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Microbio Lec FINAL > Chapter 8: Microbial Metabolism > Flashcards

Chapter 8: Microbial Metabolism Flashcards

(75 cards)

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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
noncompetitive inhibiton
inhibitor binds to entire complex preventing reaction
26
enzyme supression
suppressing enzyme synthesis when there is too much end product
27
enzyme induction
enzymes made when there are substrates present
28
molecular structure of ATP
- 5C ribose sugar - 3 phosphate - adenine nitrogenous base
29
explain glucose phosphorylation
1. glucose and ATP bind to hexokinase sites 2. hexokinase transfers a phosphate to glucose
30
examples of coenzymes
NAD and FAD
31
arginase function and its cofactor
acts on amino acid arginine; Manganese
32
nitrate reductase function and cofactor
reduces nitrate to nitrite; Mo
33
botulinum toxin function and cofactor
hydrolyzes protein needed for vesicle transport; Zn
34
what are oxireductases
enzymes that can remove electrons from one substrate and add them to another
35
aminotransferases
- involves NH3+ - redistributes nitrogen between amino acids - happens in protein metabolism and glucogenesis
36
phosphotransferases
- involves (PO4)3- - enzyme transfers phosphate groups
37
methyltransferases
- involves CH3 - methyl groups are transferred to other molecules
38
decarboxylases
- involves CO2 - removes a carboxyl group and releases carbon dioxide
39
dehydrogenases
involves H+ - hydrogen removed from organic compounds
40
transferases
- involves C, N, P, and S - move functional groups from one molecule to another
41
Hydrolases
involves H2O - breaks bonds using water
42
isomerases
molecule is turned from one isomer to another
43
lyases
- chemical bonds broken and double bonds/rings are created
44
ligase
two molecules joined together with covalent bond
45
lipase
breaks down fats in the body
46
DNAase
break down DNA w hydrolysis of phosphate DNA backbone
47
synthetases
joins two molecules by splitting phosphate group from a triphosphate
48
polymerases
formation of a specific polymer
49
cellulase
degrades cellulose
50
lactase
breaks down lactose into glucose and galactose
51
aldosaes
breaks down sugar to produce energy - found in liver and muscles
52
oxidase
O2 used as an electron acceptor to catalyze oxidation reactions
53
what happens in glycolysis
Glucose is oxidized and split into two molecules of pyruvic acid. NADH is a byproduct.
54
what is the final electron acceptor of aerobic respiration?
oxygen
55
what is the final electron acceptor in anaerobic respiration?
inorganic molecules
56
what is the final electron acceptor in fermentation?
organic compounds
57
steps of Kreb's cycle
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
what are the products of Kreb's cycle
2 CO2 3 NADH 3 H+ 1 FADH2 1 ATP
59
Where does the Kreb's cycle occur
cytoplasm in prokaryotes and mitochondria in eukaryotes
60
glycolysis features
- oxidation of glucose - occurs in cytoplasm of all cells - DOES NOT REQUIRE OXYGEN
61
glycolysis products
2 ATP 2 NADH 2 H2O
62
Electron transport system products
34 ATP 6 H2O
63
chemiosmosis
- pertains to the electron potential gradients across a membrane that leads to ATP synthesis with ATP synthase
64
in cellular metabolism how much ATP is generated in total?
38 total; 36 net
65
what happens in fermentation
pyruvic acid is converted to organic acid or alcohol
66
how many ATPs are produced in fermentation
2
67
amphibolism
refers to the way metabolic pathways have multiple functions ex. numerous intermediates can synthesize amino acids, fats, nucleic acids, carbs
68
amination
the addition of NH4 to pyruvic acid to create amino acids
69
transamination
when an amino acid makes another amino acid
70
deamination
amino acids being used as a source of glucose by releasing NH4
71
what are the two stages of photosynthesis
light-dependent and light-independent reactions
72
light dependent reaction
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
light-independent reaction
uses ATP to fix CO2 to ribulose-1-5-bisphosphate and convert it to glucose
74
phases of calvin cycle
1. Carbon fixation 2. Reduction 3. Regeneration of RuBP
75
where do light dependent reactions occur
thylakoid

Microbio Lec FINAL (6 decks)

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