Metabolism Flashcards

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1
Q

What is the first step of glycolysis?

A

Glucose enters the cell and is phosphorylated. A molecule of ATP is invested. The product is 6-glucose phosphate.

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2
Q

What is the second step of glycolysis?

A

Glucose 6-phosphate is rearranged to form fructose 6-phosphate.

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3
Q

What is the 3rd step of glycolysis?

A

The phosphate group from another ATP is used to produce fructose 1, 6- diphosphate, still a 6 carbon compound (2 ATP are invested at this point.

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4
Q

What is the 4th step of glycolysis?

A

An enzyme splits the sugar into 2 3-carbon molecules: dihydroxyacetone phosphate (DHAP) and glyceraldehyde 3-phosphate (GP)

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5
Q

What is the 5th step of glycolysis?

A

DHAP is readily converted to GP the reverse reaction may occur.

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6
Q

What is the 6th step of glycolysis?

A

The next enzyme converts each GP to another 3-carbon compound 1,3-diphosphoglyceric acid. Because each DHAP molecule can be converted to GP and each GP to 1, 3-diphosphoglyceric acid for each initial molecules of glucose. GP is oxidized by the transfer 2 hydrogen atoms to NAD+ to form NADH. The enzyme couples this reaction with the creation of a high-energy bond between sugar and a phosphate group. The 3 carbon sugar now has 3 phosphate groups.

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7
Q

What is the 7th step of glycolysis?

A

The high energy phosphate group is moved to ADP, forming ATP, the first ATP production of glycolysis. Since step 4 all products are doubled, therefore, this step is actually repays the earlier investment of 2 ATP molecules.

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8
Q

What is the 8th step of glycolysis?

A

An enzyme relocates the remaining phosphate group of 3-phosphoglyceric acid to form 2-phosphoglyceric acid in preparation for the next step.

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9
Q

What is the 9th step og glycolysis?

A

By the loss of a water molecule 2-phosphoglyceric acid is converted into phosphoenolpyruvic acid (PEP). In the process, the phosphate bond is upgraded to a high energy bond.

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10
Q

What is the 10th step of glycolysis?

A

The high energy phosphate bond is transferred from PEP to ADP, forming ATP. For each initial glucose molecule, the result of this step is 2 molecules of ATP and 2 molecules of a 3-carbon compound called pyruvic acid.

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11
Q

What is another name for glycolysis?

A

Embden-Meyerhof pathway

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12
Q

Phosphorylation

A

The transferring of phosphate group from a donor to the recipient molecule.

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13
Q

Cellular respiration

A

ATP generating process in which molecules are oxidized and the final electron acceptor comes from outside the cell and is almost always an inorganic molecule.

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14
Q

Glycolysis

A

The oxidation of glucose to pyruvic acid, usually the 1st stage in carbohydrate catabolism.

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15
Q

Oxidation

A
  • the removal of electrons from an atom or molecule, a reaction that often produces energy
  • the removal of one or more electrons from a substrate. Protons H+ are often removed with electrons
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16
Q

Reduction

A

a molecule has gained one or more electrons

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17
Q

Redox reaction

A
  • Oxidation and reduction reactions are always coupled; each time a substance is oxidized another is simultaneously reduced.
  • oxidation reaction paired with reduction reaction
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18
Q

Metabolism

A

The sum of all chemical reactions in an organism

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19
Q

Catabolism

A

The breakdown of complex molecules into monomers; provides energy and building blocks for anabolism

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20
Q

Anabolism

A

Uses energy and building blocks to build large molecules from monomers.

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21
Q

What links catabolic and anabolic reactions?

A

energy, catabolic reactions provide energy for anabolic reactions.

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22
Q

Energy+monomers =

A

macromolecule

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23
Q

during catabolism macromolecules are being broken down into ___________.

A

monomers and energy

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24
Q

How does catabolism release energy ?

A

by the oxidation of molecules

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25
Q

Anabolism uses ________

A

energy to synthesize macromolecules that make up the cell

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26
Q

ATP stores_________.

A

energy

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27
Q

Energy is released by __________ of ATP.

A

hydrolysis

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28
Q

ADP + inorganic phosphate+ energy =

A

ATP

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29
Q

ATP - Energy =

A

ADP and inorganic phosphate

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30
Q

What are metabolic pathways determined by?

A

enzymes which are encoded by genes different genes means different proteins (enzymes being made) = different metabolic pathways

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31
Q

Enzymes are encoded by

A

genes

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32
Q

Catabolic reactions transfer energy from

A

complex molecules to ATP

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33
Q

Anabolic reactions transfer energy from

A

ATP to complex molecules

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34
Q

Although microbes can cause disease and food spoilage many metabolic pathways are ____________.

A

beneficial

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35
Q

The pharmaceutical industry uses microbes such as ______________

A

bacteria and fungi to make antibiotics

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36
Q

vitamins, vaccines, antibiotics, and enzymes are dirived from ____________.

A

microbial metabolism

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37
Q

What is the big picture of the function of an enzyme?

A

they facilitate metabolic reactions

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38
Q

Most living things use __________ to manage energy needs.

A

ATP

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39
Q

Catabolic reactions couple with _____________.

A

ATP synthesis

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40
Q

Anabolic reactions couple with _________.

A

ATP break down

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41
Q

Chemical reactions

A

Chemical reactions can occur when atoms, ions, and molecules collide

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42
Q

Activation energy

A

Activation energy is needed to disrupt existing bonds, even in spontaneous reactions

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43
Q

Reaction rate

A

Reaction rate is the rate of formation of products from reactants.

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44
Q

A reaction rate can be increased by

A

Enzymes, temperature or pressure

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45
Q

Why does a reaction rate increase when pressure is applied to reactants?

A

The reactants are in closer proximity to each other which increases the likelihood of a reaction occuring

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46
Q

Why does a reaction rate increase when temperature is increased?

A

heat will energize the molecules and cause them to move faster; increasing the chances that the molecules will collide and a reaction will occur.

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47
Q

Why do enzymes increase reaction rates?

A

because they ether bend bonds between molecules allowing substrates to be broken down more easily, or they bring molecules closer together and position them to increase the chances of a chemical reaction.

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48
Q

Enzymes help to increase the likeihood of chemical reactions by _____________.

A

reducing the activation energy need elicit a chemical reaction. Enzymes are catalysts.

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49
Q

Enzymes

A

Biological catalysts; specific; not used up in that reaction

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50
Q

What are the components of an enzyme?

A

Apoenzymes, Cofactors, Holoenzymes

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51
Q

Coenzyme

A

an organic cofactor

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52
Q

Apoenzyme

A

inactive protein portion of an enzyme

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53
Q

Cofactor/coenzyme

A

non-protein agent which activates the enzyme by binding to the Apoenzyme.

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54
Q

Holoenzyme

A

whole, complete active enzyme. Made up of apoenzyme and cofactor

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55
Q

Examples of Coenzymes

A

NAD+, NADP+, FAD

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56
Q

The names of enzymes usually end in _________.

A

-ase

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57
Q

enzymes can be grouped into ____ classes

A

6; according to the type of chemical reaction they catalyze

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58
Q

Enzymes within the 6 classes are named after _________.

A

the specific types of reactions they assist

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59
Q

oxidoreductases

A

enzymes which are involved in oxidation-reduction reactions; oxygen or hydrogen are gained or lost. ex. cytochrome oxidase, lactate dehydrogenase

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60
Q

What are enzymes in oxioreductase class remove hydrogen from substances?

A

dehydrogenase; those that add electrons to molecular oxygen (O2) are called oxidases

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61
Q

Transferase

A

responsible for transfer of functional groups amino group, acetyl group or phosphate group ex. Acetate kinase, alanine deaminase

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62
Q

Hydrolase

A

responsible for hydrolysis (addition of water) ex. lipase and sucrase

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63
Q

Lyase

A

responsible for removal of groups of atoms without hydrolysis ex. Oxalate decarboxylase and isocitrate lyase

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64
Q

Isomerase

A

Responsible for rearrangement of atoms in a molecule ex. Glucose-phosphate isomerase, alanine racemase

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65
Q

Ligase

A

responsible for joining of 2 molecules (usually using energy from the break down of ATP) ex. Acetyl CoA synthase, DNA ligase

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66
Q

How does the mechanism of enzymatic reactions work?

A
  1. An enzyme molecule has an active site where it binds the substrate molecule
  2. The reaction between the substrate molecule and enzyme forms a complex and may temporarily alter the active site slightly
  3. The enzyme molecule brakes apart the substrate molecule
  4. 2 end products result from the reaction and are released from the enzyme.
  5. The enzyme molecule remains unchanged and is recycled.
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67
Q

What are the factors that influence enzyme activity

A
  1. Temperature
  2. pH
  3. Substrate concentration
  4. Inhibitors
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68
Q

Enzymes can become __________ by inappropriate pH or temp.

A

denatured

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69
Q

enzyme activity/ reaction rate increases with temperature until

A

the enzyme reaches a point where it becomes denatured and can no longer facilitate reactions

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70
Q

why are catabolic and anabolic reactions important?

A

they allow an organism to grow and reproduce by providing energy and the monomers necessary to build macromolecules

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71
Q

when glucose is transormed into ATP where do the electrons go?

A

they will be transferred to oxygen

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72
Q

During each chemical reaction in a metabolic pathway there is ___________.

A

an enzyme facilitating the reaction

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73
Q

What is the energy level of ADP?

A

low

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74
Q

What is the enegy level of ATP?

A

high; due to the ustable bonds between the phosphate groups

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75
Q

energy is stored in the bonds between ________.

A

carbon atoms

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76
Q

sunlight is converted into glucose in plants the glucose in plants then ________.

A

powers the biochemical reactions of animals

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77
Q

ADP is provided by the ___________.

A

constant breakdown of ATP.

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78
Q

why ae enzymes needed by living things?

A

because most chemical reactions are too slow to be compatible with life.

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79
Q

you need 2 things to convert a molecule into another

A
  1. activation energy
  2. enzymes
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80
Q

Enzymes are ___________.

A

biological catalysts made by living cells to help lower the activation energy of a biochemical reaction

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81
Q

the same enzyme can continue facilitating reactions as long as________.

A

substrate is available

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82
Q

some enzymes cannot work without ________.

A

cofactors

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83
Q

Lock and key model

A
  • the shape of the enzyme is specific to its substrate
  • Enzymes have a very specific 3 dementional shape
  • when you disrupt the 3d shape of an enzyme, you change the shape of the activation site and it can no longer bind with its substrate.
  • Denaturation is loss of the enzyme’s 3d structure
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84
Q

When there is low [substrate] enzymes work _______.

A

slower because substrate molecules are spread out.

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85
Q

Enzymes convert _________ to __________.

A
  • reactions
  • products
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86
Q

optimum pH/ Temperature

A

the temp/ pH at which enzymes best function

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87
Q

when is an enzyme considered denatured?

A

when it can no longer work

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88
Q

Why do amalyse enzymes stop working when they reach the stomach?

A

because the pH of the enviornment is too low and causes denaturation.

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89
Q

do all enzymes work at the same pH or temperature?

A

no, different enzymes have different optimal pH and temperatures

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90
Q

what are the types of inhibitors

A
  1. competitive inhibitors
  2. non-competitive (allosteric) inhibitors
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91
Q

competative inhibitors

A

competative inhibitors compete with a real substrate for the active site of an enzyme

92
Q

non-competitive/ allosteric inhibitors

A

binds to enzyme in another spot, which causes a change in the shape of the active site of an enzyme. these types of inhibitors disable enzymes by changing their configuration and distorting its active site.

93
Q

what is an example of a competative inhibitor?

A
  • sulfa drugs (sulfanilamide)
  • penicillin
94
Q

sulfanilamide competes with __________

A
  • PABA
  • “Sulfanilamide is a competitive inhibitor of bacterial enzyme dihydropteroate synthetase. This enzyme normally uses para-aminobenzoic acid (PABA) for synthesizing the necessary folic acid. The inhibited reaction is normally necessary in these organisms for the synthesis of folic acid. Without it, bacteria cannot replicate.
95
Q

Feedback inhibition

A
  • Also known as end-product inhibition
  • Controls amount of substance produced by a cell
  • Mechanism is allosteric inhibition
  • Feeds back to stop pathway early on to stop the wasting of nutrients.
96
Q

where is the energy for chemical reactions stored?

A

ATP

97
Q
A
98
Q

What is the structure of enzymes?

A

globular proteins with a 3 dementional shape

99
Q

What happens when an enzyme and substrate combine?

A

the substrate transforms and the enzyme does not change

100
Q

What can be a cofactor for an enzyme?

A
  • iron
  • copper
  • magnesium
  • manganese
  • zinc
  • calcium
  • cobalt

organic molecules/coenzymes:

  • NAD+
  • NADP+
  • FMN
  • FAD
  • Coenzyme A
101
Q

what happens when an enzyme is at a low temperature?

A

the reaction rate decreases

102
Q

Do Enzymatic activities increase as the amount of substrate increases?

A

yes, up until all enzymes are saturated

103
Q

a non competetive inhibitor caan bind with

A

the apoenzyme or its cofactor

104
Q

Feedback inhabition

A

occurs when the end-product of a metabolic pathway inhibits an enzyme’s activity near the start of a pathway.

105
Q

Ribozymes

A

Enzymatic RNA molecules involved in protein synthesis

106
Q

What happens during substrate level phosporylation?

A

a high energy phosphate from an intermediate (occurring in the middle of a process or series) in catabolism is added to ATP.

107
Q

each time a substance is oxidized another is _______

A

simultaniously reduced

108
Q

NAD+ is the oxidized form of

A

NADH and NADH is the reduced form of NAD+

109
Q

Is glucose oxidized or reduced?

A

glucose is a reduced molecule; energy is released during a cell’s oxidation of glucose.

110
Q

summary of how ATP is made

A

Energy released during certain metabolic reactions can be trapped to form ATP from ADP and an inorganic phosphate. addition of an inorganic phosphate is called phosphorylation.

111
Q

what happens during oxidative phosphorylation?

A

energy is released as electrons are passed to a series of electron acceptors (an electron transport chain) and finally to O2 or another inorganic compound.

112
Q

what happens during photophosphorylation?

A

energy from sunlight is trapped by chlorophyll and electrons are passed through a series of electron acceptors. The electron transfer releases energy used for the synthesis of ATP.

113
Q

Metabolic pathway

A

a series of enzymatically catalyzed chemical reactions called metabolic pathways store energy in and release energy from organic molecules

114
Q

where does most of a cell’s energy come from?

A

most of a cell’s energy is produced from the oxidation of carbohydrates

115
Q

what are the 2 major types of carbohydrate metabolism?

A
  1. Respiration
  2. Fermentation
116
Q

During cellular respiration ___________.

A

sugar is completely broken down

117
Q

During fermentation __________.

A

sugar is partially broken down

118
Q

what is the most common pathway for oxidation of glucose

A
  • glycolysis
  • Pyruvic acid is the end product
119
Q

how many ATP and NADH are made from 1 glucose molecule?

A
  • 1 glucose molecule
120
Q

NADH

A
  • Nicotinamide adenine dinucleotide (NAD) is a coenzyme found in all living cells. The compound is a dinucleotide, because it consists of two nucleotides joined through their phosphate groups. One nucleotide contains an adeninebase and the other nicotinamide. Nicotinamide adenine dinucleotide exists in two forms, an oxidized and reducedform abbreviated as NAD+ and NADH respectively.
  • In metabolism, nicotinamide adenine dinucleotide is involved in redox reactions, carrying electrons from one reaction to another
121
Q

FADH2

A

In biochemistry, flavin adenine dinucleotide (FAD) is a redox cofactor, more specifically a prosthetic group, involved in several important reactions in metabolism. FAD can exist in three (or four: flavin-N(5)-oxide) different redox states, which are the quinone, semiquinone, and hydroquinone. FAD is converted between these states by accepting or donating electrons.

FAD, in its fully oxidized form, or quinone form, accepts two electrons and two protons to become FADH2(hydroquinone form). The semiquinone (FADH·) can be formed by either reduction of FAD or oxidation of FADH2 by accepting or donating one electron and one proton, respectively.

122
Q

Pentose phosphate pathway

A
  • used to oxidize 5-carbon sugars; one ATP and 12 NADPH (from NADP+) molecules are produced from 1 glucose molecule.
  • Also known as the hexose monophosphate shunt.
  • operate simultaneously with glycolysis
  • produces important intermediate pentoses used in nucleic acid synthesis, certain amino acids, and glucose from carbon dioxide in photosynthesis.
123
Q

The Entner-Doudorof pathway

A

yeilds 1 ATP and 2 NADPH molecules from oxidation of 1 glucose molecules

124
Q

Many bacteria have additional

A

pathways in addition to glycolysis for the oxidation of glucose. The most common alternitive is the pentose phosphate pathway or the entner-doudoroff pathway

125
Q

What happens during respiration?

A

during respiration organic mole cules are oxidized (lose electrons) Energy is generated fom oxidation (the loss of electrons) of the electron transport chain.

126
Q

what functions as the final electron acceptor in aerobic respiration?

A

O2

127
Q

what are the final electon acceptrs in anaerobic respiration?

A
  • NO3- (nitrate)
  • SO42- (sulfate)
  • CO32- (Carbonate)
128
Q

Decarboxylation

A

Decarboxylation is a chemical reaction that removes a carboxyl group and releases carbon dioxide (CO2). Usually, decarboxylation refers to a reaction of carboxylic acids, removing a carbon atom from a carbon chain.

129
Q

Decarboxylation of pyruvic acid produces

A
  • 1 CO2 molecule
  • one acetyl group
130
Q

what happens to 2 carbon acetyl groups in the krebs cycle?

A
  • they get oxidized in the krebs cycle. Electrons are picked up by NAD+ and FAD for the electron transport chain.
131
Q

What must happen to pyruvic acid so it can enter the krebs cycle?

A
  • it mus be decarboxylated (lose one molecule of CO2) to become a 2 carbon compound
  • The 2 carbon compound is called an acetyl group and it attaches to Coenzyme A through a high energy bond to form Acetyl Coenzyme A
  • during this reaction pyruvic acid is oxidized and NAD+ is reduced to NADH.
132
Q

oxidation of one glucose molecules produces _________.

A

2 pyruvic acids

133
Q

For every 1 glucose that under goes glycolysis

A
  • 2 CO2 molecules are formed
  • 2 pyruvic acids are formed
  • 2 molecules of NADH are created
134
Q

what happens to Acetyl coA as it enters the krebs cycle?

A

CoA detaches from the acetyl group and and the acetyl group combines with oxaloacetic acid to form citric acid. This synthesis reaction requires energy which is provided by the high energy bond between acetyl group and CoA

135
Q

in the krebs cycle each reaction is catalyzed by

A

a specific enzyme

136
Q

how many carbo atoms does Pyruvic acid have?

A
  • 3
  • because it was split from a 6 carbon sugar
137
Q

Decarboxylation produces

A

6 molecules of CO2

138
Q

From 1 molecule of glucose oxidation produces

A
  • 6 molecules of NADH
  • 2 molecules of FADH2
  • and 2 molecules of ATP
139
Q

What do NADH and FADH2 do with the electrons they pick up?

A

they both carry electrons to the electron transport chain by NADH

140
Q

what are the carriers in the electron transport chain?

A
  • flavoproteins
  • cytochromes
  • ubiquinones
141
Q

flavoprotein

A

any of a class of conjugated proteins that contain flavins and are involved in oxidation reactions in cells.

142
Q

conjugated protein

A

A conjugated protein is a protein that functions in interaction with other (non-polypeptide) chemical groups attached by covalent bonding or weak interactions. Many proteins contain only amino acids and no other chemical groups, and they are called simple proteins.

143
Q

cytochromes

A

Cytochromes are iron containing hemeproteins central to which are heme groups that are primarily responsible for the generation of ATP via electron transport.

144
Q

ubiquinones

A
  • Coenzyme Q10, also known as ubiquinone, ubidecarenone, coenzyme Q, and abbreviated at times to CoQ10CoQ, or Q10 is a coenzyme that is ubiquitous (everywhere) in the bodies of most animals.
  • This oil-soluble, vitamin-like substance is present in most eukaryotic cells, primarily in the mitochondria. It is a component of the electron transport chain and participates in aerobic cellular respiration, which generates energy in the form of ATP.
145
Q

Proton Motive Force

A

In most cases the proton motive force is generated by an electron transport chain which acts as a proton pump, using the energy of electrons from an electron carrier (Gibbs free energy of redox reactions) to pump protons (hydrogen ions) out across the membrane, separating the charge across the membrane.

146
Q

oxidative phosphorylation

A

Oxidative phosphorylation (or OXPHOS in short) is the metabolic pathway in which the mitochondria in cells use their structure, enzymes, and energy released by theoxidation of nutrients to reform ATP.

147
Q

substrate phosphorylation

A

Substrate-level phosphorylation is a type of metabolic reaction that results in the formation of adenosine triphosphate(ATP) or guanosine triphosphate (GTP) by the direct transfer and donation of a phosphoryl (PO3) group to adenosine diphosphate (ADP) or guanosine diphosphate (GDP) from a phosphorylated reactive intermediate. Note that the phosphate group does not have to come directly from the substrate. By convention, the phosphoryl group that is transferred is referred to as a phosphate group.

148
Q

Chemiosmosis

A

Chemiosmosis is the movement of ions across a selectively permeable membrane, down their electrochemical gradient. More specifically, it relates to the generation of ATP by the movement of hydrogen ions across a membrane during cellular respiration or photosynthesis.

149
Q

protons being pumped across the membrane generate a _____________.

A

proton motive force as electrons move through a series of of acceptors or carriers

150
Q

How does ATP sythase ATP from ADP and inorganic phosphate?

A

Energy produced by the movement of protons back across the membrane

151
Q

where are electron carriers located in eukaryotes and in prokaryotes?

A
  • In eukaryotes the electron transport chain is located in the inner mitochondrial membrane
  • In prokaryotes electron carriers are located in the plasma membrane.
152
Q

how much ATP is produced in a Eukaryote’s mitochondrion from the complete oxidation of glucose?

A

36 ATP

153
Q

why is the amount of ATP formed in the krebs cycle in anaerobic conditions less than in areobic conditions?

A
  • the total ATP yeild in anaerobic respiration is less than in areobic respiration because only part of the Krebs cycle operates under anaerobic conditions.
154
Q

Fermentation

A

fermentation releases energy from sugars or other organic molecules by oxidation

155
Q

what is not required for fermentation?

A

O2

156
Q

during fermentation how many ATP are created by substrate level phosphorylation?

A

2 ATP

157
Q

electrons removed from the substrate reduce

A

NAD+

158
Q

in fermentation the final electron acceptor is

A

an organic molecule

159
Q

In lactic acid fermentation

A

pyruvate is is reduced by NADH to lactic acid

160
Q

in alcohol fermentation

A

acetaldehyde is reduced by NADH to produce ethanol

161
Q

Heterolactic fermenters

A

can use the pentose phosphate pathway to produce lactic acid and ethanol

162
Q

Lipases

A

hydrolyze lipids into glycerol and fatty acids

163
Q

Fatty acids and other hydrocarbons are catabolized by _____________.

A

beta-oxidation

164
Q

during lipid and protein catabolism catabolic products can

A

be further broken down in glycolysis and the krebs cycle

165
Q

what must happen to amino acids before they can become catabolized?

A

they must be converted to various substances that enter the krebs cycle.

166
Q

what reactions convert amino acids so they can be catabolized?

A
  • Transamination
  • Decarboxylation
  • Desulfurization
167
Q

Transamination

A

Most amino acids are deaminated byTransamination (or transfer of amino group), a chemical reaction that transfer their amino group to an ketoacid forming new amino acids.

168
Q

desulfurization

A

a reaction that removes sulfur

169
Q

What is a way that bacteria and yest can be identified?

A

by detecting the action of their enzymes

170
Q

Fermentation test

A

used to determine whether an organism can ferment a carbohydrate to produce acid and gas.

171
Q

Photosynthesis

A

the conversion of light energy from the sun into chemical energy ; the chemical energy is used for carbon fixation.

172
Q

Green plants, algae and cyanobacteria use

A

Chlorophyll a

173
Q

How does chlorophyll work?

A

electrons from chlorophyll pass through an electron transport chain from which ATP is formed from chemiosmosis

174
Q

Photosystems

A

are made up of chlorophyll and other pigments packed into thylakoid membranes

175
Q

during cyclic phosphorylation electrons _______

A

return to the chlorophyll

176
Q

what happens during non-cyclic phosphorylation?

A

the electrons are used to reduce NADP+ The electrons from H2O or H2S replace those lost from chlorophyll

177
Q

what happens when green plants, algae and cyanobacteria oxidize H2O?

A

O2 is produced

178
Q

What happens when sulfur bacteria oxidize hydrogen sulfide (H2S)

A

elemental sulfur granules are produced (S0)

179
Q

CO2 is used to synthesize sugars in the _____________.

A

Calvin-Benson cycle

180
Q

phototrophs

A

use sunlight to convert chemical energy in oxidation reactions carried on by phototrophs

181
Q

Chemotrophs

A

can use the chemical energy that phototrophs make

182
Q

What does a cell need to produce energy

A
  1. electron donor (organic or inorganic)
  2. a system of electron carries
  3. a final electron acceptor (organic or inorganic)
183
Q

Chemoautotrophs

A

use inorganic compounds as their energy source and carbon dioxide as their carbon source

184
Q

Chemoheterotrophs

A

use complex organic molecules as their carbon and energy source

185
Q

what is glycogen formed from?

A

ADPG

186
Q

UDPNAc

A

the starting material for the synthesis of peptidoglycan

187
Q

what are lipids sythesized from?

A

fatty acids and glycerol

188
Q

where is glycerol derived from?

A

dihydroxyacetone phosphate and fatty acids are built from acetyl CoA

189
Q

what substance(s) are required for protein biosynthesis?

A

amino acids

190
Q

all amino acids can be ___________ either directly or indirecctly from intermediates of _________________ particullarly from the ___________.

A
  • synthesized
  • carbohydrate metabolism
  • krebs cycle
191
Q

where do the sugars composing nucleotides come from?

A
  1. The pentose phosphate pathway
  2. Entner-Doudoroff pathway
192
Q

what forms the back bones of purines and pyrimidines?

A

carbon and nitrogen atoms from certain amino acids

193
Q

what are anabolic and catabolic interactions integrated through?

A

a group of common intermediates

194
Q

amphibolic

A

integrated metabolic pathways

195
Q
A
196
Q

In biological systems, the electrons are often associated with __________.

A

hydrogen atoms

197
Q

Biological oxidations are often ____________.

A

dehydrogenations

198
Q

cellular respiration uses __________ to make ATP.

A

Redox

199
Q

Substrate phoporylation

A

transfer of a high-energy PO4– to ADP

200
Q

Oxidative phosphorylation

A

transfer of electrons from one compound to another is used to generate ATP by chemiosmosis.

201
Q

Energy in a glucose molecule is stored in the ____________ between carbon atoms. EVERY TIME a bond is broken between two carbons, the shared electrons within that bond must be __________. They cannot be left to float aimlessly around the cell. Electron carrier molecules, such as _______________ accept _________and _____________(dehydrogenation) and are reduced to _________ and ________ respectively.

A
  • Covalent bonds
  • captured
  • NAD+ and FAD
  • electrons
  • protons
  • NADH
  • FADH2
202
Q

what are alternate glucose catabolism pathways for?

A

Alternative pathways are for breakdown of 5-carbon sugars or glucose to produce NADPH and may or may not occur when glycolysis is occurring.

  • pentose phosphate pathway
  • Entner-duodoroff pathway
203
Q

Transition step

A

•Transition step generates
acetyl-CoA from pyruvate (decarboxylation)

204
Q

Acetyl group of acetyl-CoA enters TCA cycle and ….

A

–Generates ATP and reducing power

–Generates precursor metabolites

205
Q

metabolite

A

a substance formed in or necessary for metabolism.

206
Q

TCA cycle

A

Citric acid is a so-called tricarboxylic acid, containing three carboxyl groups (COOH). Hence the Krebs cycle is sometimes referred to as the tricarboxylic acid (TCA) cycle.

207
Q

How the electron transport chain works

A

The process by which ATP is produced in the inner membrane of a mitochondrion: The electron transport system transfers protons from the inner compartment to the outer as electrons are passed from one protein to another. As the protons flow back to the inner compartment through ATP synthase, the energy of their movement is used to add phosphate to ADP, forming ATP.

208
Q

another name for Proton motive force (PMF)

A

proton gradient

209
Q

how does PMf generate energy during chemiosmosis?

A

•In chemiosmosis, pmf generates energy via oxidative phosphorylation

210
Q

if the final electron acceptor is nitrate (NO3-) the products will be..

A
  • Nitrogen dioxide (NO2-)
  • Nitrogen gas (N2) and H2O
211
Q

If the final electron acceptor is SO4- (sulfate) the products will be

A
  • Hydrogen sulfide (H2S) and H2O
212
Q

if the final electron acceptor is carbonate (CO32-) the products will be…

A
  • methane (CH4) and H2O
213
Q

industrial definition of fermentation

A
  • Spoilage of food by microorganisms (general use)
  • Any process that produces alcoholic beverages or acidic dairy products (general use)
  • Any large-scale microbial process occurring with or without air (common definition used in industry)
214
Q

scientific definition of fermentation

A
  • Uses an organic molecule as the final electron acceptor
  • Does not use the Krebs cycle or ETC
  • Energy yield low
  • Diversity of end products:

Ethanol, lactic acid, citric acid, methane, acetone, acetic acid, propionic acid + CO2

215
Q

how mant ATPs are produced in eukaryotes using oxygen as the final electron acceptor

A

38 ATP

216
Q

Proteins, carbohydrates, and lipids are all sources of ______________________.

A
  • electrons for cellular respiration
  • They are broken down into various small molecule components that enter cellular respiration pathways at various points
217
Q

Saprophytes

A

Saprophytes prefer dead/decaying material

218
Q

parasites

A

parasites prefer to colonize a living host

219
Q

Cellulase

A

digestion of cellulose (only bacteria and fungi have this enzyme)

220
Q

The ability to use amino acids as a source of energy is highly specific to different bacteria; different species produce different enzymes that can perform these metabolic reactions. What does the presence of certain enzymes mean?

A
  • the identity of a particular species, can be confirmed by biochemical testing.
  • The test can detect enzymes
221
Q

Phototrophs

A

get energy from light

222
Q

Chemotrophs

A

get energy from inorganic chemicals

223
Q

Heterotrophs

A

get carbon from organic molecules

224
Q

autotrophs

A

get carbon from CO2

225
Q

Chemoheterotrophs

A

•use same organic compound as energy source and carbon source. Most medically important bacteria.

226
Q

in which kingdom are all the nutritional modes found?

A

bacteria; they have a diversity of metabolic pathways

227
Q
A