Chapter 8: Microbial Metabolism Flashcards

1
Q

how do enzymes increase the rate of a chemical reaction?

A

by lowering the energy of activation

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2
Q

what is meant by a simple enzyme

A

consists of only a protein

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3
Q

what is a conjugated enzyme and what is another word for it?

A

contains protein and nonprotein molecules; can also go by holoenzymes

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4
Q

what is the protein portion of a conjugated enzyme called?

A

apoenzyme

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5
Q

what is the nonprotein portion of a conjugated enzyme called?

A

cofactor

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6
Q

what are the two types of cofactors?

A
  • inorganic elements such as metal ions
  • organic molecules (coenzymes)
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7
Q

what does catalase do and what cofactor does it need?

A

breaks down hydrogen peroxide; Fe

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8
Q

what does oxidase do and what cofactor does it need?

A

adds an electron to oxygen; Fe and Cu

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9
Q

what does hexokinase do and what cofactor does it need?

A

transfers a phosphate to glucose, which is the first step of glycolysis; Mg

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10
Q

what does DNA polymerase do and what cofactor does it need?

A

responsible for DNA synthesis; Zn and Mg

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11
Q

what does pyruvate dehydrogenase do and what cofactor does it need?

A

converts pyruvic acid to acetyl-CoA and CO2 in the transitional step of cell metabolism; thiamine and Mg

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12
Q

what does succinate dehydrogenase do and what cofactor does it need?

A

oxidizes succinate to fumarate in Kreb’s cycle; FAD (contains riboflavin)

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13
Q

what is the active site

A

site specific for substrate binding

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14
Q

what are the purpose of cofactors?

A

they support the work the of the enzyme

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15
Q

functions of metallic cofactors

A
  • activate enzymes
  • bring active site and substrate together
  • actively participates in chemical reaction of enzyme-substrate complex
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16
Q

functions of coenzymes

A
  • serve as temporary carrier for functional groups
  • most commonly vitamins
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17
Q

what are exoenzymes

A

enzymes that leave the cell to break down large food molecules or harmful chemicals
ex. cellulase, amylase, penicillinase

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18
Q

what are endoenzymes?

A

enzymes that remain inside the cell

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19
Q

constitutive enzymes

A

always present, does not rely on substrate for its product

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20
Q

regulated enzymes

A

induced or repressed based on substrate concentration

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21
Q

condensation reaction

A

removes a water molecule to form a bond

ex. two glucose molecules form a glycosidic bond with removal of water creating maltose

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22
Q

hydrolysis reaction

A

breaks bond with the use of water

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23
Q

competitive inhibiton

A

competition for the active site

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24
Q

allosteric inhibiton

A

competitive inhibition, but on allosteric site rather than active

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25
Q

noncompetitive inhibiton

A

inhibitor binds to entire complex preventing reaction

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26
Q

enzyme supression

A

suppressing enzyme synthesis when there is too much end product

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27
Q

enzyme induction

A

enzymes made when there are substrates present

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28
Q

molecular structure of ATP

A
  • 5C ribose sugar
  • 3 phosphate
  • adenine nitrogenous base
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29
Q

explain glucose phosphorylation

A
  1. glucose and ATP bind to hexokinase sites
  2. hexokinase transfers a phosphate to glucose
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30
Q

examples of coenzymes

A

NAD and FAD

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31
Q

arginase function and its cofactor

A

acts on amino acid arginine; Manganese

32
Q

nitrate reductase function and cofactor

A

reduces nitrate to nitrite; Mo

33
Q

botulinum toxin function and cofactor

A

hydrolyzes protein needed for vesicle transport; Zn

34
Q

what are oxireductases

A

enzymes that can remove electrons from one substrate and add them to another

35
Q

aminotransferases

A
  • involves NH3+
  • redistributes nitrogen between amino acids
  • happens in protein metabolism and glucogenesis
36
Q

phosphotransferases

A
  • involves (PO4)3-
  • enzyme transfers phosphate groups
37
Q

methyltransferases

A
  • involves CH3
  • methyl groups are transferred to other molecules
38
Q

decarboxylases

A
  • involves CO2
  • removes a carboxyl group and releases carbon dioxide
39
Q

dehydrogenases

A

involves H+
- hydrogen removed from organic compounds

40
Q

transferases

A
  • involves C, N, P, and S
  • move functional groups from one molecule to another
41
Q

Hydrolases

A

involves H2O
- breaks bonds using water

42
Q

isomerases

A

molecule is turned from one isomer to another

43
Q

lyases

A
  • chemical bonds broken and double bonds/rings are created
44
Q

ligase

A

two molecules joined together with covalent bond

45
Q

lipase

A

breaks down fats in the body

46
Q

DNAase

A

break down DNA w hydrolysis of phosphate DNA backbone

47
Q

synthetases

A

joins two molecules by splitting phosphate group from a triphosphate

48
Q

polymerases

A

formation of a specific polymer

49
Q

cellulase

A

degrades cellulose

50
Q

lactase

A

breaks down lactose into glucose and galactose

51
Q

aldosaes

A

breaks down sugar to produce energy
- found in liver and muscles

52
Q

oxidase

A

O2 used as an electron acceptor to catalyze oxidation reactions

53
Q

what happens in glycolysis

A

Glucose is oxidized and split into two molecules of pyruvic acid. NADH is a byproduct.

54
Q

what is the final electron acceptor of aerobic respiration?

55
Q

what is the final electron acceptor in anaerobic respiration?

A

inorganic molecules

56
Q

what is the final electron acceptor in fermentation?

A

organic compounds

57
Q

steps of Kreb’s cycle

A
  1. Acetyl-CoA and oxaloacetate form citrate
  2. Citrate is transformed to isocitrate
  3. Isocitrate then converted to beta-ketoglutarate. NADH and CO2 released.
  4. Beta-ketoglutarate then converted to Succinyl CoA. CO2 and NADH released.
  5. Succinyl CoA converted to succinate. ATP created.
  6. Succinyl CoA becomes fumarate. FADH2 released.
  7. With the addition of water, fumarate is then turned into malate.
  8. Malate is then converted back to oxaloacetate. NADH created.
58
Q

what are the products of Kreb’s cycle

A

2 CO2
3 NADH
3 H+
1 FADH2
1 ATP

59
Q

Where does the Kreb’s cycle occur

A

cytoplasm in prokaryotes and mitochondria in eukaryotes

60
Q

glycolysis features

A
  • oxidation of glucose
  • occurs in cytoplasm of all cells
  • DOES NOT REQUIRE OXYGEN
61
Q

glycolysis products

A

2 ATP
2 NADH
2 H2O

62
Q

Electron transport system products

A

34 ATP
6 H2O

63
Q

chemiosmosis

A
  • pertains to the electron potential gradients across a membrane that leads to ATP synthesis with ATP synthase
64
Q

in cellular metabolism how much ATP is generated in total?

A

38 total; 36 net

65
Q

what happens in fermentation

A

pyruvic acid is converted to organic acid or alcohol

66
Q

how many ATPs are produced in fermentation

67
Q

amphibolism

A

refers to the way metabolic pathways have multiple functions
ex. numerous intermediates can synthesize amino acids, fats, nucleic acids, carbs

68
Q

amination

A

the addition of NH4 to pyruvic acid to create amino acids

69
Q

transamination

A

when an amino acid makes another amino acid

70
Q

deamination

A

amino acids being used as a source of glucose by releasing NH4

71
Q

what are the two stages of photosynthesis

A

light-dependent and light-independent reactions

72
Q

light dependent reaction

A

Either chlorophyll, carotenoid, or phycobilin pigments absorb photons. Photons excite an electron, which goes through photosystem II. As this happens, H2O is split by photolysis, releasing O2. Electrons pass through several structures that pump H ions. Once PS I is reached, NADPH is created. Because of the H ions being pumped, the gradient activates ATP synthase, creating ATP.

73
Q

light-independent reaction

A

uses ATP to fix CO2 to ribulose-1-5-bisphosphate and convert it to glucose

74
Q

phases of calvin cycle

A
  1. Carbon fixation
  2. Reduction
  3. Regeneration of RuBP
75
Q

where do light dependent reactions occur