmic membrane

this sets up a concentration gradient of hydrogen ions called the proton motive force

front 64

proton motive force

back 64

consists of a difference in charge between the outside of the membrane (+) and the inside (-)

separation of charges temporarily stores potential energy

H+ can only diffuse into the membrane through ATP synthase, which sets the stage for ATP synthesis

front 65

aerobic respiration ATP production

back 65

total possible ATP is 40, but only keep at most 38 because must expended 2

4 from glycolysis

2 from krebs

34 from ETC

front 66

non ATP products of respiration

back 66

6 CO2 (Krebs)

6 O2 (consumed during ETC)

6 H2O (produced during ETC)

2 H2O (glycolysis) but 2 used in Krebs

front 67

anaerobic respiration: nitrate and nitrite reduction systems

back 67

found in E. coli

nitrate reductase catalyzes the removal of oxygen from nitrate reducing it to nitrite and water

front 68

alcoholic fermentation

back 68

occurs in yeast or bacteria species that have metabolic pathways for converting pyruvic acid to ethanol

decarboxylation of pyruvic acid to acetaldehyde

reduction of acetaldehyde to ethanol

front 69

homolactic fermentation

back 69

lactic acid bacteria reduce pyruvate to lactic acid mainly

front 70

heterolactic fermenation

back 70

glucose is fermented to a mixture of lactic acid, acetic acid, and carbon dioxide

front 71

mixed acid fermentation

back 71

members of the family enterobacteriaceae possess enzyme systems for converting pyruvic acid to several acids simultaneously

acetic, lactic, succinic, formic acids, as well as CO2

accounts for accumulation of some types of gas in the intestine

front 72

lipases

back 72

break apart fatty acids joined to glycerol which is converted to dihydroxyacetone phosphate which can enter step 4 of glycolysis

front 73

beta oxidation

back 73

oxidation of fatty acids

2-carbon units transferred to coenzyme A, creating acetyl CoA (Krebs)

oxidation of 6-carbon fatty acid yields 50 ATP, compared to 38 for a 6-carbon sugar

front 74

proteases

back 74

break down proteins to their amino acid components

amino groups removed through deamination

remaining carbon compound can easily converted to Krebs cycle intermediate

front 75

amphilbolism

back 75

most catabolic pathways contain strategic molecular intermediates that can be diverted into anabolic pathways

a given molecule can serve multiple purposes to derive maximum benefit from all nutrient and metabolites

catabolic and anabolic pathway are integrated to improve cell efficiency

front 76

precursor molecule

back 76

a compound that is the source of another compound

front 77

pyruvate as a precursor

back 77

provides intermediates for amino acids

front 78

gluconeogenesis

back 78

pyruvate is a starting point for glucose synthesis in the event of inadequate glucose supply

front 79

acetyl CoA as a precursor

back 79

can be converted into one of several amino acids

can be condensed into hydrocarbon chains for fatty acid and lipid synthesis

front 80

precursors to DNA and RNA

back 80

pathways that synthesize purines and pyrimidines originate in amino acids

can be dependent on intermediates from the Krebs cycle

front 81

carbohydrate biosynthesis

back 81

crucial role of glucose in metabolism and energy utilization

major component of cellulose cell walls and storage granules

glucose-6-P used to form glycogen

front 82

proteins

back 82

large proportion of cell's contents

essential components of enzymes, cytoplasmic membrane, cell wall, and cell appendages

twenty amino acids are needed to make these proteins

front 83

light-dependent reactions

back 83

proceed only in the presence of sunlight

catabolic, energy-producing reactions

front 84

light-independent reactions

back 84

proceed regardless of the lighting conditions

anabolic, synthetic reactions

carbon atoms from CO2 are added to the carbon backbones of organic molecules

front 85

the calvin cycle

back 85

occurs in the chloroplast stroma or the cytoplasm of cyanobacteria

use energy produced in the light phase to synthesize glucose

front 86

oxygenic photosynthesis

back 86

dominant type on earth

occurs in plants, algae, and cyanobacteria

front 87

anoxygenic photosynthesis

back 87

occurs in green and purple bacteria that utilize bacteriochlorophyll

have only cycling photosystem I

generate a small amount of ATP

use H2, H2S

many are strict anaerobes